For me, it's a visual process that catalyzes self-growth and change.
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Unfortunately, the narrative also catalyzes another wild swing of Serena's moral pendulum.
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Perhaps the biggest achievement of a documentary film is when it catalyzes social change.
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To an internet that catalyzes collaboration among diverse communities working together for the common good.
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But his presence catalyzes one of the tonal shifts that elevates season two above season one.
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And social media, specifically Snapchat, only catalyzes the violence, those on the frontlines told VICE News.
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Zimmer sees his automotive work as fostering the way a car catalyzes this kind of big-picture thinking.
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"Memory," however, is the show's emotional highlight, the song that catalyzes the choice of cat to ascend to heaven.
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Fertilizer runoff catalyzes the blooms, but warmer waters that come with a warmer climate make them harder to reign in.
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Antagonizing your ideological opponent is built into the ''-phobia'' frame, and activists have sparred over whether that catalyzes progress or impedes it.
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It's just a matter of time before she catalyzes Brodie, Reggie and the others to start tearing the scab off this thing.
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Then local government catalyzes these coalitions and hires recruiters to go into the world to find investors for their local communal assets.
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The kidnapping triggers something in Jefferson's older daughter, much like trauma catalyzes the mutation lying dormant in teenagers of the X-Men universe.
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Because ClassPass reduces the friction of going to a workout class, the product itself catalyzes a natural progression towards working out more frequently.
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"It catalyzes creativity, it gives you a better understanding of how to communicate with people and so exploration has the potential to feed innovation."
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But aside from the realization that catalyzes the events of the series, the story is maybe the flimsiest part of the whole series anyway.
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This could take the form of a federal matching program that supports statewide free college and catalyzes more community-based promise programs like Kalamazoo Promise.
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Heme is a great catalyst, and it catalyzes a chemical reaction in your mouth that generates the flavor and smell of blood in the raw form.
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When the leaders, the Arendellian lieutenant Matthias and the wise Northuldran leader Yelena, come together open-mindedly, it catalyzes the necessary cooperation to save the world.
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It catalyzes the perception of STDs as something that comes about when you're having more sex — a false assumption, as long as you have the right health resources.
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"Investment in urban resilience not only avoids losses but it generates value and it catalyzes growth," said Marc Forni, lead disaster risk management specialist at the World Bank.
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"Scientific research supported by the Federal Government catalyzes innovative breakthroughs that drive our economy," John Holdren, the director of the OSTP, wrote in a memorandum at the time.
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Plumbing through the deluge—songs, poems, philosophies, relationships, news, histories—we gradually hone in on our music, the stuff that strikes like lightning and catalyzes our own art.
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Because it means he understands the power of grievance, the power of rewriting history -- or the present -- to fit into a contorted ideology that catalyzes hate into political power.
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Dodge's death may open the book, but disinformation catalyzes it: a massive hoax that makes the world believe a nuclear detonation has wiped out the small town of Moab, Utah.
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Perhaps a local Mainer could also lose herself in the fury of documentary viewership-borne catharsis that catalyzes the incredible midnight bashes of CIFF (think surprise brass band barn raves).
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The liberty to move in the job market not only supports workers' choice, equality and wage growth but also creates the competition that catalyzes entrepreneurship, innovation and overall economic growth.
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In Klain's view, it's Trump's dysfunctional relationship with the government that catalyzes his illiberal tendencies — the more he is frustrated by the system, the more he will turn on the system.
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Traps are useless unless a third defender rotates over with perfect timing, and even then there'll be an open spot-up shooter in the corner after the first pass catalyzes their attack.
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Prellis achieves this by combining a light-sensitive photo-initiator with traditional bioinks that allows the cellular material to undergo a reaction when blasted with infrared light, which catalyzes the polymerization of the bioink.
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Othello is a more enigmatic figure: a Christian convert, a dark-skinned military hero, a Moor — a vague term that catalyzes fantasies and anxieties about Islam and Arabs, Africa and blackness, courage and lust.
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And you'd think it would also be good that the plotting of the story, involving the sudden appearance of a young woman with abnormal powers (Isa Briones) who catalyzes Picard's curiosity and discontent, is complicated and elliptical.
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Heme helps an Impossible Burger remain pink in the middle as it cooks, and it replicates how heme in cow muscle catalyzes the conversion of simple nutrients into the molecules that give beef its yeasty, bloody, savory flavor.
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When the injections begin, you have to continue making daily visits to the doctor for bloodwork and ultrasounds so they know when your body is ready for step two—a "trigger shot" that catalyzes the release of your eggs.
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Ultimately, trauma may not be the thing that catalyzes despair but rather the combination of trauma with gaping attachment wounds that service members feel when they separate from the tribe that had their back during their time in service.
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Cadogan, a tall, slight man with an undulating Jamaican accent and red-rimmed reading glasses, delivered to Ward's project an essay that successfully catalyzes an otherwise banal act—walking—into yet another arena where a black person must consider his body and its safety, its agency.
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We typically [buy] a controlling interest in a company, and it's such a large change in the shareholder base that it usually catalyzes a discussion of what is the right structure of management team over next five years, versus incrementally figuring out what you have and what you need.
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" But Elmes talked big, announcing "A New Funding Model for the Arts" on the Galapagos website and claiming an attempt "to reposition and stabilize the cultural business model by linking its success to the increased real estate values that the presence of artists and cultural organizations catalyzes over and over again.
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In the end, illegal speech may be the driving force that catalyzes a substantial change to Facebook's moderating processes — by providing harder red lines where it feels forced to act (even if defining what constitutes illegal speech in a particular region vs what is merely abusive and/or offensive entails another judgement challenge).
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And when you cook meat and the protein that's holding the heme unfolds, it catalyzes all the reactions, all the cooking chemistry that take simply nutrients like amino acid, sugars and fats that are present in any cell and turns them into hundreds of volatile aroma compounds that are the unmistakable taste of meat.
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But the tensions between the IRA and the British government are anything but a distant memory for his community, and when his brother's body is discovered, a decade after his mysterious disappearance, it catalyzes a long-building confrontation between the whole family about its connection to the violence of the past and the present.
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Kimmel, whose national profile soared after he delivered personal anecdotes attacking the Republican health care plan in his opening monologues, explained on the Bill Simmons Podcast why it's all Trump, all the time: From Sal Iacono, a writer for Kimmel's show: Trump's self-seriousness and incapacity to see humor in his flaws catalyzes a cycle of ridicule.
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Nick Laird's third novel, "Modern Gods," assumes the guise at various points of novels we've all read before: A man discovers he can't escape the violent deeds of his past; a woman fed up with her life is spiritually revived by a visit to a third-world guru; a family reunion catalyzes the sharing of secrets and sorting out of misunderstandings.
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Cystathionine beta synthase catalyzes the upper reaction and cystathionine gamma-lyase catalyzes the lower reaction.
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In humans, phenylalanine hydroxylase deficiency can cause phenylketonuria, the most common inborn error of amino acid metabolism. Phenylalanine hydroxylase catalyzes the conversion of to . Tyrosine hydroxylase catalyzes the rate-limiting step in catecholamine biosynthesis: the conversion of to . Similarly, tryptophan hydroxylase catalyzes the rate-limiting step in serotonin biosynthesis: the conversion of to .
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A dismutase is an enzyme that catalyzes a dismutation reaction.
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They are classified as oxidoreductase enzymes that catalyzes an electron transfer.
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Ph2S2 catalyzes the cis-trans isomerization of alkenes under UV-irradiation.
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Both of these substances are degraded to form homovanillic acid (HVA). Both degradations involve the enzymes monoamine oxidase (MAO) and catechol-O-methyl transferase (COMT), albeit in reverse order: MAO catalyzes dopamine to DOPAC, and COMT catalyzes DOPAC to HVA; whereas COMT catalyzes dopamine to 3-MT and MAO catalyzes 3-MT to HVA. The third metabolic end-product of dopamine is norepinephrine (noradrenaline). DOPAC can be oxidized by hydrogen peroxide, leading to the formation of toxic metabolites which destroy dopamine storage vesicles in the substantia nigra.
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In enzymology, a NADH kinase () is an enzyme that catalyzes a chemical reaction.
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This number is specific to the enzyme itself, not just the reaction it catalyzes.
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Dipyridamole also inhibits the enzyme adenosine deaminase, the enzyme that catalyzes the breakdown of adenosine.
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The enzyme catalyzes the conversion of 4-coumaroyl-CoA and malonyl-CoA to naringenin chalcone.
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As well as its primary role in folate metabolism, SHMT also catalyzes other reactions that may be biologically significant, including the conversion of 5,10-Methenyltetrahydrofolate to 10-Formyltetrahydrofolate. When coupled with C1-tetrahydrofolate synthase and tetrahydropteroate, cSHMT also catalyzes the conversion of formate to serine.
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In enzymology, a tRNA nucleotidyltransferase () is an enzyme that catalyzes the chemical reaction :tRNAn+1 \+ phosphate \rightleftharpoons tRNAn \+ a nucleoside diphosphate where tRNA-N is a product of transcription, and tRNA Nucleotidyltransferase catalyzes this cytidine-cytidine-adenosine (CCA) addition to form the tRNA-NCCA product.
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The IIC domain catalyzes the transfer of a phosphoryl group from IIB to the sugar substrate.
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It has 2 cofactors: FAD, and Iron. A similar enzyme in plants catalyzes non-acetylated polyamines.
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1.5) catalyzes the conversion of methylglyoxal and reduced glutathione to S-D-lactoyl-glutathione. Glyoxalase II (EC 3.1.2.6) catalyzes the hydrolysis of S-D-lactoyl-glutathione to glutathione and D-lactic acid. It maintains exogenous antioxidants such as vitamins C and E in their reduced (active) states.
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This gene encodes the alpha subunit of the mitochondrial trifunctional protein, which catalyzes the last three steps of mitochondrial beta-oxidation of long chain fatty acids. The enzyme converts medium- and long-chain 2-enoyl- CoA compounds into the following 3-ketoacyl-CoA when NAD is solely present, and acetyl-CoA when NAD and CoASH are present. The alpha subunit catalyzes this reaction, and is attached to HADHB, which catalyzes the last step of the reaction.
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The enzyme quercitrinase catalyzes the chemical reaction between quercitrin and H2O to yield L-rhamnose and quercetin.
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In electrical insulator plastics it suppresses arcing and tracking. In halogen-containing systems, zinc borate is used together with antimony trioxide and alumina trihydrate. It catalyzes formation of char and creates a protective layer of glass. Zinc catalyzes the release of halogens by forming zinc halides and zinc oxyhalides.
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In the presence of PII, which is encoded by glnB, NRII catalyzes the dephosphorylation of NRI–P. The nitrogen content in the cell is directly proportional to the ratio of concentration of glutamine to the concentration of 2-ketoglutarate. When nitrogen content is lower, the product of glnD gene, uridylyl transferase catalyzes the conversion of PII to give PII-UMP, hampering PII’s ability of dephosphoryating NRI–P. Uridylyl transferase catalyzes this reaction because the high concentration of 2-ketoglutarate allosterically activates it.
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Acyl-CoA:monoacylglycerol acyltransferase (MOGAT; EC 2.3.1.22) catalyzes the synthesis of diacylglycerol from 2-monoacylglycerol and fatty acyl-CoA.
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Xylylene dichloride is used as a vulcanizing agent to harden rubbers. It catalyzes the crosslinking of phenolic resins.
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Proposed mechanism of lactose hydrolysis by Lactase enzyme Lactase also catalyzes the conversion of phlorizin to phloretin and glucose.
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Gluthione- S-transferase is an enzyme that catalyzes a detoxification process involving a conjugation of gluthione into xenobiotic substrates.
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Cysteine synthesis from serine. Cystathionine beta synthase catalyzes the upper reaction and cystathionine gamma-lyase catalyzes the lower reaction. Serine is important in metabolism in that it participates in the biosynthesis of purines and pyrimidines. It is the precursor to several amino acids including glycine and cysteine, as well as tryptophan in bacteria.
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Ribonucleotide reductase (RNR), also known as ribonucleotide diphosphate reductase (rNDP), is an enzyme that catalyzes the formation of deoxyribonucleotides from ribonucleotides. It catalyzes this formation by removing the 2'-hydroxyl group of the ribose ring of nucleoside diphosphates. This reduction produces deoxyribonucleotides. Deoxyribonucleotides in turn are used in the synthesis of DNA.
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Squalene epoxidase also catalyzes the formation of diepoxysqualene (DOS). DOS is converted to 24(S),25-epoxylanosterol by lanosterol synthase.
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Cycloartenol synthase () (2,3-epoxysqualene-cycloartenol cyclase) is a plant enzyme that catalyzes the cyclization of (S)-2,3-epoxysqualene to cycloartenol.
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This is a skeletal structure of the reaction that MenB catalyzes. It was originally thought that the product of this reaction had an oxygen where the SCoA currently resides, however; new research has shown that MenB only catalyzes the above reaction. There is a different enzyme that cleaves the SCoA and attaches the oxygen.
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Salicylate synthase is an enzyme that catalyzes the chemical reaction: :chorismate → salicylic acid MbtI is the responsible enzyme from Mycobacterium tuberculosis.
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Aurones are biosynthesized starting from coumaryl-CoA. Aureusidin synthase catalyzes the creation of aurones from chalcones through hydroxylation and oxidative cyclization.
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Ultimately, Nin helps Miller to publish his novel, Tropic of Cancer, but catalyzes the Millers' separation, while she returns to Hugo.
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C-5 sterol desaturase catalyzes an intermediate step in the synthesis of major sterols. The particular biosynthetic pathway varies across eukaryotes. In animals C5SD catalyzes the dehydration of lathosterol to 7-dehydrocholesterol, a step in the synthesis of cholesterol. Cholesterol serves multiple roles in the cell including modulating membrane fluidity serving as a precursor to steroid hormones.
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Cysteine synthesis: Cystathionine beta synthase catalyzes the upper reaction and cystathionine gamma-lyase catalyzes the lower reaction. In animals, biosynthesis begins with the amino acid serine. The sulfur is derived from methionine, which is converted to homocysteine through the intermediate S-adenosylmethionine. Cystathionine beta-synthase then combines homocysteine and serine to form the asymmetrical thioether cystathionine.
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Finally, SBPase is subject to negative feedback regulation by sedoheptulose-7-phosphate and inorganic phosphate, the products of the reaction it catalyzes.
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A third release factor RF-3 catalyzes the release of RF-1 and RF-2 at the end of the termination process.
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Based on different protein structures and mechanisms of catalysis, there are 3 different types of radical SAM (RS) methylases: Class A, B, and C. Class A RS methylases are the best characterized of the 4 enzymes and are related to both RlmN and Cfr. RlmN is ubiquitous in bacteria which enhances translational fidelity and RlmN catalyzes methylation of C2 of adenosine 2503 (A2503) in 23 S rRNA and C2 of adenosine (A37). Cfr, on the other hand, catalyzes methylation of C8 of A2503 as well and it also catalyzes C2 methylation. Class B is currently the largest class of radical SAM methylases which can mathylate both sp2-hybridized and sp3-hybridized carbon atoms in different sets of substrates unlike Class A which only catalyzes sp2-hybridized carbon atoms.
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With HCl, it gives RhCl2(C2H2)2−. Rh2Cl2(C2H4)4 catalyzes the dimerization of ethylene to 1-butene. Carbonylation affords rhodium carbonyl chloride.
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The enzyme L-cysteate sulfo- lyase catalyzes this conversion. Cysteate is not a biosynthetic precursor to taurine, which is derived from cysteine sulfinate.
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Similar to copper, iron is both essential as protein cofactor but also dangerous as ferreous iron catalyzes the formation of reactive oxygen species.
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In fungi C5SD catalyzes the dehydration of episterol as a step in the synthesis of ergosterol, a sterol that regulates cell membrane fluidity and permeability. In plants such as Arabidopsis thaliana, C-5 sterol desaturase catalyzes the dehydrogenation of episterol and avenasterol in a pathway thought to lead to a variety of membrane components as well as a class of hormones called brassinosteroids.
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Aldehyde oxidase (AO) is a metabolizing enzyme, located in the cytosolic compartment of tissues in many organisms. AO catalyzes the oxidation of aldehydes into carboxylic acid, and in addition, catalyzes the hydroxylation of some heterocycles. It can also catalyze the oxidation of both cytochrome P450 (CYP450) and monoamine oxidase (MAO) intermediate products. AO plays an important role in the metabolism of several drugs.
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While all PRMT enzymes catalyze the methylation of arginine residues in proteins, PRMT1 is unique in that is catalyzes the formation of asymmetrically dimethylated arginine as opposed to the PRMT2 that catalyzes the formation of symmetrically dimethylated arginine. Individual PRMT utilize S-adenosyl-L- methionine (SAM) as the methyl donor and catalyze methyl group transfer to the ω-nitrogen of an arginine residue.
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It catalyzes the following reaction, the second step of the biosynthesis of porphyrin: :2 δ-aminolevulinic acid \rightleftharpoons porphobilinogen + 2 H2O It therefore catalyzes the condensation of 2 molecules of delta-aminolevulinate to form porphobilinogen (a precursor of heme, cytochromes and other hemoproteins). This reaction is the first common step in the biosynthesis of all biological tetrapyrroles. Zinc is essential for enzymatic activity.
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After binding to calmodulin, cyaA–ACD catalyzes the cyclization of AMP into cAMP. This catalysis raises the intracellular concentration of cAMP to toxic levels.
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Nitrospira also carry the genes encoding for all the sub-units of nitrite oxidoreductase (nxr), the enzyme that catalyzes the second step of nitrification.
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T7 RNA Polymerase is an RNA polymerase from the T7 bacteriophage that catalyzes the formation of RNA from DNA in the 5'→ 3' direction.
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This drug is a reversible inhibitor of the enzyme glucosylceramide synthase, which catalyzes the first step in synthesizing glucose-based glycosphingolipids like GM2 ganglioside.
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Formimidoyltransferase cyclodeaminase or formiminotransferase cyclodeaminase (symbol FTCD in humans) is an enzyme that catalyzes the conversion of formiminoglutamate and tetrahydrofolate into formiminotetrahydrofolate and glutamate.
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Isochorismate synthase (EC number 5.4.4.2) is an isomerase enzyme that catalyzes the first step in the biosynthesis of vitamin K2 (menaquinone) in Escherichia coli.
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Xylanase catalyzes the catabolism of xylan into xylose. Given that plants contain a lot of xylan, xylanase is thus important to the nutrient cycle.
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In biochemistry, cis-trans isomerase is a type of isomerase which catalyzes the isomerization of geometric isomers. Examples include photoisomerase and immunophilins such as cyclophilin.
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Superactivity in PRPS1, the enzyme that catalyzes the R5P to PRPP, has also been linked to gout, as well as neurodevelopmental impairment and sensorineural deafness.
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It catalyzes the following reaction: acetyl-CoA + beta-D-galactoside → CoA + 6-acetyl-beta- D-galactoside The kinetics of the enzyme were delineated in 1995.
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In enzymology, an EST is an enzyme that catalyzes the following chemical reaction: :3'-phosphoadenylyl sulfate + estrone \rightleftharpoons adenosine 3',5'-bisphosphate + estrone 3-sulfate Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and estrone, whereas its two products are adenosine 3',5'-bisphosphate and estrone 3-sulfate. The enzyme also catalyzes the same reaction for estradiol, with estradiol sulfate as the product.
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5'-deoxyadenosine deaminase (also known as "DadD") is an enzyme that catalyzes the conversion of 5′-deoxyadenosine to 5′-deoxyinosine. To a lesser extent, the enzyme also catalyzes the deamination of 5′-methylthioadenosine, S-adenosylhomocysteine, and adenosine. The molecular mass of the DadD enzyme is approximately 230 kDa. DadD maintains 90% of its enzymatic activity after being heated at 60 degrees Celsius for ten minutes.
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This gene encodes one of two enzymes which catalyzes the final reaction in the synthesis of triglycerides in which diacylglycerol is covalently bound to long chain fatty acyl-CoAs. The encoded protein catalyzes this reaction at low concentrations of magnesium chloride while the other enzyme has high activity at high concentrations of magnesium chloride. Multiple transcript variants encoding different isoforms have been found for this gene.
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IPL catalyzes the decomposition of isochorismate into salicylate and pyruvate Isochorismate lyase's only substrate is isochorismate. It catalyzes the elimination of the enolpyruvyl side chain from isochorismate to make salicylate, a precursor to the siderophore pyochelin. Believed to be a pericyclic reaction, the enzyme's transition state, when transferring a hydrogen from C2 to C9, is cyclic. Its bond breaking and subsequent formation are conjoint processes.
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The DXP-independent PLP-biosynthetic route consists of a step catalyzed by PLP-synthase, an enzyme composed of two subunits. PdxS catalyzes the condensation of ribulose 5-phosphate, glyceraldehyde-3-phosphate, and ammonia, this latter molecules is produced by PdxT which catalyzes the production of ammonia from glutamine. PdxS is a (β/α)8 barrel (also known as a TIM-barrel) that forms a dodecamer.
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The Leloir pathway catalyzes the conversion of galactose to glucose. Galactose is found in dairy products, as well as in fruits and vegetables, and can be produced endogenously in the breakdown of glycoproteins and glycolipids. Three enzymes are required in the Leloir pathway: galactokinase, galactose-1-phosphate uridylyltransferase, and UDP-galactose 4-epimerase. Galactokinase catalyzes the first committed step of galactose catabolism, forming galactose 1-phosphate.
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By far the most common use of isomerases in industrial applications is in sugar manufacturing. Glucose isomerase (also known as xylose isomerase) catalyzes the conversion of D-xylose and D-glucose to D-xylulose and D-fructose. Like most sugar isomerases, glucose isomerase catalyzes the interconversion of aldoses and ketoses. The conversion of glucose to fructose is a key component of high-fructose corn syrup production.
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Research SignPost, Trivandrum, India. 2005. Chapter 4, pp. 99–147. Additionally, List et al. have published a chiral Brønsted acid that catalyzes asymmetric Pictet–Spengler reactions.
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O-GlcNAc transferase also catalyzes the posttranslational modification that modifies transcription factors and RNA polymerase II, however the specific function of this modification is mostly unknown.
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This gene encodes a cytosolic enzyme which catalyzes the hydrolysis of peptides and proteins with mannose modifications to produce free oligosaccharides. [provided by RefSeq, Feb 2012].
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This upregulation of GRK2 is also accompanied by upregulation and increased production of the enzyme tyrosine hydroxylase, which catalyzes the rate limiting step of catecholamine synthesis.
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3-hydroxyisobutyrate dehydrogenase is a tetrameric mitochondrial enzyme that catalyzes the NAD+-dependent, reversible oxidation of 3-hydroxyisobutyrate, an intermediate of valine catabolism, to methylmalonate semialdehyde.
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This enzyme is mainly found in Artemisia annua, a temperate Asian native flowering plant, and ADS catalyzes the first committed step in the antimalarial drug artemisinin synthesis.
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Evolutionary conserved protein domain corresponding to oxidoreductase activity. NAD binding catalyzes redox reactions to alter the oxidation state of metal ions, using NADP+ as an electron acceptor.
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The enzyme formylmethanofuran:tetrahydromethanopterin formyltransferase catalyzes the transfer of the formyl group from formylmethanofuran to N5 on tetrahydromethanopterin, . This enzyme has been crystallized; it contains no prosthetic group.
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This gene encodes a gluconeogenesis regulatory enzyme which catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate. [provided by RefSeq, Jul 2008].
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CYP27C1 catalyzes 3,4-desaturation of retinoids, particularly all-trans-retinol (vitamin A1) to all-trans 3,4-dehydroretinal (vitamin A2). The enzyme is unusual among mammalian P450s in that the predominant oxidation is a desaturation and in that hydroxylation represents only a minor pathway - the enzyme catalyzes 3- and 4-hydroxylation as minor events. The enzyme is located in human skin epidermis. The function of the enzyme was only discovered in 2016.
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After its synthesis, cardiolipin cannot exert its proper functions until it is actively remodeled. Tafazzin, an acyl-specific transferase, catalyzes the acyl transfer reaction between phospholipids and lysophospholipids in a CoA- independent manner. The remodeling process of cardiolipin involves reaching a final acyl composition that is primarily linoleoyl residues. TAZ interacts with an immature cardiolipin by adding the fatty acid linoleic acid, which catalyzes the remodeling of the cardiolipin.
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It is formed by the reaction of 1,4-benzoquinone with hydrogen peroxide and is a byproduct of the metabolism of phenols, such as 1,2,4-benzenetriol. The enzyme 1,2,4-benzenetriol dehydrogenase catalyzes the conversion of 1,2,4-benzenetriol to 2-hydroxy-1,4-benzoquinone, and the enzyme hydroxybenzoquinone reductase catalyzes the reverse reaction. The enzyme 2-hydroxy-1,4-benzoquinone-2-reductase converts it to 1,4-benzoquinone. It tends to dimerize spontaneously by peroxo bridges.
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The product of this gene transfers fucose to N-acetyllactosamine polysaccharides to generate fucosylated carbohydrate structures. It catalyzes the synthesis of the non-sialylated antigen, Lewis x (CD15).
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Beta-glucosidase is an enzyme that catalyzes the hydrolysis of the glycosidic bonds to terminal non-reducing residues in beta-D-glucosides and oligosaccharides, with release of glucose.
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Methionine-R-sulfoxide reductase B2, mitochondrial is an enzyme that in humans is encoded by the MSRB2 gene. The MRSB2 enzyme catalyzes the reduction of methionine sulfoxide to methionine.
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It catalyzes the reaction of turning L-arogenate into L-phenylalanine.Jung; Zamir; Jensen. "Chloroplasts of higher plants synthesize L-phenylalanine via L-arogenate". Proc. Nati. Acad. Sci. USA. 83.
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DNA ligase III along with its cofactor XRCC1 catalyzes the nick-sealing step in short-patch BER in humans. DNA ligase I ligates the break in long-patch BER.
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This gene encodes the enzyme that catalyzes adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme. Alternatively spliced transcript variants encoding distinct isoforms have been observed.
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Platinum, a chemically similar catalyst, catalyzes dehydrogenation of five- and six-member cyclic hydrocarbons into benzene. The d-bands of ruthenium lie higher than those in platinum, generally predicting stronger ruthenium–adsorbate bonds than on platinum. Therefore, it is likely that ruthenium also catalyzes dehydrogenation of five- and six-member hydrocarbon rings to benzene. Benzene dehydrogenates further on ruthenium surfaces into hydrocarbon fragments similar to those formed by acetylene and ethene on ruthenium surfaces.
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The AT of module 4 loads methylmalonyl-CoA onto the module 4 ACP and catalyzes a Claisen condensation with the bound tetraketide. However, since module 4 contains an inactive KR domain, the β-ketone condensation product is maintained. The AT on module 5 selects for ethylmalonyl-CoA and catalyzes a Claisen condensation followed by reduction via the KR and dehydration via the DH resulting in an alkene. The ER then saturates the alkene product.
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2,4 Dienoyl-CoA reductase also known as DECR1 is an enzyme which in humans is encoded by the DECR1 gene which resides on chromosome 8. This enzyme catalyzes the following reactions File:Dienoyl-CoA reductase reaction cis-trans.svg DECR1 participates in the beta oxidation and metabolism of polyunsaturated fatty enoyl-CoA esters. Specifically, it catalyzes the reduction of 2,4 dienoyl-CoA thioesters of varying length by NADPH cofactor to 3-trans-enoyl- CoA of equivalent length.
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The GDP-L-colitose biosynthesis pathway. For clarity, groups modified by the previous enzymatic step are highlighted in yellow. The biosynthesis of colitose begins with ColE, a mannose-1-phosphate guanylyltransferase that catalyzes the addition of a GMP moiety to mannose, yielding GDP-mannose. In the next step, ColB, an NADP- dependent short-chain dehydrogenase-reductase enzyme, catalyzes the oxidation at C-4 and the removal of the hydroxyl group at C-6.
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GART catalyzes the third step in de novo purine biosynthesis, the formation of N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide (fGAR) by formyl addition to N1-(5-phospho-D-ribosyl)glycinamide (GAR). In E. coli, the purN enzyme is a 23 kDa protein but in humans it is part of a trifunctional protein of 110 kDa which includes AIRS and GARS functionalities. This protein catalyzes three different steps of the de novo purine pathway.
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Aldolase B plays a key role in carbohydrate metabolism as it catalyzes one of the major steps of the glycolytic- gluconeogenic pathway. Though it does catalyze the breakdown of glucose, it plays a particularly important role in fructose metabolism, which occurs mostly in the liver, renal cortex, and small intestinal mucosa. When fructose is absorbed, it is phosphorylated by fructokinase to form fructose 1-phosphate. Aldolase B then catalyzes F1P breakdown into glyceraldehyde and DHAP.
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In enzymology, a guanylate kinase () is an enzyme that catalyzes the chemical reaction :ATP + GMP \rightleftharpoons ADP + GDP Thus, the two substrates of this enzyme are ATP and GMP, whereas its two products are ADP and GDP. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. This enzyme participates in purine metabolism. Guanylate kinase catalyzes the ATP-dependent phosphorylation of GMP into GDP.
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Dehydrodolichyl diphosphate (dedol-PP) synthase catalyzes cis-prenyl chain elongation to produce the polyprenyl backbone of dolichol, a glycosyl carrier lipid required for the biosynthesis of several classes of glycoproteins.
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The reproduction mechanism of a typical viroid. Leaf contact transmits the viroid. The viroid enters the cell via its plasmodesmata. RNA polymerase II catalyzes rolling- circle synthesis of new viroids.
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Alpha amylase from B. amyloliquefaciens is often used in starch hydrolysis. It is also a source of subtilisin, which catalyzes the breakdown of proteins in a similar way to trypsin.
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In fireflies, an enzyme in the abdomen catalyzes a reaction that results in bioluminescence. Many significant photochemical reactions, such as ozone formation, occur in the Earth atmosphere and constitute atmospheric chemistry.
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Animal lung phosphatidylcholine, for example, contains a high proportion of dipalmitoylphosphatidylcholine. Phospholipase D catalyzes the hydrolysis of phosphatidylcholine to form phosphatidic acid (PA), releasing the soluble choline headgroup into the cytosol.
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Glutamate dehydrogenase 2 is localized to the mitochondrion and acts as a homohexamer to recycle glutamate during neurotransmission. The encoded enzyme catalyzes the reversible oxidative deamination of glutamate to alpha- ketoglutarate.
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This meeting catalyzes the most horrific event in human history. All involved are left wondering what they have done, and why. Meanwhile, Dr. Zeus seems to go from strength to strength.
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In contrast to these systems, the cationic zirconocene complex [Cp2ZrOC6H4P(tBu)2]+ effectively catalyzes the reaction, with the most notable example being the dehydrogenation of dimethylamineborane in 10min at room temperature.
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Complex IV, a multimeric protein complex that requires several assembly factors, catalyzes the transfer of reducing equivalents from cytochrome c to molecular oxygen and pumps protons across the inner mitochondrial membrane.
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Flavin-containing monooxygenase 3 (FMO3), also known as dimethylaniline monooxygenase [N-oxide-forming] 3 and trimethylamine monooxygenase, is a flavoprotein enzyme () that in humans is encoded by the FMO3 gene. This enzyme catalyzes the following chemical reaction: :trimethylamine + NADPH + H+ \+ O2 \rightleftharpoons trimethylamine N-oxide + NADP+ \+ H2O FMO3 is the main flavin-containing monooxygenase isoenzyme that is expressed in the liver of adult humans. The human FMO3 enzyme catalyzes several types of reactions, including: the of primary, secondary, and tertiary amines; the of nucleophilic sulfur-containing compounds; and the of DMXAA. FMO3 is the primary enzyme in humans which catalyzes the N-oxidation of trimethylamine into trimethylamine N-oxide; FMO1 also N-oxygenates trimethylamine, but to a much lesser extent than FMO3.
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In yeasts, galactose oxidase catalyzes the following reaction: :D-galactose + O2 \rightleftharpoons D-galacto-hexodialdose + H2O2 This reaction is essentially the oxidation of primary alcohol using dioxygen to form the corresponding aldehyde and hydrogen peroxide. It has been shown that galactose oxidase is also able to catalyze various primary alcohols other than galactose. In fact, galactose oxidase catalyzes dihydroxyacetone three times faster than it does to galactose. The reaction is regioselective, in that it cannot oxidize secondary alcohol.
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Second, an endoprotease that recognizes the farnesylated protein catalyzes cleavage of the peptide bond between the cysteine and -aaX. In the third step, isoprenylcysteine carboxyl methyltransferase catalyzes methylation of the carboxyl-terminal farnesylcysteine. The farnesylated and methylated protein is transported through a nuclear pore to the interior of the nucleus. Once in the nucleus, the protein is cleaved by a protease called zinc metallopeptidase STE24 (ZMPSTE24), which removes the last 15 amino acids, which includes the farnesylated cysteine.
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Squalene monooxygenase (also called squalene epoxidase) is an enzyme that uses NADPH and molecular oxygen to oxidize squalene to 2,3-oxidosqualene (squalene epoxide). Squalene epoxidase catalyzes the first oxygenation step in sterol biosynthesis and is thought to be one of the rate-limiting enzymes in this pathway. In humans, squalene epoxidase is encoded by the SQLE gene. Several eukaryote genomes lack a squalene monooxygenase encoding gene, but instead encode an alternative squalene epoxidase that catalyzes the oxidation of squalene.
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While most members of the POT family catalyze peptide transport, one is a nitrate permease and one can transport histidine, as well as peptides. Some of the peptide transporters can also transport antibiotics. They function by proton symport, but the substrate:H+ stoichiometry is variable: the high- affinity rat PepT2 carrier catalyzes uptake of 2 and 3 H+ with neutral and anionic dipeptides, respectively, while the low affinity PepT1 carrier catalyzes uptake of one H+ per neutral peptide.
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The encoded protein (PHC) catalyzes the transport of phosphate from the cytosol into the mitochondrial matrix, either by proton cotransport or in exchange for hydroxyl ions. In the final steps of oxidative phosphorylation, this protein catalyzes the uptake of a phosphate ion with a proton across the mitochondrial inner membrane. The availability of inorganic phosphate for oxidative phosphorylation is mainly dependent on PHC activity. To substantially affect oxidative phosphorylation, PHC depletion must be severe, exceeding 85%.
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Fe(acac)3 has been examined as a precatalyst and reagent in organic chemistry, although the active iron-containing species is usually unidentified in these processes. In one instance, Fe(acac)3 was shown to promote cross-coupling a diene to an olefin. Fe(acac)3 catalyzes the dimerization of isoprene to a mixture of 1,5-dimethyl-1,5-cyclooctadiene and 2,5-dimethyl-1,5-cyclooctadiene. : Fe(acac)3 also catalyzes the ring-opening polymerization of 1,3-benzoxazine.
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Glutamate-Prephanate Aminotransferase catalyzes the reversible reaction shown below: The enzyme catalyzes the reaction above, an important step in the synthesis of phenylalanine, tyrosine, and tryptophan. From left to right, the species involved are L-arogenate, 2-oxoglutarate, prephenate, and L-glutamate. Glutamate-Prephenate Aminotransferase Reaction, and its primary purpose is to convert prephenate into arogenate via transamination, using glutamate as the amino donor. As stated previously, the left side of the reaction is strongly favored.
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Genome sequencing of M. hakonensis has revealed the presence of genes coding for enzyme Urease, with genes present for subunits A and B. Urease catalyzes the degradation of urea to ammonia and bicarbonate. Sequences also revealed the presence of genes for haloacetate dehalogenase. Haloacetate dehalogenase catalyzes the conversion of haloacetate to glycolate and the halide ion(e.g. fluoride). M. hakonensis also contains the gene for maleylacetate reductase, a key component in biological degradation of halogenated aromatic organic compounds.
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The biosynthesis of aspartate is frequently involves the transamination of oxaloacetate. The enzyme aspartokinase, which catalyzes the phosphorylation of aspartate and initiates its conversion into other amino acids, can be broken up into 3 isozymes, AK-I, II and III. AK-I is feed-back inhibited by threonine, while AK-II and III are inhibited by lysine. As a sidenote, AK-III catalyzes the phosphorylation of aspartic acid that is the committed step in this biosynthetic pathway.
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Cis- prenyltransferases include dehydrodolichol diphosphate synthase (involved in the production of a precursor to dolichol). The beta subunit of the farnesyltransferases is responsible for peptide binding. Squalene-hopene cyclase is a bacterial enzyme that catalyzes the cyclization of squalene into hopene, a key step in hopanoid (triterpenoid) metabolism. Lanosterol synthase () (oxidosqualene-lanosterol cyclase) catalyzes the cyclization of (S)-2,3-epoxysqualene to lanosterol, the initial precursor of cholesterol, steroid hormones and vitamin D in vertebrates and of ergosterol in fungi.
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Mtb IDH-1 is most structurally similar to the R132H mutant human IDH found in certain glioblastomas. Similar to human R132H ICDH, Mtb ICDH-1 also catalyzes the formation of α-hydroxyglutarate.
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2,3-bisphosphoglycerate is required a cofactor for dPGM. In contrast, the iPGM class is independent of 2,3-bisphosphoglycerate and catalyzes the intramolecular transfer of the phosphate group on monophosphoglycerates using a phosphoserineintermediate.
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The Cyp11a2 is a fish gene encoding a CYP450 monooxygenase, which was originally identified in Zebrafish (Danio rerio), is the isozyme and paralogous of fish CYP11A1, catalyzes conversion of cholesterol to pregnenolone.
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BLVRB binds to human heme oxygenase-1 (hHO-1) in conjunction with cytochrome p450 reductase to catalyzes the NADPH-cytochrome P450 reductase-dependent oxidation of heme to biliverdin, CO, and free iron.
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This gene encodes a subunit of the tRNA splicing endonuclease complex, which catalyzes the removal of introns from precursor tRNAs. The complex is also implicated in pre-mRNA 3-prime end processing.
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Bismuth chloride is used as a catalyst in organic synthesis. In particular, it catalyzes the Michael reaction and the Mukaiyama aldol reaction. The addition of other metal iodides increases its catalytic activity.
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Fructose-1,6-bisphosphatase 1, a gluconeogenesis regulatory enzyme, catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate. Fructose-1,6-diphosphatase deficiency is associated with hypoglycemia and metabolic acidosis.
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Protein O-GlcNAc transferase also known as OGT is an enzyme () that in humans is encoded by the OGT gene. OGT catalyzes the addition of the O-GlcNAc post- translational modification to proteins.
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The product of this gene transfers fucose to N-acetyllactosamine polysaccharides to generate fucosylated carbohydrate structures. It catalyzes the synthesis of the non-sialylated antigen, Lewis x (CD15). [provided by RefSeq, Jan 2009].
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A novel peptidyl-prolyl cis/trans isomerase from Escherichia coli. FEBS Lett 343:65. is the smallest known protein with prolyl isomerase activity, which catalyzes the cis-trans isomerization of proline peptide bonds.
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Sodium nitroprusside, a metabolite of which is thiocyanate, is however still used for the treatment of a hypertensive emergency. Rhodanese catalyzes the reaction of sodium nitroprusside with thiosulfate to form the metabolite thiocyanate.
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This enzyme is also called 5-O-(1-carboxyvinyl)-3-phosphoshikimate phosphate-lyase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis. Chorismate synthase catalyzes the last of the seven steps in the shikimate pathway which is used in prokaryotes, fungi and plants for the biosynthesis of aromatic amino acids. It catalyzes the 1,4-trans elimination of the phosphate group from 5-enolpyruvylshikimate-3-phosphate (EPSP) to form chorismate which can then be used in phenylalanine, tyrosine or tryptophan biosynthesis.
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Estrone sulfotransferase (EST) (), also known as estrogen sulfotransferase, is an enzyme that catalyzes the transformation of an unconjugated estrogen like estrone into a sulfated estrogen like estrone sulfate. It is a steroid sulfotransferase and belongs to the family of transferases, to be specific, the sulfotransferases, which transfer sulfur-containing groups. This enzyme participates in androgen and estrogen metabolism and sulfur metabolism. Steroid sulfatase is an enzyme that catalyzes the reverse reaction, the transfer of a sulfate to an unconjugated estrogen.
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In lipids, lipases contribute to the breakdown of fats and lipoproteins and other larger molecules into smaller molecules like fatty acids and glycerol. Fatty acids and other small molecules are used for synthesis and as a source of energy. In biochemistry, a hydrolase is an enzyme that catalyzes the hydrolysis of a chemical bond. For example, any enzyme that catalyzes the following reaction is a hydrolase: :A-B + H2O -> A-OH + B-H where A-B represents a chemical bond of unspecified molecules.
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Conversion by IPP isomerase Isopentenyl-diphosphate delta isomerase type I (also known as IPP isomerase) is seen in cholesterol synthesis and in particular it catalyzes the conversion of isopentenyl diphosphate (IPP) to dimethylallyl diphosphate (DMAPP). In this isomerization reaction a stable carbon-carbon double bond is rearranged top create a highly electrophilic allylic isomer. IPP isomerase catalyzes this reaction by the stereoselective antarafacial transposition of a single proton. The double bond is protonated at C4 to form a tertiary carbocation intermediate at C3.
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Alcohol dehydrogenase [NADP+] also known as aldehyde reductase or aldo-keto reductase family 1 member A1 is an enzyme that in humans is encoded by the AKR1A1 gene. AKR1A1 belongs to the aldo-keto reductase (AKR) superfamily. It catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols and catalyzes the reduction of mevaldate to mevalonic acid and of glyceraldehyde to glycerol. Mutations in the AKR1A1 gene has been found associated with non-Hodgkin's lymphoma.
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Aminocyclopropane-1-carboxylic acid synthase (ACC synthase, ACS) () is an enzyme that catalyzes the synthesis of 1-Aminocyclopropane-1-carboxylic acid (ACC), a precursor for ethylene, from S-Adenosyl methionine (AdoMet, SAM), an intermediate in the Yang cycle and activated methyl cycle and a useful molecule for methyl transfer. ACC synthase, like other PLP dependent enzymes, catalyzes the reaction through a quinonoid zwitterion intermediate and uses cofactor pyridoxal phosphate (PLP, the active form of vitamin B6) for stabilization. In enzymology, a 1-aminocyclopropane-1-carboxylate synthase is an enzyme that catalyzes the chemical reaction :S-adenosyl-L-methionine \rightleftharpoons 1-aminocyclopropane-1-carboxylate + methylthioadenosine Hence, this enzyme has one substrate, S-adenosyl-L-methionine, and two products, 1-aminocyclopropane-1-carboxylate and methylthioadenosine. This enzyme belongs to the family of lyases, specifically carbon-sulfur lyases.
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The enzyme glucose oxidase (GOx) converts glucose into gluconic acid and hydrogen peroxide while consuming oxygen. Another enzyme, peroxidase, catalyzes a chromogenic reaction (Trinder reaction) of phenol with 4-aminoantipyrine to a purple dye.
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This gene encodes a component of the U5 small nuclear ribonucleoprotein (snRNP) particle. The U5 snRNP is part of the spliceosome, a multiprotein complex that catalyzes the removal of introns from pre-messenger RNAs.
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The archaeon Sulfolobus solfataricus RadA recombinase catalyzes DNA pairing and strand exchange, central steps in recombinational repair. The RadA recombinase has greater similarity to the eukaryotic Rad51 recombinase than to the bacterial RecA recombinase.
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Both subunits contain dozens of ribosomal proteins arranged on a scaffold composed of ribosomal RNA (rRNA). The small subunit monitors the complementarity between tRNA anticodon and mRNA, while the large subunit catalyzes peptide bond formation.
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DNA topoisomerase 1 is an enzyme that in humans is encoded by the TOP1 gene. It is a DNA topoisomerase, an enzyme that catalyzes the transient breaking and rejoining of a single strand of DNA.
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The phosphatidic acid is also a precursor for triglyceride biosynthesis. Phosphatidic acid phosphotase catalyzes the conversion of phosphatidic acid to diacylglyceride, which will be converted to triacylglyceride by acyltransferase. Tryglyceride biosynthesis occurs in the cytosol.
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Yeast pyruvate kinase () Pyruvate kinase enzyme catalyzes the last step of glycolysis, in which pyruvate and ATP are formed. Pyruvate kinase catalyzes the transfer of a phosphate group from phosphoenolpyruvate (PEP) to ADP, yielding one molecule of pyruvate and one molecule of ATP. Liver pyruvate kinase is indirectly regulated by epinephrine and glucagon, through protein kinase A. This protein kinase phosphorylates liver pyruvate kinase to deactivate it. Muscle pyruvate kinase is not inhibited by epinephrine activation of protein kinase A. Glucagon signals fasting (no glucose available).
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Tn5 and most other transposases contain a DDE motif, which is the active site that catalyzes the movement of the transposon. Aspartate-97, Aspartate-188, and Glutamate-326 make up the active site, which is a triad of acidic residues. The DDE motif is said to coordinate divalent metal ions, most often magnesium and manganese, which are important in the catalytic reaction. Because transposase is incredibly inactive, the DDE region is mutated so that the transposase becomes hyperactive and catalyzes the movement of the transposon.
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The protein encoded by AMT catalyzes the release of ammonia and the transfer of a methylene carbon unit to a tetrahydrofolate moiety. The aminomethyl intermediate is the product of the decarboxylation of glycine catalyzed by P-protein. In the reverse reaction, T-protein catalyzes the formation of the H-protein-bound aminomethyl lipoate intermediate from 5,10-CH2-H4folate, ammonia, and reduced H-protein via an ordered Ter Bi mechanism, in which reduced H-protein is the first substrate to bind followed by 5,10-CH2-H4folate and ammonia.
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While OGT catalyzes the addition of O-GlcNAc to serine and threonine, OGA catalyzes the hydrolytic cleavage of O-GlcNAc from post- transitionally modified proteins. OGA is a member of the family of hexosaminidases. However, unlike lysosomal hexosaminidases, OGA activity is the highest at neutral pH (approximately 7) and it localizes mainly to the cytosol. OGA and OGT are synthesized from two conserved genes (OGA is encoded by MGEA5) and are expressed throughout the human body with high levels in the brain and pancreas.
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The enzyme aspartate aminotransferase catalyzes the transfer of an amino group from aspartate onto α-ketoglutarate to yield glutamate and oxaloacetate. Asparagine is synthesized by an ATP- dependent addition of an amino group onto aspartate; asparagine synthetase catalyzes the addition of nitrogen from glutamine or soluble ammonia to aspartate to yield asparagine. The diaminopimelic acid lysine biosynthetic pathway The diaminopimelic acid biosynthetic pathway of lysine belongs to the aspartate family of amino acids. This pathway involves nine enzyme-catalyzed reactions that convert aspartate to lysine.
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4-Hydroxyphenylpyruvate dioxygenase (HPPD), also known as α-ketoisocaproate dioxygenase (KIC dioxygenase), is an Fe(II)-containing non-heme oxygenase that catalyzes the second reaction in the catabolism of tyrosine - the conversion of 4-hydroxyphenylpyruvate into homogentisate. HPPD also catalyzes the conversion of phenylpyruvate to 2-hydroxyphenylacetate and the conversion of α-ketoisocaproate to β-hydroxy β-methylbutyrate. HPPD is an enzyme that is found in nearly all aerobic forms of life. This reaction shows the conversion of 4-hydroxyphenylpyruvate into homogentisate by HPPD.
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Lysophosphatidylcholine acyltransferase 1 is a protein in humans that is encoded by the LPCAT1 gene. Lysophosphatidylcholine (LPC) acyltransferase (LPCAT; EC 2.3.1.23) catalyzes the conversion of LPC to phosphatidylcholine (PC) in the remodeling pathway of PC biosynthesis.
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This gene encodes an enzyme (cob(I)yrinic acid a,c-diamide adenosyltransferase) that catalyzes the final step in the conversion of vitamin B12 into adenosylcobalamin (AdoCbl), a vitamin B12-containing coenzyme for methylmalonyl-CoA mutase.
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Ambrein is synthesized from common triterpenoid precursor squalene. The Squalene-hopene cyclase(SHC) catalyzes cyclization of squalene into the monocyclic 3-deoxyachilleol A. Tetraprenyl-beta-curcumene synthase(BmeTC) converts 3-deoxyachilleol A into the tricyclic ambrein.
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For example, cannabidiolic acid (CBDA) synthase is a flavoprotein that catalyzes a similar oxidative cyclization of CPGA into CBDA, the dominant cannabinoid constituent of fiber-type C. sativa. CBDA undergoes a similar decarboxylation to form cannabidiol.
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Several other enzymes have been described later, including HMFO. This flavin dependent oxidase catalyzes the three consecutive oxidations to form FDCA from HMF.W.P. Dijkman, D.E. Groothuis, M.W. Fraaije. Angew. Chem. Int. Ed. 2014, 53: 6515-6518.
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However, the Joint Commission on Biochemical Nomenclature (JCBN) dictates that 'synthase' can be used with any enzyme that catalyzes synthesis (whether or not it uses nucleoside triphosphates), whereas 'synthetase' is to be used synonymously with 'ligase'.
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A model for a proposed 2-Site Ping-Pong mechanism of Tyrosine Sulfation A model for a proposed SN2-like In-Line Displacement mechanism of Tyrosine Sulfation Tyrosylprotein sulfotransferase is an enzyme that catalyzes tyrosine sulfation.
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50S includes the activity that catalyzes peptide bond formation (peptidyl transfer reaction), prevents premature polypeptide hydrolysis, provides a binding site for the G-protein factors (assists initiation, elongation, and termination), and helps protein folding after synthesis.
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More specifically, it catalyzes the direct exchange of a hydrogen atom with its isotopes deuterium and tritium, without the use of an intermediate. It has been shown that isotope exchange with Crabtree’s catalyst is highly regioselective.
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Fuculose or 6-deoxy-tagatose is a ketohexose deoxy sugar. Fuculose is involved in the process of sugar metabolism. It is both a human and Escherichia coli metabolite and catalyzes the production of dihydroxyacetone phosphate(DHAP).
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Biosynthesis of pyocyanin from Pseudomonas aeruginosa. Hydrogens abstracted during next enzymatic step colored red. Pyocyanin biosynthesis begins with the synthesis of the phenazine-1-carboxylic acid (PCA) core. In this reaction the enzyme PhzE catalyzes the loss of the hydroxyl group from C4 of Chorismic Acid as well as the transfer of an amine group from glutamine to form glutamic acid and 2-amino-2-desoxyisochorismic acid (ADIC). Following this, PhzD catalyzes the hydrolytic removal the pyruvate moiety from ADIC to form (5S,6S)-6-amino-5-hydroxy-1,3-cyclohexadieve-1-carboxylic acid (DHHA). In the next step, PhzF catalyzes two steps: the abstraction of a hydrogen from C3 of DHHA, delocalization of the double bond system and reprotonation at C1 as well as enol tautomerization to form the highly unstable 6-amino-5-oxocyclohex-2-ene-1-carboxylic acid (AOCHC).
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In enzymology, a thiosulfate sulfurtransferase () is an enzyme that catalyzes the chemical reaction :thiosulfate + cyanide \rightleftharpoons sulfite + thiocyanate Thus, the two substrates of this enzyme are thiosulfate and cyanide, whereas its two products are sulfite and thiocyanate.
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Soluble guanylate cyclase (sGC), a heterodimeric protein consisting of an alpha and a beta subunit, catalyzes the conversion of GTP to the second messenger cGMP and functions as the main receptor for nitric oxide and nitrovasodilator drugs.
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This ubiquitin protein ligase recognizes which protein needs to be tagged and catalyzes the transfer of ubiquitin to that protein. This pathway repeats itself until the target protein has a full chain of ubiquitin attached to itself.
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Oxygen catalyzes the pyrolysis of polymers at low concentration and initiates oxidation at high concentration. Transition concentrations are different for different polymers. (e.g., polypropylene, between 5% and 15%). Additionally, polymers exhibit a structural-dependent relationship with oxygen.
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It is caused by abnormalities in the gene coding for uridine diphosphoglucuronate glucuronosyltransferase (UGT1A1). UGT1A1 normally catalyzes the conjugation of bilirubin and glucuronic acid within hepatocytes. Conjugated bilirubin is more water soluble and is excreted in bile.
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Ribonuclease H1 also known as RNase H1 is an enzyme that in humans is encoded by the RNASEH1 gene. The RNase H1 is a non-specific endonuclease and catalyzes the cleavage of RNA via a hydrolytic mechanism.
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CNPase catalyzes the following reaction: :nucleoside 2',3'-cyclic phosphate + H2O \rightleftharpoons nucleoside 2'-phosphate Thus, the two substrates of this enzyme are nucleoside 2',3'-cyclic phosphate and H2O, whereas its product is nucleoside 2'-phosphate.
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This enzyme catalyzes the reduction of progesterone to the inactive form 20-alpha-hydroxy-progesterone. This gene shares high sequence identity with three other gene members, and is clustered with those three genes at chromosome 10p15-p14.
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Histidine decarboxylase (HDC) is the enzyme that catalyzes the reaction which produces histamine from histidine. Measurement of histidine carboxylase in the marrow cells of patients with mast cell leukemia is a very sensitive marker of mast cells.
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Adenylyl cyclase catalyzes the conversion of ATP to cAMP. cAMP binds to protein kinase A, and the complex phosphorylates phosphorylase kinase. Phosphorylated phosphorylase kinase phosphorylates phosphorylase. Phosphorylated phosphorylase clips glucose units from glycogen as glucose 1-phosphate.
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Aldose reductase catalyzes the NADPH-dependent conversion of glucose to sorbitol, the first step in polyol pathway of glucose metabolism. The second and last step in the pathway is catalyzed by sorbitol dehydrogenase, which catalyzes the NAD-linked oxidation of sorbitol to fructose. Thus, the polyol pathway results in conversion of glucose to fructose with stoichiometric utilization of NADPH and production of NADH. ;glucose + NADPH + H+ \rightleftharpoons sorbitol + NADP+ Galactose is also a substrate for the polyol pathway, but the corresponding keto sugar is not produced because sorbitol dehydrogenase is incapable of oxidizing galactitol.
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Diphosphomevalonate decarboxylase (), most commonly referred to in scientific literature as mevalonate diphosphate decarboxylase, is an enzyme that catalyzes the chemical reaction :ATP + (R)-5-diphosphomevalonate \rightleftharpoons ADP + phosphate + isopentenyl diphosphate + CO2 This enzyme converts mevalonate 5-diphosphate (MVAPP) to isopentenyl diphosphate (IPP) through ATP dependent decarboxylation. The two substrates of this enzyme are ATP and mevalonate 5-diphosphate, whereas its 4 products are ADP, phosphate, isopentenyl diphosphate, and CO2. Mevalonate diphosphate decarboxylase catalyzes the final step in the mevalonate pathway. The mevalonate pathway is responsible for the biosynthesis of isoprenoids from acetate.
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Human steroidogenesis, showing 21-α hydroxylase at upper center, with pathways to aldosterone and cortisol at right, and pathways to androgens at left. The enzyme P450c21, commonly referred to as 21-hydroxylase (21-OH), is embedded in the smooth endoplasmic reticulum of the cells of the adrenal cortex. It catalyzes hydroxylation of 17α-hydroxyprogesterone (17OHP) to 11-deoxycortisol in the glucocorticoid pathway, which starts from pregnenolone and finishes with cortisol. It also catalyzes hydroxylation of progesterone to 11-deoxycorticosterone (DOC) in the mineralocorticoid pathway on its way from pregnenolone to aldosterone.
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APRTase catalyzes the following reaction in the purine nucleotide salvage pathway: Adenine + Phosphoribosyl Pyrophosphate (PRPP) → Adenylate (AMP) + Pyrophosphate (PPi) ARPTase catalyzes a phosphoribosyl transfer from PRPP to adenine, forming AMP and releasing pyrophosphate (PPi). In organisms that can synthesize purines de novo, the nucleotide salvage pathway provides an alternative that is energetically more efficient. It can salvage adenine from the polyamine biosynthetic pathway or from dietary sources of purines. Although APRTase is functionally redundant in these organisms, it becomes more important during periods of rapid growth, such as embryogenesis and tumor growth.
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On the other hand, it catalyzes the oxidation of alkanes to tertiary alcohols, amides to t-butyldioxyamides, and tertiary amines to α-(t-butyldioxyamides) using tert-butyl hydroperoxide. Using other peroxides, oxygen, and acetone, the catalyst can oxidize alcohols to aldehydes or ketones. Using dichlorotris(triphenylphosphine)ruthenium(II) the N-alkylation of amines with alcohols is also possible (see "borrowing hydrogen"). :650px RuCl2(PPh3)3 efficiently catalyzes carbon-carbon bond formation from cross couplings of alcohols through C-H activation of sp3 carbons in the presence of a Lewis acid.
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Reaction catalyzed by lactate dehydrogenase Lactate dehydrogenase catalyzes the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+. It converts pyruvate, the final product of glycolysis, to lactate when oxygen is absent or in short supply, and it performs the reverse reaction during the Cori cycle in the liver. At high concentrations of lactate, the enzyme exhibits feedback inhibition, and the rate of conversion of pyruvate to lactate is decreased. It also catalyzes the dehydrogenation of 2-hydroxybutyrate, but it is a much poorer substrate than lactate.
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In enzymology, a polynucleotide 5'-hydroxyl-kinase () is an enzyme that catalyzes the chemical reaction :ATP + 5'-dephospho-DNA \rightleftharpoons ADP + 5'-phospho-DNA Thus, the two substrates of this enzyme are ATP and 5'-dephospho-DNA, whereas its two products are ADP and 5'-phospho-DNA. Polynucleotide kinase is a T7 bacteriophage (or T4 bacteriophage) enzyme that catalyzes the transfer of a gamma-phosphate from ATP to the free hydroxyl end of the 5' DNA or RNA. The resulting product could be used to end-label DNA or RNA, or in a ligation reactions..
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Lecithin retinol acyltransferase is a microsomal enzyme that catalyzes the esterification of all-trans-retinol into all-trans- retinyl ester during phototransduction, an essential reaction for the retinoid cycle in visual system and vitamin A status in liver.
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EF-G (elongation factor G, historically known as translocase) is a prokaryotic elongation factor involved in protein translation. As a GTPase, EF-G catalyzes the movement (translocation) of transfer RNA (tRNA) and messenger RNA (mRNA) through the ribosome.
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As a peptidase, this protein catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoding DIABLO protein.
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Besides hydrogenation, the catalyst catalyzes the isomerization and hydroboration of alkenes. An example of isomerization with Crabtree's catalyst. The reaction proceeds 98% to completion in 30 minutes at room temperature. Crabtree's catalyst is used in isotope exchange reactions.
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This gene encodes adenylyl cyclase 3, which is a membrane-associated enzyme and catalyzes the formation of the secondary messenger cyclic adenosine monophosphate (cAMP). The ADCY3 subtype likely mediates odorant detection (possibly) via modulation of intracellular cAMP concentration.
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It can allow people to conquer their fears and negative emotions. Ibogaine catalyzes an altered state of consciousness reminiscent of dreaming while fully conscious and aware so that memories, life experiences, and issues of trauma can be processed.
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Nucleoside diphosphate (NDP) kinase catalyzes in vivo ATP-dependent synthesis of ribo- and deoxyribonucleoside triphosphates. In mutated Escherichia coli that had a disrupted nucleoside diphosphate kinase, adenylate kinase performed dual enzymatic functions. ADK complements nucleoside diphosphate kinase deficiency.
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In enzymology, an acylphosphatase () is an enzyme that catalyzes the following chemical reaction: The chemical reaction catalyzed by acylphosphatase enzymes. Thus, the two substrates of this enzyme are acylphosphate and H2O, whereas its two products are carboxylate and phosphate.
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Acetyl-CoA synthetase (ACS) or Acetate-CoA ligase is an enzyme () involved in metabolism of acetate. It is in the ligase class of enzymes, meaning that it catalyzes the formation of a new chemical bond between two large molecules.
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This isoform of 17β-HSD is expressed predominantly in the testis and catalyzes the conversion of androstenedione to testosterone. It preferentially uses NADP as cofactor. Deficiency can result in impaired virilization of genetically male infants, formerly termed male pseudohermaphroditism.
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In enzymology, a 4-hydroxy-2-oxovalerate aldolase () is an enzyme that catalyzes the chemical reaction :4-hydroxy-2-oxopentanoate \rightleftharpoons acetaldehyde + pyruvate Hence, this enzyme has one substrate, 4-hydroxy-2-oxopentanoate, and two products, acetaldehyde and pyruvate.
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In the penultimate step, N-terminal G domain adenylate the apo form of the molybdopterin to form the intermediate adenylated molybdopterin. In the terminal step, the C-terminal E domain catalyzes the deadenylation and also the metal insertion mechanism.
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Phosphatidylinositol transfer protein beta isoform is a protein that in humans is encoded by the PITPNB gene. The protein encoded by this gene is found in the cytoplasm, where it catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes.
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Once the second Serine is phosphorylated, Ser2, elongation is activated. In order to terminate elongation dephosphorylation must occur. Once the domain is completely dephosphorylated the RNAP II enzyme is "recycled" and catalyzes the same process with another initiation site.
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ERG4 or Delta(24(24(1)))-sterol reductase or Delta(24(28))-sterol reductase is a enzyme that catalyzes the last step of ergosterol biosynthesis pathway in fungi Saccharomyces cerevisiae (Baker's yeast), which 5,7,22,24(28)-ergostatetraenol converted into ergosterol.
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Cytochrome P450 family 107 subfamily G member 1 (abbreviated CYP107G1) is a Actinobacteria Cytochrome P450 enzyme originally from Streptomyces rapamycinicus, which catalyzes the oxidation reaction of C27 of pre-rapamycin in the biosynthesis pathway of the macrolide antibiotic rapamycin.
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1.95), serC (EC 2.6.1.52), and serB (EC 3.1.3.3).Uniprot: serB Serine biosynthesis Glycine biosynthesis: Serine hydroxymethyltransferase (SHMT = serine transhydroxymethylase) also catalyzes the reversible conversions of L-serine to glycine (retro-aldol cleavage) and 5,6,7,8-tetrahydrofolate to 5,10-methylenetetrahydrofolate (mTHF) (hydrolysis).
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In effect, the reaction accelerates itself or is autocatalyzed. An example is the hydrolysis of an ester such as aspirin to a carboxylic acid and an alcohol. In the absence of added acid catalysts, the carboxylic acid product catalyzes the hydrolysis.
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In enzymology, a 3-mercaptopyruvate sulfurtransferase () is an enzyme that catalyzes the chemical reactions of 3-mercaptopyruvate. This enzyme belongs to the family of transferases, specifically the sulfurtransferases. This enzyme participates in cysteine metabolism. It is encoded by the MPST gene.
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The excess of EDTA is back- titrated with a suitable metal ion such as Mn2+ or Cu2+. At the endpoint, the first excess of metal ion catalyzes a strongly exothermic reaction between a polyhdric phenol (such as resorcinol) and hydrogen peroxide.
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Diagram showing glycolytic and gluconeogenic pathways. Note that phosphoglycerate kinase is used in both directions. PGK is present in all living organisms as one of the two ATP-generating enzymes in glycolysis. In the gluconeogenic pathway, PGK catalyzes the reverse reaction.
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Dopamine beta-hydroxylase catalyzes the hydroxylation of not only dopamine but also other phenylethylamine derivatives when available. The minimum requirement seems to be the phenylethylamine skeleton: a benzene ring with a two-carbon side chain that terminates in an amino group.
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Glyceraldehyde-3-phosphate dehydrogenase (NADP+) catalyzes :GAP + NADP+ \+ H2O → 3-PG + NADPH + H+ Glyceraldehyde-3-phosphate dehydrogenase and phosphoglycerate kinase catalyze :GAP + NAD+ \+ Pi 1,3-bisphosphoglycerate + NADH + H+ :1,3-bisphosphoglycerate + ADP 3-PG + ATP Usually [NADPH] / [NADP+] >> 1 >> [NADH] / [NAD+].
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The enzyme ornithine decarboxylase (ODC) catalyzes the decarboxylation of ornithine (a product of the urea cycle) to form putrescine. This reaction is the committed step in polyamine synthesis. In humans, this protein has 461 amino acids and forms a homodimer.
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Tryptophanyl-tRNA synthetase (WARS) catalyzes the aminoacylation of tRNA(trp) with tryptophan and is induced by interferon. Tryptophanyl-tRNA synthetase belongs to the class I tRNA synthetase family. Four transcript variants encoding two different isoforms have been found for this gene.
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In enzymology, a threo-3-hydroxyaspartate ammonia-lyase () is an enzyme that catalyzes the chemical reaction :threo-3-hydroxy-L-aspartate \rightleftharpoons oxaloacetate + NH3 Hence, this enzyme has one substrate, threo-3-hydroxy-L-aspartate, and two products, oxaloacetate and NH3.
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Prostaglandin-F synthase (PGFS) catalyzes the formation of 9α,11β-PGF2α,β from PGD2 and PGF2α from PGH2 in the presence of NADPH. This enzyme has recently been crystallized in complex with PGD2 and bimatoprost (a synthetic analogue of PGF2α).
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Sepiapterin reductase (7,8-dihydrobiopterin:NADP+ oxidoreductase; EC 1.1.1.153) catalyzes the NADPH-dependent reduction of various carbonyl substances, including derivatives of pteridines, and belongs to a group of enzymes called aldo-keto reductases. SPR plays an important role in the biosynthesis of tetrahydrobiopterin.
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Iodotyrosine deiodinase catalyzes mono- and diiodotyrosine deiodination. The reaction is NADPH-dependent. Flavin mononucleotide (FMN) is a cofactor. Although flavin is commonly utilized in various catalytic reactions, its use in this reductive dehalogenation is unique and not yet fully understood.
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3-Nitrooxypropanol, abbreviated 3NOP, is an organic compound with the formula HOCH2CH2CH2ONO2. It is the mononitrate ester of 1,3-propanediol. The compound is an inhibitor of the enzyme methyl coenzyme M reductase (MCR). MCR catalyzes the final step in methanogenesis.
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It is formed by the reaction of indium(III) oxide with hydrogen fluoride or hydrofluoric acid. Indium(III) fluoride is used in the synthesis of non-oxide glasses. It catalyzes the addition of trimethylsilyl cyanide (TMSCN) to aldehydes to form cyanohydrins.
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Adenylosuccinate lyase deficiency, is a rare autosomal recessive metabolic disorder characterized by the appearance of succinylaminoimidazolecarboxamide riboside (SAICA riboside) and succinyladenosine (S-Ado) in cerebrospinal fluid, urine. These two succinylpurines are the dephosphorylated derivatives of SAICA ribotide (SAICAR) and adenylosuccinate (S-AMP), the two substrates of adenylosuccinate lyase (ADSL), which catalyzes an important reaction in the de novo pathway of purine biosynthesis. ADSL catalyzes two distinct reactions in the synthesis of purine nucleotides, both of which involve the β-elimination of fumarate to produce aminoimidazole carboxamide ribotide (AICAR) from SAICAR or adenosine monophosphate (AMP) from S-AMP.
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Ammonia (NH3) is a toxic substance for many aerobic organisms and must be excreted. Some aquatic organisms release the toxin right directly into their environment, while other ureotelic species must convert their toxic nitrogen waste into non-toxic components, like uric acid or urea, through a series of catalyzed steps better known as the urea cycle. ASL catalyzes the fourth step in the cycle, following the action of argininosuccinate synthetase (ASS) in the liver cytosol. While ASS catalyzes the formation of argininosuccinate from citrulline and aspartate, ASL breaks the newly formed argininosuccinate into L-arginine and fumarate.
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After glycogen phosphorylase catalyzes the phosphorolytic cleavage of a glucosyl residue from the glycogen polymer, the freed glucose has a phosphate group on its 1-carbon. This glucose 1-phosphate molecule is not itself a useful metabolic intermediate, but phosphoglucomutase catalyzes the conversion of this glucose 1-phosphate to glucose 6-phosphate (see below for the mechanism of this reaction). Glucose 6-phosphate’s metabolic fate depends on the needs of the cell at the time it is generated. If the cell is low on energy, then glucose 6-phosphate will travel down the glycolytic pathway, eventually yielding two molecules of adenosine triphosphate.
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Five missense mutations (A287P, R457H, V492E, C569Y, and V608F) and a splicing mutation in the POR genes have been found in patients who had hormonal evidence for combined deficiencies of two steroidogenic cytochrome P450 enzymes - P450c17 CYP17A1, which catalyzes steroid 17α-hydroxylation and 17,20 lyase reaction, and P450c21 21-Hydroxylase, which catalyzes steroid 21-hydroxylation. Another POR missense mutation Y181D has also been identified. Fifteen of nineteen patients having abnormal genitalia and disordered steroidogenesis were homozygous or apparent compound heterozygous for POR mutations that destroyed or dramatically inhibited POR activity. More than 200 variations in POR gene have been identified.
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In the final step of phenazine-1-carboxylic acid synthesis the enzyme PhzG catalyzes the oxidation of THPCA to dihydro-phenazine-1-carboxylic acid. This is the last catalyzed step in the production of PCA, the last step is an uncatalyzed oxidation of DHPCA to PCA. The conversion of PCA to Pyocyanin is achieved in two enzymatic steps: firstly, PCA is methylated on N5 to 5-methylphenazine-1-carboxylate betaine by the enzyme PhzM using the cofactor S-adenosyl-L-methionine and secondly, PhzS catalyzes the hydroxylative decarboxylation of this substrate to form the final product, Pyocyanin.
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In enzymology, a dihydropyrimidine dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction :5,6-dihydrouracil + NADP+ \rightleftharpoons uracil + NADPH + H+ Thus, the two substrates of this enzyme are 5,6-dihydrouracil and NADP+, whereas its 3 products are uracil, NADPH, and H+. In humans the enzyme is encoded by the DPYD gene. It is the initial and rate- limiting step in pyrimidine catabolism. It catalyzes the reduction of uracil and thymine. It is also involved in the degradation of the chemotherapeutic drugs 5-fluorouracil and tegafur.. It also participates in beta-alanine metabolism and pantothenate and coa biosynthesis.
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In enzymology, a glyceollin synthase is an enzyme that catalyzes the last committed step in glyceollin biosynthesis. This enzyme has been classified as a cytochrome dependent monooxygenase. It uses cyclization of prenyl residue to convert glyceollidins (I and II) into glyceollins (I - III). This enzyme catalyzes the following chemical reaction: :2-(or 4-)dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan + NADPH + H+ \+ O2 \rightleftharpoons glyceollin + NADP+ \+ 2 H2O The five substrates of this enzyme are 2-dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan, 4-dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan, NADPH, H+, and O2, whereas its three products are glyceollin, NADP+, and H2O.
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Using information from Escherichia coli derived asparagine synthetase, some basic mechanisms of the enzyme have been understood. The N-terminal active site catalyzes glutamine hydrolysis to yield glutamate and ammonia. The C-terminal active site catalyzes activation of the side-chain carboxylate of aspartate to form an electrophilic intermediate, β-aspartyl-AMP (βAspAMP) 1, and inorganic pyrophosphate (PPi). The tunnel that links the two active sites allows for the passage of an ammonia molecule to act as a common intermediate to couple the two half-reactions carried out in the independent active sites of the enzyme.
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In prokaryotes, the order is inverted, and the acylation substrate is rather D-Glucosamide-1-phosphate, and a single enzyme catalyzes both the carbon transfer as well as the UTP binding, generating directly UDP-GlcNAc (UDP-N- Acetyl-D-Glucosamide). Picture reproduced from. More specifically, the GNA enzyme catalyzes the fourth step of the HBP pathway in eukaryotes, promoting a carbon transfer from Acetyl-CoA to the other substrate, D-Glucosamine-6-phosphate which will finally yield UDP-N-Acetylglucosamine. This is a small, but an important chemical step that is crucial to the properties of the sub-products of this metabolic pathway.
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Trichotriol reacts in a non-enzymatic cyclization reaction to its isomere isotrichodermol. In the reaction the hydroxyl group on the C2 of the cyclopentane binds to the C11 of the cyclohexene forming a tetrahydropyran ring. The shifted OH-group at C9 is lost during the reaction. An acetyltransferase (encoded by TRI101) catalyzes the acetylation of the C3 OH-group of isotrichodermol forming isotrichdermin. Isotrichodermin is converted to 15-decalonecitrin due to a substitution (encoded by TRI11) of one hydrogen by one hydroxyl at C15 which is then acetylated under help of TRI3. The same substitution and following acetylation reactions occur at C4 again under the control of TRI13 and TRI7. TRI1 in F.sporotrichiodies further catalyzes the addition of a fourth OH-group at C8 and a fifth OH-group at C7 at which then the hydrogen is eliminated and a keto group forms. In a last step an esterase controlled by TRI8 catalyzes the deacetylation at C3, C4 and C15 resulting in the end product nivalenol.
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Module 6 loads methylmalonyl CoA onto the ACP and catalyzes a Claisen condensation followed by a β-keto reduction by the KR domain. The heptaketide product is then passed to the KS on module 7 on TylGV via paired docking domains on TylGIV.
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Lp-PLA2 is platelet-activating factor (PAF) acetylhydrolase (EC 3.1.1.47), a secreted enzyme that catalyzes the degradation of PAF to inactive products by hydrolysis of the acetyl group at the sn-2 position, producing the biologically inactive products LYSO-PAF and acetate.
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This region is usually very thermodynamically stable and occurs only in the phospholipid membrane between cells. The intracellular domain is the serine/threonine kinase domain. In this domain, phosphorylation catalyzes a protein kinase cascade leading to a response.Shiu, S.H., and Bleecker, A.B. (2001).
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In humans, uric acid is the final step in the catabolic pathway of purines. Rasburicase catalyzes enzymatic oxidation of poorly soluble uric acid into an inactive and more soluble metabolite allantoin with carbon dioxide and hydrogen peroxide as byproducts in the chemical reaction.
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This gene product is a component of the ribonucleoprotein complex responsible for telomerase activity which catalyzes the addition of new telomeres on the chromosome ends. The telomerase- associated proteins are conserved from ciliates to humans. It is also a minor vault protein.
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IMP dehydrogenase 1 acts as a homotetramer to regulate cell growth. IMPDH1 is an enzyme that catalyzes the synthesis of xanthine monophosphate (XMP) from inosine-5'-monophosphate (IMP). This is the rate-limiting step in the de novo synthesis of guanine nucleotides.
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Additionally, HBr catalyzes many organic reactions.Hercouet, A.; LeCorre, M. (1988) Triphenylphosphonium bromide: A convenient and quantitative source of gaseous hydrogen bromide. Synthesis, 157–158.Greenwood, N. N.; Earnshaw, A. Chemistry of the Elements; Butterworth-Heineman: Oxford, Great Britain; 1997; pp. 809–812.
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The BorJ gene product, a PMP- dependent transaminase, then introduces an amine into the polyketide, generating intermediate Borrelidin B. BorI then catalyzes the conversion of the amine to an N,N-dihydroxy species and the dehydration to form borrelidin via an aldoxime intermediate.
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NiCl2(dppp) in an effective catalyst for coupling reactions such as the Kumada coupling and Suzuki reactions (example below). It also catalyzes other reactions that convert enol ethers, dithioacetals, and vinyl sulfides to olefins.Tien-Yau Luh; Tien-Min Yuan. "Cross-Coupling Reactions".
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In vitro, the ISWI protein alone can assemble nucleosomes on linear DNA and it can move nucleosomes on linear DNA from the center to the extremities. Inside the CHRAC complex, ISWI catalyzes the inverse reaction, moving nucleosomes from the extremities to the center.
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The enzyme horseradish peroxidase (HRP), found in the roots of horseradish, is used extensively in biochemistry applications. It is a metalloenzyme with many isoforms, of which the most studied type is C. It catalyzes the oxidation of various organic substrates by hydrogen peroxide.
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In enzymology, a tryptophan 2'-dioxygenase () is an enzyme that catalyzes the chemical reaction 350px L-tryptophan + + \rightleftharpoons (indol-3-yl)glycolaldehyde + + Thus, the 3 substrates of this enzyme are L-tryptophan, and , whereas its 3 products are (indol-3-yl)glycolaldehyde, , and .
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In enzymology, a L-ascorbate oxidase () is an enzyme that catalyzes the chemical reaction :2 L-ascorbate + O2 \rightleftharpoons 2 dehydroascorbate + 2 H2O Thus, the two substrates of this enzyme are L-ascorbate and O2, whereas its two products are dehydroascorbate and H2O.
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In enzymology, a nicotinate dehydrogenase () is an enzyme that catalyzes the chemical reaction 400px nicotinate + H2O + NADP+ \rightleftharpoons 6-hydroxynicotinate + NADPH + H+ The 3 substrates of this enzyme are nicotinate, H2O, and NADP+, whereas its 3 products are 6-hydroxynicotinate, NADPH, and H+.
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Nonessential amino acids are produced in the body. The pathways for the synthesis of nonessential amino acids are quite simple. Glutamate dehydrogenase catalyzes the reductive amination of α-ketoglutarate to glutamate. A transamination reaction takes place in the synthesis of most amino acids.
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Illustration of a GPCR signaling protein. In response to a molecule such as a hormone binding to the exterior domain (blue) the GPCR changes shape and catalyzes a chemical reaction on the interior domain (red). The gray feature is the surrounding bilayer.
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Ehrmann is the President of the InSideOut Initiative, an evidenced-based, systems-level approach that inspires and catalyzes communities to transform the current “win-at-all-costs” interscholastic sports culture to one that values the human growth and development of student-athletes.
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Uridine monophosphate (UMP)/cytidine monophosphate (CMP) kinase (EC 2.7.4.4) catalyzes the phosphoryl transfer from ATP to UMP, CMP, and deoxy-CMP (dCMP), resulting in the formation of ADP and the corresponding nucleoside diphosphate. These nucleoside diphosphates are required for cellular nucleic acid synthesis.
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The conversion of phe to tyr is catalyzed by the enzyme phenylalanine hydroxylase, a monooxygenase. This enzyme catalyzes the reaction causing the addition of a hydroxyl group to the end of the 6-carbon aromatic ring of phenylalanine, such that it becomes tyrosine.
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This variant of testosterone 17beta- dehydrogenase () catalyzes the reaction :testosterone + NAD+ \rightleftharpoons androst-4-ene-3,17-dione + NADH + H+ Thus, the two substrates of this enzyme are testosterone and NAD+, whereas its 3 products are androst-4-ene-3,17-dione, NADH, and H+.
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This variant of testosterone 17beta-dehydrogenase () catalyzes the reaction :testosterone + NADP+ \rightleftharpoons androst-4-ene-3,17-dione + NADPH + H+ Thus, the two substrates of this enzyme are testosterone and NADP+, whereas its 3 products are androst-4-ene-3,17-dione, NADPH, and H+.
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In enzymology, a diacylglycerol cholinephosphotransferase () is an enzyme that catalyzes the chemical reaction 400px CDP-choline + 1,2-diacylglycerol \rightleftharpoons CMP + a phosphatidylcholine Thus, the two substrates of this enzyme are CDP-choline and 1,2-diacylglycerol, whereas its two products are CMP and phosphatidylcholine.
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Lathosterol oxidase is an enzyme that in humans is encoded by the SC5DL gene. This gene encodes an enzyme of cholesterol biosynthesis. The encoded protein catalyzes the conversion of lathosterol into 7-dehydrocholesterol. Mutations in this gene have been associated with lathosterolosis.
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Cu(acac)2 is prepared by treating acetylacetone with aqueous . It is available commercially, catalyzes coupling and carbene transfer reactions. :150x150px Unlike the copper(II) derivative, copper(I) acetylacetonate is an air-sensitive oligomeric species. It is employed to catalyze Michael additions.
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Sirohydrochlorin is a tetrapyrrole macrocyclic metabolic intermediate in the biosynthesis of sirohaem, the iron-containing prosthetic group in sulfite reductase enzymes. It is also the biosynthetic precursor to cofactor F430, an enzyme which catalyzes the release of methane in the final step of methanogenesis.
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The conjugate acid [HP(MeNCH2CH2)3N]+ has a pKa of 32.9 in acetonitrile. For comparison, the conjugate acid of triethylamine has a pKa's near 17 in acetonitrile. Owing to its ability to deprotonate weak carbon acids, the Verkade base catalyzes a variety of condensation reactions.
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Thiamine-triphosphatase is an enzyme involved in thiamine metabolism. It catalyzes the chemical reaction :thiamine triphosphate + H2O \rightleftharpoons thiamine diphosphate + phosphate This enzyme belongs to the family of acid anhydride hydrolases, specifically those acting on phosphorus- containing anhydrides. Its systematic name is thiamine triphosphate phosphohydrolase.
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The enzyme monomethylamine methyltransferase catalyzes the reaction of monomethylamine to methane. This enzyme includes pyrrolysine. The unusual amino acid is inserted using a unique tRNA, the anticodon of which is UAG. In most organisms, and in most Methanosarcinaceae proteins, UAG is a stop codon.
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Adenylate cyclase catalyzes the conversion of adenosine triphosphate into cAMP, which is a second messenger, thereby increasing the intracellular cAMP levels, resulting in relaxation of smooth muscles. cAMP levels are regulated through the activity of phosphodiesterase isozymes/isoforms, which degrades it to 5′-AMP.
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Chvostek's sign is found in tetany. However, it may also be present in hypomagnesemia. Magnesium is a cofactor for adenylate cyclase, which catalyzes the conversion of ATP to 3',5'-cyclic AMP. The 3',5'-cyclic AMP (cAMP) is required for parathyroid hormone activation.
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The enzyme from the pathogenic fungus Aspergillus fumigatus catalyzes a step in the biosynthesis of the siderophores triacetylfusarinine and desferriferricrocin, while the enzyme from the bacterium Kutzneria 744 is involved in the biosynthesis of piperazate, a building block of the kutzneride family of antifungal antibiotics.
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Fructose-bisphosphate aldolase [EC 4.1.2.13] catalyzes a key reaction in glycolysis and energy production and is produced by all four species. The P.falciparum aldolase is a 41 kDa protein and has 61-68% sequence similarity to known eukaryotic aldolases. Its crystal structure has been published.
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DAP-decarboxylase catalyzes the final step in the meso-diaminopimelate/lysine biosynthetic pathway. Lysine is used for protein synthesis and used in the peptidoglycan layer of Gram-positive bacteria cell walls. This enzyme is not found in humans, but the ortholog is ornithine decarboxylase.
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In enzymology, an anthranilate synthase () is an enzyme that catalyzes the chemical reaction :chorismate + L-glutamine \rightleftharpoons anthranilate + pyruvate + L-glutamate 2 Thus, the two substrates of this enzyme are chorismate and L-glutamine, whereas its 3 products are anthranilate, pyruvate, and L-glutamate.
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Pectinase enzymes are used for extracting juice from purée. This is done when the enzyme pectinase breaks down the substrate pectin and the juice is extracted. The enzyme pectinase lowers the activation energy needed for the juice to be produced and catalyzes the reaction.
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This locus encodes a sialyltransferase. The encoded type II transmembrane protein catalyzes the transfer of sialic acid from CMP to an oligosaccharide substrate. Polymorphisms at this locus may be associated with variations in risperidone response in schizophrenic patients. Alternatively spliced transcript variants have been described.
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In addition, gene knockout studies can be performed using flux balance analysis. The enzyme that correlates to the gene that needs to be removed is given a constraint value of 0. Then, the reaction that the particular enzyme catalyzes is completely removed from the analysis.
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Thymidylate synthase (TS) () is an enzyme that catalyzes the conversion of deoxyuridine monophosphate (dUMP) to deoxythymidine monophosphate (dTMP). Thymidine is one of the nucleotides in DNA. With inhibition of TS, an imbalance of deoxynucleotides and increased levels of dUMP arise. Both cause DNA damage.
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Hydrobromic acid is mainly used for the production of inorganic bromides, especially the bromides of zinc, calcium, and sodium. It is a useful reagent for generating organobromine compounds. Certain ethers are cleaved with HBr. It also catalyzes alkylation reactions and the extraction of certain ores.
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Chloro(cyclopentadienyl)bis(triphenylphosphine)ruthenium(II) serves as a catalyst for a variety of specialized reactions. For example, in the presence of NH4PF6 it catalyzes the isomerisation of allylic alcohols to the corresponding saturated carbonyls.Murahashi, Shun-Ichi. "Ruthenium in Organic Synthesis" (2006) Wiley-VCH: Weinheim.
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PtO2, also known as Adams' catalyst, is used as a hydrogenation catalyst, specifically for vegetable oils. Platinum also strongly catalyzes the decomposition of hydrogen peroxide into water and oxygen and it is used in fuel cells as a catalyst for the reduction of oxygen.
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The pistol ribozyme is an RNA structure that catalyzes its own cleavage at a specific site. In other words, it is a self-cleaving ribozyme. The pistol ribozyme was discovered through comparative genomic analysis. Subsequent biochemical analysis determined further biochemical characteristics of the ribozyme.
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Therefore, TcdA catalyzes glucosylation and the subsequent irreversible inactivation of target molecules in the Ras family of small GTPases. These target molecules include RhoA, Rac, and Cdc42, which are regulatory proteins of the eukaryotic actin cytoskeleton and modulators of many various cell signaling pathways.
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In the presence of excess ATP, the enzyme ribonucleotide reductase initiates a chain reaction with UDP, which catalyzes the formation of deoxyuridine diphosphate (dUDP), which is then converted to deoxyuridine triphosphate (dUTP), then deoxyuridine monophosphate (dUMP) via the addition or removal of phosphate groups.
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Notable is esomeprazole, the optically pure form of the proton-pump inhibitor omeprazole. Another commercially important sulfoxides include armodafinil. Methionine sulfoxide forms from the amino acid methionine and its accumulation is associated with aging. The enzyme DMSO reductase catalyzes the interconversion of DMSO and dimethylsulfide.
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Present in the shikimate pathway, in the pathway to synthesize tyrosine (a non-essential amino acid in both plants and animals). It catalyzes the oxidative decarboxylation reaction of prephenate to 4-hydroxyphenylpyruvate."InterPro." Bifunctional Chorismate Mutase/prephenate Dehydrogenase T-protein (IPR008244). InterPro, n.d. Web.
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Prephenate dehydrogenase catalysis In enzymology, a prephenate dehydrogenase () is an enzyme that catalyzes the chemical reaction : prephenate + NAD+ \rightleftharpoons 4-hydroxyphenylpyruvate + CO2 \+ NADH Thus, the two substrates of this enzyme are prephenate and NAD+, whereas its 3 products are 4-hydroxyphenylpyruvate, CO2, and NADH.
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Structurally CDKAL1 contains two iron (Fe) sulfur (S) clusters, therefore its function can be reduced by inhibiting Fe-S cluster biosynthesis. Enzymatically, CDKAL1 catalyzes methylthiolation of N6-threonylcarbamoyl adenosine 37 (t6A37) in cytosolic tRNA, which has been determined to stabilize anticodon-codon interactions during translation.
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Arsenate reductase (azurin) () is an enzyme that catalyzes the chemical reaction :arsenite + H2O + 2 azurinox \rightleftharpoons arsenate + 2 azurinred \+ 2 H+ The 3 substrates of this enzyme are arsenite, water, and oxidised azurin, whereas its 3 products are arsenate, reduced azurin, and hydrogen ion.
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3-oxo-5α-steroid 4-dehydrogenase 1 is an enzyme that in humans is encoded by the SRD5A1 gene. It is one of three forms of 5α-reductase. Steroid 5α-reductase (EC 1.3.99.5) catalyzes the conversion of testosterone into the more potent androgen, dihydrotestosterone (DHT).
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It catalyzes the transfer of electrons from NADH to coenzyme Q10 (CoQ10) and, in eukaryotes, it is located in the inner mitochondrial membrane. This enzyme helps to establish a transmembrane difference of proton electrochemical potential that the ATP synthase then uses to synthesize ATP.
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This enzyme catalyzes the conversion of 4-maleylacetoacetate to 4-fumarylacetoacetate. 4-Maleylacetoacetate isomerase belongs to the zeta class of the glutathione S-transferase (GST) superfamily.; This image shows the structure of the peptide backbone of 4-maleylacetoacetate isomerase, highlighting the glutathione binding site.
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In enzymology, a steroid Δ5-isomerase () is an enzyme that catalyzes the chemical reaction :a 3-oxo-Δ5-steroid \rightleftharpoons a 3-oxo-Δ4-steroid Hence, this enzyme has one substrate, a 3-oxo-Δ5-steroid, and one product, a 3-oxo-Δ4-steroid.
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In enzymology, a hepoxilin-epoxide hydrolase () is an enzyme that catalyzes the conversion of the epoxyalcohol metabolites arachidonic acid, hepoxilin A3 and hepoxilin B3 to their tri-hydroxyl products, trioxolin A3 and trioxilin B3, respectively. These reactions in general inactivate the two biologically active hepoxilins.
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Thiamin pyrophosphokinase 1 is an enzyme that in humans is encoded by the TPK1 gene. This gene encodes a protein, that exists as a homodimer, which catalyzes the conversion of thiamine to thiamine pyrophosphate. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
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3-Hydroxyacyl CoA dehydrogenase is classified as an oxidoreductase. It is involved in fatty acid metabolic processes. Specifically it catalyzes the third step of beta oxidation; the oxidation of L-3-hydroxyacyl CoA by NAD+. The reaction converts the hydroxyl group into a keto group.
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Dolichyl monophosphate is an essential glycosyl carrier lipid for C- and O-mannosylation and N-glycosylation of proteins and for biosynthesis of glycosylphosphatidylinositol anchors in endoplasmic reticulum (ER). Dolichol kinase catalyzes CTP-mediated phosphorylation of dolichol, the terminal step in de novo dolichyl monophosphate biosynthesis.
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Bacteria in the genus Ureaplasma are known commensals in humans and possess the enzyme Urease (catalyzes urea to carbon dioxide and ammonia). Both Mycoplasma and Ureaplasma species can be grown on the same PPLO medium due to their similarities in metabolism and growth requirement.
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Elongase is a generic term for an enzyme that catalyzes carbon chain extension of an organic molecule, especially a fatty acid. Elongases play a variety of roles in mammalian organisms, accounting for changes in tissue function, lipid regulation, and the overall physiology of an organism.
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The enzyme is also involved in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. NQO1 catalyzes the reduction of vitamin K1,K2 and K3 into their hydroquinone form, but it only has a high affinity for Vitamin K3. Vitamin K hydroquinone serves as a cofactor for vitamin K γ‐carboxylase that catalyzes γ‐carboxylation of specific glutamic acid residues in Gla‐factors/proteins (Gla domain) leading to their activation and participation in blood clotting and bone metabolism. Vitamin K is used as radiation sensitizer or in mixtures with other chemotherapeutic drugs to treat several types of cancer.
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Cyanase catalyzes the metabolic conversion of toxic cyanate to carbamate (H2NCOO−). The enzyme does this by first catalyzing the conversion of cyanate to carbamate, which then spontaneously decomposes to carbon dioxide and ammonia: # cyanate (OCN−) + HCO3− \+ H+ \rightleftharpoons carbamate (H2NCOO−) + CO2 # carbamate (H2NCOO−) + H+ \rightleftharpoons NH3 \+ CO2 (spontaneous) The resulting net reaction is: :cyanate (OCN−) + HCO3− \+ 2 H+ \rightleftharpoons NH3 \+ 2 CO2 Cyanase enzyme catalyzes the reaction of bicarbonate and cyanate forming carbamate, to be rapidly decomposed into carbon dioxide and ammonia. The two adjacent anion binding sights signified by the catalytic Arg 96 residues on different monomers allow this reaction to occur in the pocket. Created on ChemDraw.
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The biosynthesis of ribostamycin begins with the sugar, D-glucose, which is phosphorylated at the 6 position to form glucose-6-phosphate. The enzyme rbmA contains a genetic sequence that corresponds to NAD+ binding and catalyzes the formation of 2-deoxy-scyllo- inosose. The enzyme rmbB then catalyzes the transamination of 2-deoxy-scyllo- inosose to 2-deoxy-scyllo-inosamine with L-glutamine and pyridoxal phosphate (PLP). Enzyme rbmC oxidizes the ring to 2-deoxy-3-amino-scyllo-inosose, which is then transaminated by enzyme rmbB to DOS. DOS is then glycosylated by the glycosyltransferase rmbD with uridine diphosphate N-acetylglucosamine (UDP- Glc-NAc) to form 2’-N-acetylparomamine.
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The ABO gene resides on chromosome 9 at the band 9q34.2 and contains 7 exons. The ABO locus encodes three alleles. The A allele produces α-1,3-N-acetylgalactosamine transferase (A-transferase), which catalyzes the transfer of GalNAc residues from the UDP-GalNAc donor nucleotide to the Gal residues of the acceptor H antigen, converting the H antigen into A antigen in A and AB individuals. The B allele encodes α-1,3-galactosyl transferase (B-transferase), which catalyzes the transfer of Gal residues from the UDP-Gal donor nucleotide to the Gal residues of the acceptor H antigen, converting the H antigen into B antigen in B and AB individuals.
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The covalent linkage between the ribose and pyrimidine occurs at position C1See IUPAC nomenclature of organic chemistry for details on carbon residue numbering of the ribose unit, which contains a pyrophosphate, and N1 of the pyrimidine ring. Orotate phosphoribosyltransferase (PRPP transferase) catalyzes the net reaction yielding orotidine monophosphate (OMP): :Orotate + 5-Phospho-α-D-ribose 1-diphosphate (PRPP) → Orotidine 5'-phosphate + Pyrophosphate Orotidine 5'-monophosphate is decarboxylated by orotidine-5'-phosphate decarboxylase to form uridine monophosphate (UMP). PRPP transferase catalyzes both the ribosylation and decarboxylation reactions, forming UMP from orotic acid in the presence of PRPP. It is from UMP that other pyrimidine nucleotides are derived.
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6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2 is an enzyme that in humans is encoded by the PFKFB2 gene. The protein encoded by this gene is involved in both the synthesis and degradation of fructose-2,6-bisphosphate, a regulatory molecule that controls glycolysis in eukaryotes. The encoded protein has a 6-phosphofructo-2-kinase activity that catalyzes the synthesis of fructose-2,6-bisphosphate, and a fructose-2,6-biphosphatase activity that catalyzes the degradation of fructose-2,6-bisphosphate. This protein regulates fructose-2,6-bisphosphate levels in the heart, while a related enzyme encoded by a different gene regulates fructose-2,6-bisphosphate levels in the liver and muscle.
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The cyclooxygenase active site, which catalyzes the formation of prostaglandin G2 (PGG2) from arachidonic acid, resides at the apex of a long hydrophobic channel, extending from the membrane-binding domain to the center of the molecule. The peroxidase active site, which catalyzes the reduction of PGG2 to PGH2, is located on the other side of the molecule, at the heme binding site. Both MPO and the catalytic domain of PGHS are mainly alpha-helical, 19 helices being identified as topologically and spatially equivalent; PGHS contains 5 additional N-terminal helices that have no equivalent in MPO. In both proteins, three Asn residues in each monomer are glycosylated.
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In enzymology, a dTDP-glucose 4,6-dehydratase () is an enzyme that catalyzes the chemical reaction :dTDP-glucose \rightleftharpoons dTDP-4-dehydro-6-deoxy- D-glucose + H2O Hence, this enzyme has one substrate, dTDP-glucose, and two products, dTDP-4-dehydro-6-deoxy-D-glucose and H2O.
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In enzymology, a 5-dehydro-4-deoxyglucarate dehydratase () is an enzyme that catalyzes the chemical reaction :5-dehydro-4-deoxy-D-glucarate \rightleftharpoons 2,5-dioxopentanoate + H2O + CO2 Hence, this enzyme has one substrate, 5-dehydro-4-deoxy-D-glucarate, but three products: 2,5-dioxopentanoate, H2O, and CO2.
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These two enantiomers of MMSA are substrates for MMSDH, which catalyzes their oxidative decarboxylation to propionyl-CoA. Both NAD+ and CoA act as cofactors with the enzyme, although they work in opposite directions; NAD+ works to protect the enzyme against proteolysis, but CoA esters diminish that effect.
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Sedoheptulose-bisphosphatase (also sedoheptulose-1,7-bisphosphatase or SBPase) () is an enzyme that catalyzes the removal of a phosphate group from sedoheptulose 1,7-bisphosphate to produce sedoheptulose 7-phosphate. SBPase is an example of a phosphatase, or, more generally, a hydrolase. This enzyme participates in the Calvin cycle.
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In enzymology, an acetylxylan esterase () is an enzyme that catalyzes a chemical reaction, the deacetylation of xylans and xylo-oligosaccharides. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is likewise acetylxylan esterase.
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Also like the other forms of CAH, 11β-OH CAH is inherited as an autosomal recessive disease. 11β-Hydroxylase mediates the final step of the glucocorticoid pathway, producing cortisol from 11-deoxycortisol. It also catalyzes the conversion of 11-deoxycorticosterone (DOC) to corticosterone in the mineralocorticoid pathway.
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Acylglycerol kinase synthesizes phosphatidic and lysophosphatidic acids. The enzyme uses ATP to put a phosphate group on acyl glycerol and diacylglycerol. It catalyzes the following reactions: ATP + acylglycerol = ADP + acyl-sn-glycerol 3-phosphate. ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate.
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In enzymology, aldose reductase (or aldehyde reductase) () is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. It is primarily known for catalyzing the reduction of glucose to sorbitol, the first step in polyol pathway of glucose metabolism.
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The protein encoded by COX10 is an assembly factor essential to COX synthesis, participating in the first step of the mitochondrial heme A biosynthetic pathway. It catalyzes the farnesylation of the vinyl group at position C2 of protoheme (heme B) and converts it to heme O.
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The pathway used is called the ubiquinone biosynthesis pathway, it catalyzes the first step in the biosynthesis of ubiquinone in E. coli. Ubiquinone is a lipid-soluble electron- transporting coenzyme. They are essential electron carriers in prokaryotes and are essential in aerobic organisms to achieve ATP.
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Lecithin cholesterol acyltransferase deficiency is a disorder of lipoprotein metabolism. The disease has two forms: Familial LCAT deficiency, in which there is complete LCAT deficiency, and Fish-eye disease, in which there is a partial deficiency. Lecithin cholesterol acyltransferase catalyzes the formation of cholesterol esters in lipoproteins.
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A computer-generated image of a type of pancreatic lipase (PLRP2) from the guinea pig. . A lipase (, ) is any enzyme that catalyzes the hydrolysis of fats (lipids). Lipases are a subclass of the esterases. Lipases perform essential roles in digestion, transport and processing of dietary lipids (e.g.
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For instance, the transferase hexokinase catalyzes the phosphorylation of glucose to make glucose-6-phosphate. Active site residues of hexokinase allow for stabilization of the glucose molecule in the active site and spur the onset of an alternative pathway of favorable interactions, decreasing the activation energy.
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Stereoselective proline- catalyzed aldol reaction. In this reaction proline catalyzes the reaction through creation of an enamine intermediate that is highly nucleophilic. The acid group on the catalyst helps facilitate the carbon-carbon bond formation by coordinating with the aldehyde oxygen. This greatly improves stereoselectivity and yield.
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UDP-glucuronic acid decarboxylase 1 is an enzyme that in humans is encoded by the UXS1 gene. UDP-glucuronate decarboxylase (UGD; EC 4.1.1.35) catalyzes the formation of UDP-xylose from UDP-glucuronate. UDP-xylose is then used to initiate glycosaminoglycan biosynthesis on the core protein of proteoglycans.
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This protein belongs to the aldehyde dehydrogenase family of proteins. It has a high activity for oxidation of gamma-aminobutyraldehyde and other amino aldehydes. The enzyme catalyzes the dehydrogenation of gamma-aminobutyraldehyde to gamma- aminobutyric acid (GABA). This isozyme is a tetramer of identical 54-kD subunits.
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4.8); and dsr is the dissimilatory (bi)sulfite reductase (EC 1.8.99.5); The enzyme dissimilatory (bi)sulfite reductase, dsrAB (EC 1.8.99.5), that catalyzes the last step of dissimilatory sulfate reduction, is the functional gene most used as a molecular marker to detect the presence of sulfate-reducing microorganisms.
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Pyruvate decarboxylase starts this process by converting pyruvate into acetaldehyde and carbon dioxide. Pyruvate decarboxylase depends on cofactors thiamine pyrophosphate (TPP) and magnesium. This enzyme should not be mistaken for the unrelated enzyme pyruvate dehydrogenase, an oxidoreductase (), that catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA.
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Stizolobium hassjoo catalyzes the conversion of L-dihydroxyphenylalanine into stizolobinic acid, alpha-amino-6-carboxy-2-oxo-2H-pyran-3-propionic acid, and stizolobic acid, alpha-amino-6-carboxy-2-oxo-2H-pyran-4-propionic acid, in the presence of NADP+ or NAD+ under aerobic conditions.
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Pathway for the biosynthesis of trans-cinnamaldehyde. The biosynthesis of cinnamaldehyde begins with deamination of L-phenylalanine into cinnamic acid by the action of phenylalanine ammonia lyase (PAL). PAL catalyzes this reaction by a non-oxidative deamination. This deamination relies on the MIO prosthetic group of PAL.
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Riboflavin kinase catalyzes the phosphorylation of riboflavin to create flavin mononucleotide(FMN). It has an ordered binding mechanism where riboflavin must bind to the kinase before it binds to the ATP molecule. Divalent cations help coordinate the nucleotide. The general mechanism is shown in the figure below.
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Shortly after the start of transcription, the 5' end of the mRNA being synthesized is bound by a cap-synthesizing complex associated with RNA polymerase. This enzymatic complex catalyzes the chemical reactions that are required for mRNA capping. Synthesis proceeds as a multi-step biochemical reaction.
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In enzymology, a (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline N-methyltransferase is an enzyme that catalyzes the chemical reaction: 500px : S-adenosyl-L-methionine + (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline \rightleftharpoons S-adenosyl-L-homocysteine + N-methyl-(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline This enzyme participates in alkaloid biosynthesis.
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TSG101 plays an important role in the pathogenesis of HIV and other viruses. In uninfected cells, TSG101 functions in the biogenesis of the multivesicular body (MVB), which suggests that HIV may bind TSG101 in order to gain access to the downstream machinery that catalyzes MVB vesicle budding.
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Phospholipase A2 (EC 3.1.1.4) catalyzes the release of fatty acids from glycero-3-phosphocholines. The best known varieties are the digestive enzymes secreted as zymogens by the pancreas of mammals as well as fish. Sequences of pancreatic PLA2 enzymes from a variety of mammals have been reported.
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Oxidosqualene cyclase is a key enzyme in the cholesterol biosynthesis pathway. It catalyzes the formation of lanosterol, which is then converted through many steps into cholesterol. The body uses cholesterol for temperature regulation. It is also a precursor for testosterone in males and oestradiol in females.
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This gene encodes a member of the ALG6/ALG8 glucosyltransferase family. The encoded protein catalyzes the addition of the first glucose residue to the growing lipid- linked oligosaccharide precursor of N-linked glycosylation. Mutations in this gene are associated with congenital disorders of glycosylation type Ic.
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FAH catalyzes the conversion of fumarylacetoacetate to fumarate and acetoacetate. Loss of FAH results in the accumulation of upstream compounds in the catabolic pathway. These include maleylacetoacetate (MAA) and fumarylacetoacetate (FAA). MAA and FAA are converted to succinylacetoacetate (SAA) which is then catabolized to succinylacetone (SA).
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These peptidases contain an active cysteine residue in their centers that catalyzes the hydrolytic cleavage of peptide bonds. Zingibain is noted for its activity as a proteinase and a collagenase. It was first isolated, purified, and reported in 1973 by Ichikawa et al. at Japan Women's University.
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Directed evolution of bacterial proteins related to bioremediation of radionuclides is also a field research. YieF enzyme, for example, naturally catalyzes the reduction of chromium with a very wide range of substrates. Following protein engineering, however, it has also been able to participate in uranyl ion reduction.
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In enzymology, an inulin fructotransferase (DFA-III-forming) () is an enzyme that catalyzes the chemical reaction :Produces alpha-D-fructofuranose beta-D- fructofuranose 1,2':2,3'-dianhydride (DFA III) by successively eliminating the diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
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Sucrase is a digestive enzyme that catalyzes the hydrolysis of sucrose to its subunits fructose and glucose. One form, sucrase-isomaltase, is secreted in the small intestine on the brush border. The sucrase enzyme invertase, which occurs more commonly in plants, also hydrolyzes sucrose but by a different mechanism.
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Ribonuclease (commonly abbreviated RNase) is a type of nuclease that catalyzes the degradation of RNA into smaller components. Ribonucleases can be divided into endoribonucleases and exoribonucleases, and comprise several sub-classes within the EC 2.7 (for the phosphorolytic enzymes) and 3.1 (for the hydrolytic enzymes) classes of enzymes.
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In enzymology, a nucleoside phosphoacylhydrolase () is an enzyme that catalyzes the chemical reaction :Hydrolyses mixed phospho-anhydride bonds This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is nucleoside-5'-phosphoacylate acylhydrolase.
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Exonuclease III (ExoIII) is an enzyme that belongs to the exonuclease family. ExoIII catalyzes the stepwise removal of mononucleotides from 3´-hydroxyl termini of double-stranded DNA. A limited number of nucleotides are removed during each binding event, resulting in coordinated progressive deletions within the population of DNA molecules.
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In enzymology, a histidinol-phosphatase () is an enzyme that catalyzes the chemical reaction :L-histidinol phosphate + H2O \rightleftharpoons L-histidinol + phosphate Thus, the two substrates of this enzyme are L-histidinol phosphate and H2O, whereas its two products are L-histidinol and phosphate. This enzyme participates in histidine metabolism.
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The human gene AGK encodes the enzyme mitochondrial acylglycerol kinase. The protein encoded by this gene is a mitochondrial membrane protein involved in lipid and glycerolipid metabolism. It catalyzes the formation of phosphatidic and lysophosphatidic acids. Defects in this gene have been associated with mitochondrial DNA depletion syndrome 10.
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Glycogen phosphorylase is one of the phosphorylase enzymes (). Glycogen phosphorylase catalyzes the rate-limiting step in glycogenolysis in animals by releasing glucose-1-phosphate from the terminal alpha-1,4-glycosidic bond. Glycogen phosphorylase is also studied as a model protein regulated by both reversible phosphorylation and allosteric effects.
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Tyrosinase is a copper-containing enzyme present in plant and animal tissues that catalyzes the production of melanin and other pigments from tyrosine by oxidation. It is found inside melanosomes which are synthesized in the skin melanocytes. In humans, the tyrosinase enzyme is encoded by the TYR gene.
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Hydrogen easily diffuses through heated palladium, and membrane reactors with Pd membranes are used in the production of high purity hydrogen. Palladium is used in palladium-hydrogen electrodes in electrochemical studies. Palladium(II) chloride readily catalyzes carbon monoxide gas to carbon dioxide and is useful in carbon monoxide detectors.
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Mandelate racemase () is a bacterial enzyme which catalyzes the interconversion of the enantiomers of mandelate via an enol intermediate. This enzyme catalyses the following chemical reaction : (S)-mandelate \rightleftharpoons (R)-mandelate It is a member of the enolase superfamily of enzymes, along with muconate lactonizing enzyme and enolase.
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RuBisCO also catalyzes RuBP with oxygen () in a process called photorespiration, a process that is more prevalent at high temperatures. During photorespiration RuBP combines with to become 3-PGA + phosphoglycolic acid. In the Calvin cycle, RuBP is a product of the phosphorylation of ribulose-5-phosphate by ATP.
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Dopamine beta-hydroxylase (DBH), also known as dopamine beta-monooxygenase, is an enzyme () that in humans is encoded by the DBH gene. Dopamine beta- hydroxylase catalyzes the conversion of dopamine to norepinephrine. Dopamine is converted to norepinephrine by the enzyme dopamine β-hydroxylase. Ascorbic acid serves as a cofactor.
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Trifolin is a chemical compound. It is the kaempferol 3-galactoside. It can be found in Camptotheca acuminata, in Euphorbia condylocarpa or in Consolida oliveriana. Kaempferol 3-O-galactosyltransferase is an enzyme that catalyzes the chemical reaction: UDP-galactose + kaempferol → UDP + kaempferol 3-O-beta-D-galactoside (trifolin).
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In enzymology, formate C-acetyltransferase (pyruvate formate lyase) () is an enzyme. Pyruvate formate lyase is found in Escherichia coli and other organisms. It helps regulate anaerobic glucose metabolism. Using radical non- redox chemistry, it catalyzes the reversible conversion of pyruvate and coenzyme-A into formate and acetyl-CoA.
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In enzymology, a sulfhydrogenase (), also known as sulfur reductase, is an enzyme that catalyzes the reduction of elemental sulfur or polysulfide to hydrogen sulfide using hydrogen as electron donor. This enzyme belongs to the family of oxidoreductases. The systematic name of this enzyme class is H2:polysulfide oxidoreductase.
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In enzymology, an iron—cytochrome-c reductase (created 1972 as , transferred 2014 to ) is an enzyme that catalyzes the chemical reaction :ferrocytochrome c + Fe3+ \rightleftharpoons ferricytochrome c + Fe2+ Thus, the two substrates of this enzyme are ferrocytochrome c and Fe3+, whereas its two products are ferricytochrome c and Fe2+.
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The chelator can have an effect on the kinetic rate and even the catalyzed reaction. If the substrate Mn(II) is chelated with lactate, MnP instead catalyzes the evolution of O2. However, this side reaction has little impact on enzymatic activity because it follows slower third order kinetics.
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The leucine synthesis pathway diverges from the valine pathway beginning with α-ketoisovalerate. α-Isopropylmalate synthase catalyzes this condensation with acetyl CoA to produce α-isopropylmalate. An isomerase converts α-isopropylmalate to β-isopropylmalate. The third step is the NAD+-dependent oxidation of β-isopropylmalate catalyzed by a dehydrogenase.
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His7 splits phosphoribulosylformimino-AICAR-P to form D-erythro- imidazole-glycerol-phosphate. After, His3 forms imidazole acetol-phosphate releasing water. His5 then makes L-histidinol-phosphate, which is then hydrolyzed by His2 making histidinol. His4 catalyzes the oxidation of L-histidinol to form L-histidinal, an amino aldehyde.
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550px Figure 2. Nucleotidyl transfer by DNA polymerase. T7 DNA polymerase catalyzes the phosphoryl transfer during DNA replication of the T7 phage. As shown in Figure 2, the 3’ hydroxyl group of a primer acts as a nucleophile and attacks the phosphodiester bond of nucleoside 5’-triphosphate (dTMP-PP).
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In enzymology, a triphosphate-protein phosphotransferase () is an enzyme that catalyzes the chemical reaction :triphosphate + [microsomal-membrane protein] \rightleftharpoons diphosphate + phospho-[microsomal-membrane protein] Thus, the two substrates of this enzyme are triphosphate and microsomal-membrane protein, whereas its two products are diphosphate and phospho-[microsomal- membrane protein].
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Kirkegaard and Baltimore presented evidence that RNA-dependent RNA polymerase (RdRP) catalyzes recombination by a copy choice mechanism in which the RdRP switches between (+)ssRNA templates during negative strand synthesis. Recombination in RNA viruses appears to be an adaptive mechanism for transmitting an undamaged genome to virus progeny.
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Activity of the two enzymes is not always necessarily coupled. In E. coli glgX selectively catalyzes the cleavage of 4-subunit branches, without the action of glucanotransferase. The product of this cleavage, maltotetraose, is further degraded by maltodextrin phosphorylase. E. coli GlgX is structurally similar to the protein isoamylase.
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11β-HSD also reversibly catalyzes the conversion of 7-ketocholesterol to 7-beta-hydroxycholesterol. Carbenoxolone is a modestly potent, reasonably effective, water-soluble blocker of gap junctions. Carbenoxolone has also been used in topical creams such as Carbosan gel, marketed for treatment of lip sores and mouth ulcers.
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Echinocandin B can undergo deacylation (removal of the lipid side chain) by the action of a deacylase enzyme from the filamentous bacterium Actinoplanes utahensis, which catalyzes the cleavage of the linoleoyl side chain; in three subsequent synthetic steps, including a chemical reacylation, the antifungal drug anidulafungin is synthesized.
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Lastly, the protein Alpha-N-methyltransferease (TAE1) was found to interact with TMEM239. TAE1 catalyzes the methylation of alpha-amino groups of Alanine or Serine residues in [Ala/Ser]-Pro-Lys motifs and Pro-Pro-Lys motifs. TAE1 is also responsible for methylating a number of ribosomal proteins.
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The oxidase catalyzes the transfer of four electrons from reduced plastoquinone to molecular oxygen to form water . The net reaction is written below: 2 QH2 \+ O2 → 2 Q + 2 H2O Analysis of substrate specificity revealed that the enzyme almost exclusively catalyzes the reduction of plastoquinone over other quinones such as ubiquinone and duroquinone. Additionally, iron is essential for the catalytic function of the enzyme and cannot be substituted by another metal cation like Cu2+, Zn2+, or Mn2+ at the catalytic center. It is unlikely that four electrons could be transferred at once in a single iron cluster, so all of the proposed mechanisms involve two separate two-electron transfers from reduced plastoquinone to the di-iron center.
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The glycine cleavage system (GCS) is the major physiological pathway for glycine degradation in mammals and is confined to mitochondria of the liver, kidney, small intestine, pituitary, thyroid glands, and brain. The P-protein is a pyridoxal phosphate-dependent glycine decarboxylase that transfers the methylamine moiety of glycine to one of the thiol groups in the lipoyl component of H-protein, a hydrogen-carrier protein and the second component of the complex. The T-protein catalyzes the release of ammonia and transfer of the one-carbon fragment from the intermediate lipoyl residue to tetrahydrofolate, while the L-protein, a lipoamide dehydrogenase, catalyzes the oxidation of the dihydrolipoyl residue of H-protein and reduction of NAD.
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CpCo(CO)2 catalyzes the cyclotrimerization of alkynes. The catalytic cycle begins with dissociation of one CO ligand forming bis(alkyne) intermediate.Pauson, P.L. “Dicarbonyl(cyclopentadienyl)cobalt(I).” Encyclopedia of Reagents for Organic Synthesis. 2001. :CpCo(CO)2 \+ 2 R2C2 → CpCo(R2C2)2 \+ 2 CO This reaction proceeds by formation of metal-alkyne complexes by dissociation of CO. Although monoalkyne complexes CpCo(CO)(R1C2R2) have not been isolated, their analogues, CpCo(PPh3)(R1C2R2) are made by the following reactions: :CpCo(CO)2 \+ PR3 → CO + CpCo(CO)(PR3) :CpCoL(PR3) + R2C2 → L + CpCo(PR3)(R2C2) (where L = CO or PR3) CpCo(CO)2 catalyzes the formation of pyridines from a mixture of alkynes and nitriles.
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In the field of enzymology, a glycerophospholipid arachidonoyl-transferase (CoA-independent) () is an enzyme that catalyzes the chemical reaction: :1-organyl-2-arachidonoyl-sn-glycero-3-phosphocholine + 1-organyl-2-lyso-sn- glycero-3-phosphoethanolamine \rightleftharpoons 1-organyl-2-arachidonoyl-sn- glycero-3-phosphoethanolamine + 1-organyl-2-lyso-sn-glycero-3-phosphocholine This enzyme catalyzes the transfer of arachidonic acid and other polyenoic fatty acids from intact choline or ethanolamine-containing glycerophospholipids to the sn-2 position of a lyso- glycerophospholipid. The organyl group on sn-1 of the donor or acceptor molecule can be alkyl, acyl or alk-1-enyl. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups.
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In the realm of gene silencing, Polycomb repressive complex 2, one of two classes of the Polycomb group (PcG) family of proteins, catalyzes the di- and tri-methylation of histone H3 lysine 27 (H3K27me2/me3). By binding to the H3K27me2/3-tagged nucleosome, PRC1 (also a complex of PcG family proteins) catalyzes the mono-ubiquitinylation of histone H2A at lysine 119 (H2AK119Ub1), blocking RNA polymerase II activity and resulting in transcriptional suppression. PcG knockout ES cells do not differentiate efficiently into the three germ layers, and deletion of the PRC1 and PRC2 genes leads to increased expression of lineage-affiliated genes and unscheduled differentiation. Presumably, PcG complexes are responsible for transcriptionally repressing differentiation and development-promoting genes.
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In enzymology, a histidinol dehydrogenase (HIS4) (HDH) () is an enzyme that catalyzes the chemical reaction :L-histidinol + 2 NAD+ \rightleftharpoons L-histidine + 2 NADH + 2 H+ Thus, the two substrates of this enzyme are L-histidinol and NAD+, whereas its 3 products are L-histidine, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-histidinol:NAD+ oxidoreductase. This enzyme is also called L-histidinol dehydrogenase. Histidinol dehydrogenase catalyzes the terminal step in the biosynthesis of histidine in bacteria, fungi, and plants, the four-electron oxidation of L-histidinol to histidine.
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The enzyme plays an important role in vitamin metabolism by chain shortening. CYP4F2 is the only known enzyme to ω-hydroxylate tocotrienols and tocopherols (types of Vitamin E), thus making it a key regulator of circulating plasma Vitamin E levels. It catalyzes ω-hydroxylation of the phytyl chain of tocopherols (forms of vitamin E), with preference for gamma- tocopherols over α-tocopherols, thus promoting retention of α-tocopherols in tissues. Both types of Vitamin K (K1 and K2) can be used as co-factors for γ-glutamyl carboxylase, an enzyme that catalyzes the posttranslational modification of Vitamin K-dependent proteins, thus biochemically activating the proteins involved in blood coagulation and bone mineralization.
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Mung Bean Nuclease catalyzes the specific degradation of single-stranded DNA or RNA, and produces mono and oligonucleotides carrying a 5′-P terminus. Mung bean nuclease has a stringent single-stranded specificity for DNA or RNA. Mung bean nuclease has an estimated molecular weight of 39 kDa by SDS-PAGE.
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Ni-SOD is homohexameric, meaning that it has six identical subunits. Each subunit has a single nickel containing active site. The disproportionation mechanism involves a reduction- oxidation cycle where a single electron transfer is catalyzed by the Ni2+/Ni3+ redox couple. Ni-SOD catalyzes close to the barrier of diffusion.
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Mercury(II) reductase (), commonly known as MerA, is an oxidoreductase enzyme and flavoprotein that catalyzes the reduction of Hg2+ to Hg0. Mercury(II) reductase is found in the cytoplasm of many eubacteria in both aerobic and anaerobic environments and serves to convert toxic mercury ions into relatively inert elemental mercury.
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The protein encoded by this gene belongs to the transglutaminase superfamily. It catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Mutations in this gene are associated with spinocerebellar ataxia type 35 (SCA35). Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
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Figure 1: Lanosterol synthase mechanism. The discrete carbocation intermediates show the non- concerted nature of the mechanism. Though some data on the mechanism has been obtained by the use of suicide inhibitors, mutagenesis studies, and homology modeling, it is still not fully understood how the enzyme catalyzes the formation of lanosterol.
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Spermidine is an aliphatic polyamine. Spermidine synthase (SPDS) catalyzes its formation from putrescine. It is a precursor to other polyamines, such as spermine and its structural isomer thermospermine. Spermidine synchronizes an array of biological processes (such as Ca2+, Na+, K+ -ATPase) thus maintaining membrane potential and controlling intracellular pH and volume.
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The protein encoded by this gene is a subunit of a bipartite UDP-N-acetylglucosamine transferase. It heterodimerizes with asparagine-linked glycosylation 14 (ALG14) homolog to form a functional UDP-GlcNAc glycosyltransferase that catalyzes the second sugar addition of the highly conserved oligosaccharide precursor in endoplasmic reticulum N-linked glycosylation.
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In enzymology, juvenile hormone esterase (JH esterase) is an enzyme that catalyzes the hydrolysis of juvenile hormone. For example, the juvenile hormone II (found in Lepidoptera): :methyl (2E,6E)-(10R,11S)-10,11-epoxy-3,7,11-trimethyltrideca-2,6-dienoate + H2O \rightleftharpoons (2E,6E)-(10R,11S)-10,11-epoxy-3,7,11-trimethyltrideca-2,6-dienoic acid + methanol.
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Some cells synthesize argininosuccinic acid from citrulline and aspartic acid and use it as a precursor for arginine in the urea cycle or citrulline-NO cycle. The enzyme that catalyzes the reaction is argininosuccinate synthetase. Argininosuccinic acid is a precursor to fumarate in the citric acid cycle via argininosuccinate lyase.
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Soluble guanylate cyclase (sGC), a heterodimeric protein consisting of an alpha and a beta subunit, catalyzes the conversion of GTP to the second messenger cGMP and functions as the main receptor for nitric oxide and nitrovasodilator drugs. Mutations in this gene have been associated to cases of myocardial infarction (10.1038/nature12722).
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In enzymology, a glycochenodeoxycholate sulfotransferase () is an enzyme that catalyzes the chemical reaction :3'-phosphoadenylyl sulfate + glycochenodeoxycholate \rightleftharpoons adenosine 3',5'-bisphosphate + glycochenodeoxycholate 7-sulfate Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and glycochenodeoxycholate, whereas its two products are adenosine 3',5'-bisphosphate and glycochenodeoxycholate 7-sulfate.
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Beta-1,4-galactosyltransferase 7 also known as galactosyltransferase I is an enzyme that in humans is encoded by the B4GALT7 gene. Galactosyltransferase I catalyzes the synthesis of the glycosaminoglycan-protein linkage in proteoglycans. Proteoglycans in turn are structural components of the extracellular matrix that is found between cells in connective tissues.
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The protein encoded by this gene is a cytoplasmic enzyme involved in cellular energy homeostasis. The encoded protein reversibly catalyzes the transfer of "energy-rich" phosphate between ATP and creatine and between phospho-creatine and ADP. Its functional entity is a MM-CK homodimer in striated (sarcomeric) skeletal and cardiac muscle.
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ECH catalyzes the second step (hydratation) in the breakdown of fatty acids (β-oxidation). Fatty acid metabolism is how human bodies turn fats into energy. Fats in foods are generally in the form of triglycerols. These must be broken down in order for the fats to pass into human bodies.
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In enzymology, an L-lactate dehydrogenase (cytochrome) (EC number 1.1.2.3) is an enzyme that catalyzes the chemical reaction :(S)-lactate + 2 ferricytochrome c \rightleftharpoons pyruvate + 2 ferrocytochrome c Thus, the two substrates of this enzyme are (S)-lactate and ferricytochrome c, whereas its two products are pyruvate and ferrocytochrome c.
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Delta-aminolevulinate synthase 2 also known as ALAS2 is a protein that in humans is encoded by the ALAS2 gene. ALAS2 is an aminolevulinic acid synthase. The product of this gene specifies an erythroid-specific mitochondrially located enzyme. The encoded protein catalyzes the first step in the heme biosynthetic pathway.
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N-Acetylglutamic acid is the second intermediate in the arginine production pathway in Escherichia coli and is produced via NAGS. In this pathway, N-acetylglutamic acid kinase (NAGK) catalyzes the phosphorylation of the gamma (third) carboxyl group of N-acetylglutamic acid using the phosphate produced by hydrolysis of adenosine triphosphate (ATP).
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A stereoretentive Stille coupling using alkyl carbastannatranes. Palladium also catalyzes Stille coupling of secondary alkyl carbastannatranes and aryl electrophiles. This report serves as the first example of employing chiral alkyl carbastannatrane reagents in enantioselective synthesis. Related methodology enable selective acyl substitution using enantioenriched stannatranes as an alternative to classical enolate chemistry.
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Different biosynthetic pathways are responsible for converting the different B3 vitamins into NAD+. The enzyme nicotinamide phosphoribosyltransferase (Nampt) catalyzes the rate-limiting step of the two- step pathway converting nicotinamide to NAD+. NR kinase enzymes can also function as a salvage pathway for NAD+, but this pathway is not essential.
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The category of EC 2.10 includes enzymes that transfer molybdenum or tungsten-containing groups. However, as of 2011, only one enzyme has been added: molybdopterin molybdotransferase. This enzyme is a component of MoCo biosynthesis in Escherichia coli. The reaction it catalyzes is as follows: adenylyl-molybdopterin + molybdate \rightarrow molybdenum cofactor + AMP.
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In enzymology, a cis-2-enoyl-CoA reductase (NADPH) () is an enzyme that catalyzes the chemical reaction :acyl-CoA + NADP+ \rightleftharpoons cis-2,3-dehydroacyl-CoA + NADPH + H+ Thus, the two substrates of this enzyme are acyl-CoA and NADP+, whereas its 3 products are cis-2,3-dehydroacyl-CoA, NADPH, and H+.
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In enzymology, a deacetoxycephalosporin-C synthase () is an enzyme that catalyzes the chemical reaction center penicillin N + 2-oxoglutarate + O2 \rightleftharpoons deacetoxycephalosporin C + succinate + CO2 \+ H2O The 3 substrates of this enzyme are penicillin N, 2-oxoglutarate, and O2, whereas its 4 products are deacetoxycephalosporin C, succinate, CO2, and H2O.
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The biocompatibility and high surface energy of Au allow it to bind to a large amount of protein without altering its activity and results in a more sensitive sensor. Moreover, Au NP also catalyzes biological reactions. Gold nanoparticle under 2 nm has shown catalytic activity to the oxidation of styrene.
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NOR catalyzes the formation of nitrogen to nitrogen (N--N) bonding. The conformation changes of the active site and attached ligands (ie. Glu211) allows NO to be positioned in the crowded binuclear center and form N --N bonds. The precise mechanism of catalysis is still unknown, although hypotheses have been proposed.
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Rapid urease test, also known as the CLO test (Campylobacter-like organism test), is a rapid diagnostic test for diagnosis of Helicobacter pylori. The basis of the test is the ability of H. pylori to secrete the urease enzyme, which catalyzes the conversion of urea to ammonia and carbon dioxide.
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In enzymology, a phosphoribosylanthranilate isomerase [ PRAI ] () is an enzyme that catalyzes the third step of the synthesis of the amino acid tryptophan. This enzyme participates in the phenylalanine, tyrosine and tryptophan biosynthesis pathway, also known as the aromatic amino acid biosynthesis pathway In yeast it is encoded by the TRP1 gene.
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This reduction was proposed to be a cause of breast cancer. EZH2 is the catalytic subunit of Polycomb Repressor Complex 2 (PRC2) which catalyzes methylation of histone H3 at lysine 27 (H3K27me) and mediates gene silencing of target genes via local chromatin reorganization. EZH2 protein is up-regulated in numerous cancers.
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Euchromatic histone-lysine N-methyltransferase 2 (EHMT2), also known as G9a, is a histone methyltransferase enzyme that in humans is encoded by the EHMT2 gene. G9a catalyzes the mono- and di-methylated states of histone H3 at lysine residue 9 (i.e., H3K9me1 and H3K9me2) and lysine residue 27 (H3K27me1 and HeK27me2).
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Glyoxylate reductase (), first isolated from spinach leaves, is an enzyme that catalyzes the reduction of glyoxylate to glycolate, using the cofactor NADH or NADPH. The systematic name of this enzyme class is glycolate:NAD+ oxidoreductase. Other names in common use include NADH-glyoxylate reductase, glyoxylic acid reductase, and NADH-dependent glyoxylate reductase.
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In enzymology, a shikimate dehydrogenase () is an enzyme that catalyzes the chemical reaction :shikimate + NADP+ \rightleftharpoons 3-dehydroshikimate + NADPH + H+ Thus, the two substrates of this enzyme are shikimate and NADP+, whereas its 3 products are 3-dehydroshikimate, NADPH, and H+. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis.
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The Shikimate Dehydrogenase Reaction Shikimate Dehydrogenase catalyzes the reversible NADPH-dependent reaction of 3-dehydroshikimate to shikimate. The enzyme reduces the carbon-oxygen double bond of a carbonyl functional group to a hydroxyl (OH) group, producing the shikimate anion. The reaction is NADPH dependent with NADPH being oxidised to NADP+.
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In enzymology, a polynucleotide adenylyltransferase () is an enzyme that catalyzes the chemical reaction :ATP + RNA-3'OH \rightleftharpoons pyrophosphate + RNApA-3'OH Thus, the two substrates of this enzyme are ATP and RNA, whereas its two products are pyrophosphate and RNA with an extra adenosine nucleotide at its 3' end.
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In enzymology, an UTP—hexose-1-phosphate uridylyltransferase () is an enzyme that catalyzes the chemical reaction :UTP + alpha-D-galactose 1-phosphate \rightleftharpoons diphosphate + UDP-galactose Thus, the two substrates of this enzyme are UTP and alpha-D-galactose 1-phosphate, whereas its two products are diphosphate and UDP-galactose.
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In enzymology, an elongation factor 2 kinase () is an enzyme that catalyzes the chemical reaction: :ATP + [elongation factor 2] \rightleftharpoons ADP + [elongation factor 2] phosphate. Thus, the two substrates of this enzyme are ATP and elongation factor 2, whereas its two products are adenosine diphosphate (ADP) and elongation factor 2 phosphate.
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In enzymology, a ribitol 2-dehydrogenase () is an enzyme that catalyzes the chemical reaction :ribitol + NAD+ \rightleftharpoons D-ribulose + NADH + H+ Thus, the two substrates of this enzyme are ribitol and NAD+, whereas its 3 products are D-ribulose, NADH, and H+. This enzyme participates in pentose and glucuronate interconversions.
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PNGase F catalyzes the cleavage of an internal glycoside bond in an oligosaccharide. It cleaves all asparagine-linked complex, hybrid, or high mannose oligosaccharides unless the core GlcNAc contains an alpha 1,3- fucose.PNGase F cleavage sites. The asparagine residue, from which the glycan is removed, is deaminated to aspartic acid.
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Unlike the prevalence of cobalt(II) complexes, compounds of rhodium(II) are rare. The sandwich compound rhodocene is one example, even it exists in equilibrium with a dimeric Rh(I) derivative. Although not organometallic, rhodium(II) acetate (Rh2(OAc)4) catalyzes cyclopropanations via organometallic intermediates. Rhodium(II) porphyrin complexes react with methane.
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Eosinophil peroxidase catalyzes the haloperoxidase reaction. EPO can take chloride, bromide and iodide as substrates, as well as the pseudohalide thiocyanate (SCN−). However, the enzyme prefers bromide over chloride, iodide over bromide and thiocyanate over iodide, with regard to reaction velocities. In fact, only myeloperoxidase can oxidize chloride with any considerable rate.
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Protein L-isoaspartyl methyltransferase (PIMT, PCMT), also called S-adenosyl- L-methionine:protein-L-isoaspartate O-methyltransferase, is an enzyme which recognizes and catalyzes the repair of damaged L-isoaspartyl and D-aspartyl groups in proteins. It is a highly conserved enzyme which is present in nearly all eukaryotes, archaebacteria, and Gram-negative eubacteria.
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Imidazolonepropionase catalyzes the reaction to form formiminoglutamate (FIGLU) from 4-imidazolone-5-propionate. The formimino group is transferred to tetrahydrofolate, and the remaining five carbons form glutamate. Overall, these reactions result in the formation of glutamate and ammonia. Glutamate can then be deaminated by glutamate dehydrogenase or transaminated to form α-ketoglutarate.
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Heme oxygenase or haem oxygenase (HO) is an enzyme that catalyzes the degradation of heme. This produces biliverdin, ferrous iron, and carbon monoxide. HO was first described in the late 1960s when Raimo Tenhunen demonstrated an enzymatic reaction for heme catabolism. HO is the premier source for endogenous carbon monoxide (CO) production.
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UDP-N-acetylglucosamine transferase subunit ALG14 homolog is a protein that in humans is encoded by the ALG14 gene. Asparagine (N)-glycosylation is an essential modification that regulates protein folding and stability. ALG13 and ALG14 (this protein) constitute the UDP-GlcNAc transferase, which catalyzes a key step in endoplasmic reticulum N-linked glycosylation.
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The biosynthesis of lipid-linked oligosaccharides is highly conserved among eukaryotes and is catalyzed by 14 glycosyltransferases in an ordered stepwise manner. The Alg1 mannosyltransferase I (MT I) catalyzes the first mannosylation step in this process. Clinically, the deficiency of ALG1 in humans results in ALG1-CDG, a congenital disorder of glycosylation.
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In enzymology, a polyneuridine-aldehyde esterase () is an enzyme that catalyzes the chemical reaction: :polyneuridine aldehyde + H2O \rightleftharpoons 16-epivellosimine + CO2 \+ methanol Thus, the two substrates of this enzyme are polyneuridine aldehyde and H2O, whereas its three products are 16-epivellosimine, CO2, and methanol. This enzyme participates in indole and ipecac alkaloid biosynthesis.
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Kexin () is a prohormone-processing protease, specifically a yeast serine peptidase, found in the budding yeast (S. cerevisiae). It catalyzes the cleavage of -Lys-Arg- and -Arg-Arg- bonds to process yeast alpha-factor pheromone and killer toxin precursors. The human homolog is PCSK4. It is a family of subtilisin-like peptidases.
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Tryptophan hydroxylase (TPH) is an enzyme () involved in the synthesis of the neurotransmitter serotonin. Tyrosine hydroxylase, phenylalanine hydroxylase, and tryptophan hydroxylase together constitute the family of biopterin- dependent aromatic amino acid hydroxylases. TPH catalyzes the following chemical reaction : L-tryptophan + tetrahydrobiopterin + O2 \rightleftharpoons 5-Hydroxytryptophan + dihydrobiopterin + H2O It employs one additional cofactor, iron.
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Probable leucyl-tRNA synthetase, mitochondrial is an enzyme that in humans is encoded by the LARS2 gene. This gene encodes a class 1 aminoacyl-tRNA synthetase, mitochondrial leucyl-tRNA synthetase. Each of the twenty aminoacyl-tRNA synthetases catalyzes the aminoacylation of a specific tRNA or tRNA isoaccepting family with the cognate amino acid.
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RuBisCo catalyzes the fixation of atmospheric carbon dioxide in the chloroplasts of plants. It uses ribulose 1,5-bisphosphate (RuBP) as substrate and facilitates carboxylation at the C2 carbon via an endiolate intermediate. The two three-carbon products (3-Phosphoglycerate) are subsequently fed into the Calvin cycle. Atmospheric oxygen competes with this reaction.
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Ethion can undergo biotransformation in the human body, this happens in the liver. Ethion undergoes desulfurization here and is thereby changed in its active metabolite: ethion monoxon. This enzyme cytochrome P-450 catalyzes this step. Ethion monoxon is an inhibitor of the neuro enzyme cholinesterase (ChE), because it contains an active oxygen.
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Rising action is the second phase in Freytag's five-phase structure. It starts with a conflict, for example, the death of a character. The inciting incident is the point of the plot that begins the conflict. It is the event that catalyzes the protagonist to go into motion and to take action.
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Sarcosine oxidase is an enzyme () that catalyzes the oxidative demethylation of sarcosine to yield glycine, H2O2, 5,10-CH2-tetrahydrofolate in a reaction requiring H4-tetrahydrofolate and oxygen. Corynebacterial sarcosine oxidase is a heterotetramer and is produced as an inducible enzyme when Corynebacterium sp.is grown with sarcosine as source of carbon and energy.
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L-gulonolactone oxidase (EC 1.1.3.8) is an enzyme that produces vitamin C, but is non-functional in Haplorrhini (including humans), in some bats, and in guinea pigs. It catalyzes the reaction of L-gulono-1,4-lactone with oxygen to L-xylo-hex-3-gulonolactone and hydrogen peroxide. It uses FAD as a cofactor.
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These enzymes can also N-acetylate 4-aminobiphenyl. N-Acetylated products are difficult to oxidize and because of this acetylation is considered a detoxification step for aromatic amines. Glucuronidation also represents a major metabolic pathway for carcinogenic aromatic amines. A certain human UGT catalyzes the formation of the N-glucuronide of 4-aminobiphenyl.
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In microorganisms and plants, the enzyme serine acetyltransferase catalyzes the transfer of acetyl group from acetyl-CoA onto L-serine to yield O-acetyl-L-serine. The following reaction step, catalyzed by the enzyme O-acetyl serine (thiol) lyase, replaces the acetyl group of O-acetyl-L-serine with sulfide to yield cysteine.
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The overall reaction is: : Isobutyryl-CoA + 6 malonyl-CoA +12 NADPH + 12H+ → Isopalmitic acid + 6 CO2 12 NADP + 5 H2O + 7 CoA The difference between (straight-chain) fatty acid synthase and branch- chain fatty acid synthase is substrate specificity of the enzyme that catalyzes the reaction of acyl-CoA to acyl-ACP.
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In enzymology, a benzene 1,2-dioxygenase () is an enzyme that catalyzes the chemical reaction 350px benzene + NADH + H+ \+ O2 \rightleftharpoons cis-cyclohexa-3,5-diene-1,2-diol + NAD+ The 4 substrates of this enzyme are benzene, NADH, H+, and O2, whereas its two products are cis-cyclohexa-3,5-diene-1,2-diol and NAD+.
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In enzymology, a malate synthase () is an enzyme that catalyzes the chemical reaction :acetyl-CoA + H2O + glyoxylate \rightarrow (S)-malate + CoA The 3 substrates of this enzyme are acetyl-CoA, H2O, and glyoxylate, whereas its two products are (S)-malate and CoA. This enzyme participates in pyruvate metabolism and glyoxylate and dicarboxylate metabolism.
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In enzymology, a chrysanthemyl diphosphate synthase () is an enzyme involved in the biosynthesis of terpenoids. This enzyme is also known as CPPase. It catalyzes the chemical reaction shown below (color-coded to show how precursors link): :320px The substrate of CPPase is dimethylallyl diphosphate. The two products are diphosphate and chrysanthemyl diphosphate.
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This gene encodes a nuclear protein, which is a tyrosine kinase belonging to the Ser/Thr family of protein kinases. This protein catalyzes the inhibitory tyrosine phosphorylation of CDC2/cyclin B kinase, and appears to coordinate the transition between DNA replication and mitosis by protecting the nucleus from cytoplasmically activated CDC2 kinase.
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In biochemistry, NAD(P)+ transhydrogenase (Si-specific) () is an enzyme that catalyzes the chemical reaction :NADPH + NAD+ \rightleftharpoons NADP+ \+ NADH Thus, the two substrates of this enzyme are NADPH and NAD+, whereas its two products are NADP+ and NADH. This enzyme participates in nicotinate and nicotinamide metabolism. It employs one cofactor, FAD.
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Here, the enzyme aminoacyl-tRNA-synthetase catalyzes two reactions. In the first one, it attaches an AMP molecule (cleaved from ATP) to the amino acid. The second reaction cleaves the aminoacyl-AMP producing the energy to join the amino acid to the tRNA molecule. Ribosomes have two subunits, one large and one small.
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The encoded protein catalyzes the last step of the mitochondrial fatty acid beta oxidation spiral. Unlike most mitochondrial matrix proteins, it contains a non-cleavable amino-terminal targeting signal. ACAA2 has been shown to be a functional BNIP3 binding partner, which provides a possible link between fatty acid metabolism and cell apoptosis.
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This gene encodes one of the SERCA Ca2+-ATPases, which are intracellular pumps located in the sarcoplasmic or endoplasmic reticula of muscle cells. This enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen, and is involved in muscular excitation and contraction.
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Argininosuccinate synthase or synthetase (ASS; ) is an enzyme that catalyzes the synthesis of argininosuccinate from citrulline and aspartate. In humans, argininosuccinate synthase is encoded by the ASS gene located on chromosome 9. ASS is responsible for the third step of the urea cycle and one of the reactions of the citrulline-NO cycle.
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This method begins with the amplification of gene fragments which need to be recombined, using uracil dNTPs. This amplification solution also contains primers, PfuTurbo, and Cx Hotstart DNA polymerase. Amplified products are next incubated with USER enzyme. This enzyme catalyzes the removal of uracil residues from DNA creating single base pair gaps.
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This gene encodes a protein that possesses three distinct enzymatic activities, methylenetetrahydrofolate dehydrogenase (1.5.1.5), methenyltetrahydrofolate cyclohydrolase (3.5.4.9) and formate–tetrahydrofolate ligase (6.3.4.3). Each of these activities catalyzes one of three sequential reactions in the interconversion of 1-carbon derivatives of tetrahydrofolate, which are substrates for methionine, thymidylate, and de novo purine syntheses.
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In enzymology, a selenocysteine lyase (SCL) () is an enzyme that catalyzes the chemical reaction :L-selenocysteine + reduced acceptor \rightleftharpoons selenide + L-alanine + acceptor Thus, the two substrates of this enzyme are L-selenocysteine and reduced acceptor, whereas its 3 products are selenide, L-alanine, and acceptor. This enzyme employs one cofactor, pyridoxal phosphate.
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Terpenes synthases have a role in producing important molecules in metabolism, these molecules are part of a large group called terpenoids . In particular, the C terminal domain catalyzes the cyclization of geranyl diphosphate, orienting and stabilizing multiple reactive carbocation intermediates. Or in simpler terms, the C terminal aids the synthesis of new molecules.
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Lactate dehydrogenase catalyzes the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+. In homolactic fermentation, one molecule of glucose is ultimately converted to two molecules of lactic acid. Heterolactic fermentation, in contrast, yields carbon dioxide and ethanol in addition to lactic acid, in a process called the phosphoketolase pathway.
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Lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells. LDH catalyzes the conversion of lactate to pyruvate and back, as it converts NAD+ to NADH and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. LDH exists in four distinct enzyme classes.
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An example of a moonlighting enzyme is pyruvate carboxylase. This enzyme catalyzes the carboxylation of pyruvate into oxaloacetate, thereby replenishing the tricarboxylic acid cycle. Surprisingly, in yeast species such as H. polymorpha and P. pastoris, pyruvate carboylase is also essential for proper targeting and assembly of the peroxisomal protein alcohol oxidase (AO).
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Figure 1. Hypothesized hydride transfer reaction mechanism catalyzed by homoserine dehydrogenase and NAD(P)H. PBD ). Homoserine dehydrogenase catalyzes the reaction of aspartate-semialdehyde (ASA) to homoserine. The overall reaction reduces the C4 carboxylic acid functional group of ASA to a primary alcohol and oxidizes the C1 aldehyde to a carboxylic acid.
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PRK catalyzes the phosphorylation of RuP into RuBP. A catalytic residue in the enzyme (i.e. aspartate in RsPRK) deprotonates the O1 hydroxyl oxygen on RuP and activates it for nucleophilic attack of the γ-phosphoryl group of ATP. As the γ-phosphoryl group is transferred from ATP to RuP, its stereochemistry inverts.
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DNA (cytosine-5)-methyltransferase 1 is an enzyme that catalyzes the transfer of methyl groups to specific CpG structures in DNA, a process called DNA methylation. In humans, it is encoded by the DNMT1 gene. DNMT1 forms part of the family of DNA methyltransferase enzymes, which consists primarily of DNMT1, DNMT3A, and DNMT3B.
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Aldose reductase is able to dip into this galactose reservoir and synthesize significant amounts of galactitol. As is mentioned above, galactitol is not a suitable substrate for the enzyme, polyol dehydrogenase, which catalyzes the next step in the carbohydrate metabolic cycle. Thus, the sugar alcohol idly begins to accumulate in the lens.
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A ball-and-stick model of VO(acac)2 Vanadyl acetylacetonate is a blue complex with the formula V(O)(acac)2. This complex features the vanadyl(IV) group, and many related compounds are known. The molecule is square pyramidal, with idealized C2v symmetry. The complex catalyzes epoxidation of allylic alcohols by peroxides.
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Pho1 of A. thaliana is a member of the PHO1 family (11 paralogues in A. thaliana). This protein is 782 amino acyl residues in length and possesses 7 transmembrane segments (TMSs). It functions in inorganic phosphate transport and homeostasis. Pho1 catalyzes efflux of phosphate from epidermal and cortical cells into the xylem.
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6-deoxyerythronolide B hydroxylase is an Actinobacteria Cytochrome P450 enzyme originally from Saccharopolyspora erythraea, catalyzes the 6S-hydroxylate of 6-deoxyerythronolide B (6-DEB) to erythronolide B (EB) which is the first step of biosynthesis of the macrolide antibiotic erythromycin. This bacterial enzyme belongs to CYP family CYP107, with the CYP Symbol CYP107A1.
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NURF interacts with chromatin by binding to modified histones or interacting with various transcription factors. NURF catalyzes nucleosome sliding in either direction on DNA without any apparent modifications to the histone octamer itself. NURF is essential for the expression of homeotic genes. The ISWI ATPase specifically recognizes intact N-terminal histone tails.
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Carbon-based life originates from carboxylation that couples atmospheric carbon dioxide to a sugar. The process is usually catalysed by the enzyme RuBisCO. Ribulose-1,5-bisphosphate carboxylase/oxygenase, the enzyme that catalyzes this carboxylation, is possibly the single most abundant protein on Earth. The Calvin cycle showing the carboxylation of ribulose-1,5-bisphosphate.
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Aldosterone synthase is the enzyme that has steroid 18-hydroxylase activity as well as steroid 11 beta-hydroxylase activity. The 18-hydroxylase activity consists in catalyzing sequential hydroxylations of the steroid angular methyl group at C18. Whereas steroid 11β-hydroxylase (encoded by CYP11B1 gene) only catalyzes hydroxylation at position 11 beta (mainly of 11-deoxycorticosterone and 11-deoxycortisol), aldosterone synthase (encoded by CYP11B2 gene) catalyzes the synthesis of aldosterone from deoxycorticosterone, a process that successively requires hydroxylation at positions 11 beta and 18 and oxidation at position 18. Adrenocorticotropic hormone is assumed to play a role in the regulation of aldosterone synthase likely through stimulating the synthesis of 11-deoxycorticosterone which is the initial substrate of the enzymatic action in aldosterone synthase.
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The enzyme 4-hydroxybenzoate 3-monooxygenase, also commonly referred to as para-hydroxybenzoate hydroxylase (PHBH), is a flavoprotein belonging to the family of oxidoreductases. Specifically, it is a hydroxylase, and is one of the most studied enzymes and catalyzes reactions involved in soil detoxification, metabolism, and other biosynthetic processes. 4-hydroxybenzoate 3-monooygenase catalyzes the regioselective hydroxylation of 4-hydroxybenzoate, giving 3,4-dihydroxybenzoate as the product. The mechanism consists of the following general steps: (1) reduction of the flavin, (2) reaction of the flavin with O2, producing C4a-hydroperoxyflavin, and (3) binding and activation of the substrate, leading to product formation and release. Throughout the mechanism, the flavin changes between “open” and “closed” conformations, thus altering the substrate reaction environment.
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In biochemistry and pharmacology, GABA transaminase enzymes comprise a family of transaminases which degrade the neurotransmitter GABA. GABA transaminases include 4-aminobutyrate transaminase, which catalyzes the chemical reaction: :4-aminobutanoate (GABA) + 2-oxoglutarate succinate semialdehyde + L-glutamate and the enzyme 4-aminobutyrate—pyruvate transaminase, which catalyzes the chemical reactions: : (1) 4-aminobutanoate (GABA) + pyruvate succinate semialdehyde + L-alanine : (2) 4-aminobutanoate (GABA) + glyoxylate succinate semialdehyde + glycine GABA transaminase is targeted by multiple antiepileptic and analgesic drugs referred to as GABA transaminase inhibitors. Inhibition of this enzyme increases neuronal and synaptic GABA concentrations due to reduced metabolism and degradation of GABA. Inhibitors of the 4-aminobutyrate transaminase isoform include aminooxyacetic acid, gabaculine, phenelzine, phenylethylidenehydrazine (PEH), rosmarinic acid, valproic acid and vigabatrin.
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Mechanism of methionine gamma-lyase In enzymology, a methionine gamma-lyase () is an enzyme that catalyzes the chemical reaction :L-methionine + H2O \rightleftharpoons methanethiol + NH3 \+ 2-oxobutanoate Thus, the two substrates of this enzyme are L-methionine and H2O, whereas its 3 products are methanethiol, NH3, and 2-oxobutanoate. MGL also catalyzes α, β-elimination L-cysteine, degradation of O-substituted serine or homoserine, β- or γ-replacement, as well as deamination and γ-addition of L-vinylglycine. The reaction mechanism initially consists of the amino group of the substrate connected by a Schiff-base linkage to PLP. When a lysine residue replaces the amino group, an external aldimine is formed and hydrogens from the substrate are shifted to PLP.
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Mad1 function in SAC. Mad1 homodimer in unattached kinetochores is bound to two c-Mad2 and forms a catalytic receptor for cytozolic o-Mad2. Complex Mad1-cMadD2-oMad2 catalyzes conformational change of inactive oMad2 to the active c-Mad2 form. C-Mad2 then binds to Cdc20 and mediates APC/C inhibition and mitotic arrest.
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This family of glycosyl hydrolases (CAZY GH_65) includes vacuolar acid trehalase and maltose phosphorylases. Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. It consists of three structural domains. The C-terminal domain forms a two layered jelly roll motif.
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The dark-operative version is a completely different protein, consisting of three subunits that exhibit significant sequence similarity to the three subunits of nitrogenase, which catalyzes the formation of ammonia from dinitrogen. Yuichi FujitaDagger and Carl E. Bauer (2000). Reconstitution of Light-independent Protochlorophyllide Reductase from Purified Bchl and BchN-BchB Subunits. J. Biol. Chem.
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The RNF128 gene encodes and type 1 transmembrane protein. This protein functions as a E3 ubiquitin protein ligase that catalyzes Lys-43 and Lys-63 linked polyubiquitin chains and acts as an inhibitor of cytokine gene transcription when expressed in retrovirally transduced T cells. This protein contains 428 amino acids and has two known isoforms.
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In enzymology, a cellulose-polysulfatase () is an enzyme that catalyzes the chemical reaction of cleaving off the 2- and 3-sulfate groups of the polysulfates of cellulose and charonin. This enzyme belongs to the family of hydrolases, specifically those acting on sulfuric ester bonds. The systematic name of this enzyme class is cellulose-sulfate sulfohydrolase.
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One feature of enzymes is their high specificity. They are specific on a singular substrate, reaction or both together, that means, that the enzymes can catalyze all reactions wherein the substrate can experience. The enzyme cholesterol 7 alpha hydroxylase catalyzes the reaction that converts cholesterol into cholesterol 7 alpha hydroxylase reducing and oxidizing that molecule.
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Lactoperoxidase is a peroxidase enzyme secreted from mammary, salivary, and other mucosal glands that functions as a natural antibacterial agent. Lactoperoxidase is a member of the heme peroxidase family of enzymes. In humans, lactoperoxidase is encoded by the LPO gene. Lactoperoxidase catalyzes the oxidation of a number of inorganic and organic substrates by hydrogen peroxide.
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Aureusidin synthase is homologous to plant polyphenol oxidase, but contains certain significant modifications. Aurone synthase catalyzes the formation of aurones. Aurone synthase purified from Coreopsis grandiflora shows weak tyrosinase activity against isoliquiritigenin, but the enzyme does not react with the classic tyrosinase substrates L-tyrosine and tyramine and must therefore be classified as catechol oxidase.
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The protein encoded by this gene catalyzes the formation of inositol 1,4,5-trisphosphate and diacylglycerol from phosphatidylinositol 4,5-bisphosphate. This reaction uses calcium as a cofactor and plays an important role in the intracellular transduction of many extracellular signals in the retina. Two transcript variants encoding different isoforms have been found for this gene.
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Xylosyltransferase 1 is an enzyme that in humans is encoded by the XYLT1 gene. Xylosyltransferase (XT; EC 2.4.2.26) catalyzes the transfer of UDP-xylose to serine residues within XT recognition sequences of target proteins. Addition of this xylose to the core protein is required for the biosynthesis of the glycosaminoglycan chains characteristic of proteoglycans.
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Acylphosphatase is a small cytosolic enzyme that catalyzes the hydrolysis of the carboxyl-phosphate bond of acylphosphates. Two isoenzymes have been isolated, called muscle acylphosphatase and erythrocyte acylphosphatase, on the basis of their tissue localization. This gene encodes the erythrocyte acylphosphatase isoenzyme. Alternatively spliced transcript variants that encode different proteins were identified through data analysis.
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Nezelof syndrome is an autosomal recessive congenital immunodeficiency condition due to underdevelopment of the thymus. The defect is a type of purine nucleoside phosphorylase deficiency with inactive phosphorylase, this results in an accumulation of deoxy-GTP which inhibits ribonucleotide reductase. Ribonucleotide reductase catalyzes the formation of deoxyribonucleotides from ribonucleotides, thus, DNA replication is inhibited.
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First, citryl-coA synthetase catalyzes the formation of citryl-CoA, which is immediately cleaved by citryl-CoA lyase. It was also observed that there is significant level of protein sequence homology between the CCL protein and the C-terminal region of ATP citrate lyase (ACL), an enzyme commonly employed by the reductive TCA cycle.
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This gene encodes a mitochondrial aminoacyl- tRNA synthetase, which catalyzes the attachment of valine to tRNA(Val) for mitochondrial translation. Mutations in this gene cause combined oxidative phosphorylation deficiency-20, and are also associated with early-onset mitochondrial encephalopathies. Alternative splicing of this gene results in multiple transcript variants. [provided by RefSeq, Aug 2014].
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This ribozyme was shown to be located adjacent to the polyadenylation site and in vitro studies showed that it catalyzes a first-order reaction where its mechanism of cleavage is similar to the manganese ribozyme present in Tetrahymena group I introns. In vivo studies showed that this ribozyme is not functional with the cell.
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This is because it associated with a wide range of diseases and its inconsistency. Cystathionase catalyzes cystathionine to cysteine and α-ketobutyrate. Cysteine is an essential amino acid and its conversion from cystathionine occurs in the trans-sulfuration pathway. The availability of cysteine is necessary for the synthesis of an important anti-oxidant, glutathione.
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Nitric oxide reductase, an enzyme, catalyzes the reduction of nitric oxide (NO) to nitrous oxide (N2O). The enzyme participates in nitrogen metabolism and in the microbial defense against nitric oxide toxicity. The catalyzed reaction may be dependent on different participating small molecules: Cytochrome c (EC: 1.7.2.5, Nitric oxide reductase (cytochrome c)), NADPH (EC:1.7.
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Retracts the Cilium of the cell, which is necessary prior to mitosis of the cell. HDAC also encourages cell motility and catalyzes α-tubulin deacetylation. As a result the enzyme also encourages cancer cell metastasis. HDAC6 also affects transcription and translation by regulating the heat-shock protein 90 (Hsp90) and stress granules (SGs), respectively.
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Glucosamine—fructose-6-phosphate aminotransferase isomerizing 1 is an enzyme that in humans is encoded by the GFPT1 gene. Glutamine-fructose-6-phosphate transaminase 1 is the first and rate-limiting enzyme of the hexosamine pathway. GFAT controls the flux of glucose into the hexosamine pathway and catalyzes the formation of glucosamine 6-phosphate.
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The figure shows how, in the cholesterol biosynthesis pathway, squalene is converted to oxidosqualene, which is then converted to lanosterol by oxidosqualene cyclase. Lanosterol is a precursor to cholesterol. This final conversion occurs in many steps. Mechanistically, the enzyme catalyzes the formation of four rings along the long chain of the substrate (oxidosqualene), producing lanosterol.
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Phosphomannomutase 2 catalyzes the isomerization of mannose 6-phosphate to mannose 1-phosphate. Mannose 1-phosphate is a precursor to GDP- mannose necessary for the synthesis of dolichol-P-oligosaccharides. Mutations in the gene have been shown to cause defects in the protein glycosylation pathway which manifest as congenital disorder of glycosylation type Ia.
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The protein encoded by RPIA gene is an enzyme, which catalyzes the reversible conversion between ribose-5-phosphate and ribulose-5-phosphate in the pentose-phosphate pathway. This gene is highly conserved in most organisms. The enzyme plays an essential role in the carbohydrate metabolism. Mutations in this gene cause ribose 5-phosphate isomerase deficiency.
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A neurotransmitter sodium symporter (NSS) (TC# 2.A.22) is type of neurotransmitter transporter that catalyzes the uptake of a variety of neurotransmitters, amino acids, osmolytes and related nitrogenous substances by a solute:Na+ symport mechanism. The NSS family is a member of the APC superfamily. Its constituents have been found in bacteria, archaea and eukaryotes.
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In enzymology, a 3-β(or 20-α)-hydroxysteroid dehydrogenase () is an enzyme that catalyzes the chemical reaction :5α-androstan-3β,17β-diol + NADP+ \rightleftharpoons 17β-hydroxy-5α-androstan-3-one + NADPH + H+ This enzyme possesses the combined activities of the 3-β-hydroxysteroid dehydrogenase/Δ-5-4 isomerase and 20-α-hydroxysteroid dehydrogenase enzymes.
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Dihydrosirohydrochlorin is one of several naturally occurring tetrapyrrole macrocyclic metabolic intermediates in the biosynthesis of vitamin B12 (cobalamin). Its oxidised form, sirohydrochlorin, is precursor to sirohaem, the iron-containing prosthetic group in sulfite reductase enzymes. Further biosynthetic transformations convert sirohydrochlorin to cofactor F430 for an enzyme which catalyzes the release of methane in the final step of methanogenesis.
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This gene encodes the alpha subunit of the heterodimeric enzyme succinate coenzyme A ligase. This enzyme is targeted to the mitochondria and catalyzes the conversion of succinyl CoA and ADP or GDP to succinate and ATP or GTP. Mutations in this gene are the cause of the metabolic disorder fatal infantile lactic acidosis and mitochondrial DNA depletion.
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GFP catalyzes the oxidation and only requires molecular oxygen. GFP has been modified by changing the wavelength of light absorbed to include other colors of fluorescence. YFP or yellow fluorescent protein, BFP or blue fluorescent protein, and CFP or cyan fluorescent protein are examples of GFP variants. These variants are produced by the genetic engineering of the GFP gene.
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3-Dehydroquinate Dehydratase is an enzyme that catalyzes the third step of the shikimate pathway. The shikimate pathway is a biosynthetic pathway that allows plants, fungi, and bacteria to produce aromatic amino acids. Mammals do not have this pathway, meaning that they must obtain these essential amino acids through their diet. Aromatic Amino acids include Phenylalanine, Tyrosine, and Tryptophan.
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2'-5'-oligoadenylate synthetase 3 is an enzyme that in humans is encoded by the OAS3 gene. This gene encodes an enzyme included in the 2', 5' oligoadenylate synthase family. This enzyme is induced by interferons and catalyzes the 2', 5' oligomers of ATP. These oligos activate latent RNase L, leading to degradation of both viral and endogenous RNA.
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The solution initially turns green and then turns colorless with the depletion of dissolved oxygen. Shaking the solution introduces fresh oxygen and colors the solution green again until the oxygen is consumed. This version relies on three enzymatic reactions. First, the glucose oxidase catalyzes the oxidation of glucose in the presence of oxygen and produces hydrogen peroxide.
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Dihydropyrimidinase is an enzyme that in humans is encoded by the DPYS gene. Dihydropyrimidinase catalyzes the conversion of 5,6-dihydrouracil to 3-ureidopropionate in pyrimidine metabolism. Dihydropyrimidinase is expressed at a high level in liver and kidney as a major 2.5-kb transcript and a minor 3.8-kb transcript. Defects in the DPYS gene are linked to dihydropyrimidinuria.
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P450scc catalyzes the conversion of cholesterol to pregnenolone in three monooxygenase reactions. These involve 2 hydroxylations of the cholesterol side-chain, which generate, first, 22R-hydroxycholesterol and then 20alpha,22R-dihydroxycholesterol. The final step cleaves the bond between carbons 20 and 22, resulting in the production of pregnenolone and isocaproic aldehyde. Each monooxygenase step requires 2 electrons (reducing equivalents).
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Mannose-1-phosphate guanyltransferase beta is an enzyme that in humans is encoded by the GMPPB gene. This gene is thought to encode a GDP-mannose pyrophosphorylase. This enzyme catalyzes the reaction which converts mannose-1-phosphate and GTP to GDP-mannose which is involved in the production of N-linked oligosaccharides. The gene encodes two transcript variants.
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RNA polymerase II (also called RNAP II and Pol II) is an enzyme found in eukaryotic cells. It catalyzes the transcription of DNA to synthesize precursors of mRNA and most snRNA and microRNA. In humans, RNAP II consists of seventeen protein molecules (gene products encoded by POLR2A-L, where the proteins synthesized from 2C-, E-, and F-form homodimers).
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In enzymology, a steroid-lactonase () is an enzyme that catalyzes the chemical reaction :testololactone + H2O \rightleftharpoons testolate Thus, the two substrates of this enzyme are testololactone and H2O, whereas its product is testolate. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is testololactone lactonohydrolase.
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There are at least 2 known steps in the de novo synthesis of myo- inositol from glucose 6-phosphate. In the first step, glucose 6-phosphate is converted to D-inositol 1 monophosphate by the enzyme glucose 6 phosphate cyclase. Inositol monophosphatase catalyzes the final step in which D-inositol 1 monophosphate is dephosphorylated to form myo-inositol.
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Alpha-galactosidase (α-GAL, also known as α-GAL A; E.C. 3.2.1.22) is a glycoside hydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. Glycosidase is an important class of enzyme catalyzing many catabolic processes, including cleaving glycoproteins and glycolipids, and polysaccharides. Specifically, α-GAL catalyzes the removal of the terminal α-galactose from oligosaccharides.
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Kynurenine 3-monooxygenase is an enzyme that in humans is encoded by the KMO gene. Kynurenine 3-monooxygenase (KMO; EC 1.14.13.9) is an NADPH-dependent flavin monooxygenase that catalyzes the hydroxylation of the L-tryptophan metabolite L-kynurenine to form L-3-hydroxykynurenine.[supplied by OMIM] This is the first step in the degradation of Kyneurinine to Quinolinic acid.
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MPST catalyzes the transfer of a sulfur atom from mercaptopyruvate to sulfur acceptors like cyanides or thiol compounds. Thus it is also considered to participate in cysteine degradation. MPST generates H2S in coronary artery, mediating its effects through direct modulation of NO, namely vasodilation. This has important implications for H2S-based therapy in healthy and diseased coronary arteries.
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In enzymology, a phosphoribosylaminoimidazolecarboxamide formyltransferase (), also known by the shorter name AICAR transformylase, is an enzyme that catalyzes the chemical reaction :10-formyltetrahydrofolate + AICAR \rightleftharpoons tetrahydrofolate + FAICAR Thus, the two substrates of this enzyme are 10-formyltetrahydrofolate and AICAR, whereas its two products are tetrahydrofolate and FAICAR. This enzyme participates in purine metabolism and one carbon pool by folate.
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Tellimagrandin II is formed from pentagalloyl glucose by oxidative dehydrogenation and coupling of 2 galloyl groups. β-glucogallin: 1,2,3,4,6-pentagalloyl-β-d-glucose galloyltransferase is an enzyme found in the leaves of Rhus typhina that catalyzes the galloylation of 1,2,3,4,6-penta-O-galloyl-β-D-glucose to 3-O-digalloyl-1,2,4,6-tetra-O-galloyl-β-d-glucose (hexa-galloylglucose).
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In enzymology, a histidine-tRNA ligase () is an enzyme that catalyzes the chemical reaction :ATP + L-histidine + tRNAHis \rightleftharpoons AMP + diphosphate + L-histidyl-tRNAHis The 3 substrates of this enzyme are ATP, L-histidine, and tRNA(His), whereas its 3 products are AMP, diphosphate, and L-histidyl-tRNA(His). This enzyme participates in histidine metabolism and aminoacyl-trna biosynthesis.
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A disintegrin and metalloproteinase with thrombospondin motifs 7 (ADAMTS7) is an enzyme that in humans is encoded by the ADAMTS7 gene on chromosome 15. It is ubiquitously expressed in many tissues and cell types. This enzyme catalyzes the degradation of cartilage oligomeric matrix protein (COMP) degradation. ADAMTS7 has been associated with cancer and arthritis in multiple tissue types.
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Molybdates are widely used in catalysis. In terms of scale, the largest consumer of molybdate is as a precursor to catalysts for hydrodesulfurization, the process by which sulfur is removed from petroleum. Bismuth molybdates, nominally of the composition Bi9PMo12O52, catalyzes ammoxidation of propylene to acrylonitrile. Ferric molybdates are used industrially to catalyze the oxidation of methanol to formaldehyde.
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In addition to inhibiting gene expression, splicing ribozymes can be used to repair damaged or defective RNA. Splicing ribozymes catalyze RNA splicing, removing a section of RNA that contains a mutation and replacing it with well-functioning RNA. Existing ribozymes can also be altered in a way that changes the reaction(s) that the ribozyme catalyzes.
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The methyl group is removed later, but it serves to activate the adjacent methylene bridge facilitating its attack on the terminal carbonyl group, a reaction catalyzed by DnrD. Dnr D, the fourth ring cyclase (AAME cyclase), catalyzes an intramolecular aldol addition reaction. No cofactors are required and neither aromatization nor dehydration occurs. A simple base catalyzed mechanism is proposed.
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The protein encoded by this gene belongs to the family of P-type cation transport ATPases. This gene encodes a catalytic subunit of the ouabain- sensitive H+/K+ -ATPase that catalyzes the hydrolysis of ATP coupled with the exchange of H+ and K+ ions across the plasma membrane. It is also responsible for potassium absorption in various tissues.
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Diglyceride acyltransferase (or O-acyltransferase), DGAT, catalyzes the formation of triglycerides from diacylglycerol and Acyl-CoA. The reaction catalyzed by DGAT is considered the terminal and only committed step in triglyceride synthesis and to be essential for intestinal absorption (i.e. DGAT1) and adipose tissue formation (i.e. DGAT2). The protein is homologous to other membrane-bound O-acyltransferases.
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Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial is an enzyme that in humans is encoded by the SUCLG2 gene on chromosome 3. This gene encodes a GTP-specific beta subunit of succinyl-CoA synthetase. Succinyl-CoA synthetase catalyzes the reversible reaction involving the formation of succinyl-CoA and succinate. Alternate splicing results in multiple transcript variants.
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Citrate is structurally similar to the substrate 3-phosphoglycerate. The citrate molecule is shown in green. The suspected catalytically essential histidine residue involved in forming the phosphohistidine complex is directly to the left of the bound citrate molecule. :This enzyme is not to be confused with Bisphosphoglycerate mutase which catalyzes the conversion of 1,3-bisphosphoglycerate to 2,3-bisphosphoglycerate.
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Choi researched jasmonates, which are believed to participate in signal transduction processes between external stresses, such as wounding, pathogenic attack, or cell response by activating the defense genes. He discovered a new enzyme, (EC2.1.1.141) jasmonate carboxyl methyltransferase (JMT), which catalyzes the methylation of jasmonate to MeJA. The overexpression of the JMT gene confers resistance to pathogens.
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Several splice variants have been described that prevent this oligomerization without influencing the affinity for receptors. They nevertheless affect the composition of inhibitory synapses and can even play a role in diseases like epilepsy. The gephyrin protein is also required for insertion of molybdenum into molybdopterin. As aforementioned, gephyrin also catalyzes terminal two steps of Moco biosynthesis.
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This gene belongs to the pyrroline-5-carboxylate reductase family. The encoded mitochondrial protein catalyzes the conversion of pyrroline-5-carboxylate to proline, which is the last step in proline biosynthesis. Loss of PYCR2 does not lead to a gross defect in mitochondrial protein synthesis, but loss of function of PYCR2 leads to increased apoptosis under oxidative stress.
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Chlorination of S4N4 gives thiazyl chloride. Passing gaseous S4N4 over silver metal yields the low temperature superconductor polythiazyl or polysulfurnitride (transition temperature (0.26±0.03) K), often simply called "(SN)x". In the conversion, the silver first becomes sulfided, and the resulting Ag2S catalyzes the conversion of the S4N4 into the four-membered ring S2N2, which readily polymerizes.
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ETQ-QO links the oxidation of fatty acids and some amino acids to oxidative phosphorylation in the mitochondria. Specifically, it catalyzes the transfer of electrons from electron transferring flavoprotein (ETF) to ubiquinone, reducing it to ubiquinol. The entire sequence of transfer reactions is as follows: Acyl-CoA → Acyl-CoA dehydrogenase → ETF → ETF-QO → UQ → Complex III.
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Pyruvate dehydrogenase is an enzyme that catalyzes the reaction of pyruvate and a lipoamide to give the acetylated dihydrolipoamide and carbon dioxide. The conversion requires the coenzyme thiamine pyrophosphate. 350px Pyruvate dehydrogenase is usually encountered as a component, referred to as E1, of the pyruvate dehydrogenase complex (PDC). PDC consists of other enzymes, referred to as E2 and E3.
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It was initially considered an oxidase. It catalyzes the reduction of NO2− to NO. This tetraheme enzyme has two subunits, each containing a c-type and a d-type heme. The reduced d hemes bind nitrite and convert it to product. Cytochrome c nitrite reductase (ccNIR) is a multiheme enzyme that converts nitrite to ammonia on each active site.
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Arginase belong to the ureohydrolase family of enzymes. Arginase catalyzes the fifth and final step in the urea cycle, a series of biochemical reactions in mammals during which the body disposes of harmful ammonia. Specifically, arginase converts L-arginine into L-ornithine and urea. Mammalian arginase is active as a trimer, but some bacterial arginases are hexameric.
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Dimethylallyl pyrophosphate (DMAPP; or alternatively, dimethylallyl diphosphate (DMADP); also isoprenyl pyrophosphate) is an isoprenoid precursor. It is a product of both the mevalonate pathway and the MEP pathway of isoprenoid precursor biosynthesis. It is an isomer of isopentenyl pyrophosphate (IPP) and exists in virtually all life forms. The enzyme isopentenyl pyrophosphate isomerase catalyzes isomerization between DMAPP and IPP.
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Once the PARP-1 protein recognizes the DNA damage, it catalyzes post-transcriptional modification of PAR. PAR will be formed either as a branched or linear molecule. Branching and long-chain polymers will be more toxic to the cell than simple short polymers. The more extreme the DNA damage, the more PAR accumulates in the nucleus.
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Bacteria must synthesize folic acid because they do not have a transporter for it. Without folic acid, bacteria cannot grow and divide. Therefore, because of sulfa drugs' competitive inhibition, they are excellent antibacterial agents. An example of competitive inhibition was demonstrated experimentally for the enzyme succinic dehydrogenase, which catalyzes the oxidation of succinate to fumarate in the Krebs cycle.
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Tabersonine is a terpene indole alkaloid found in the medicinal plant Catharanthus roseus. Tabersonine is hydroxylated at the 16 position by the enzyme tabersonine 16-hydroxylase (T16H) to form 16-hydroxytabersonine.St- Pierre and De Luca (1995) A Cytochrome P-450 Monooxygenase Catalyzes the First Step in the Conversion of Tabersonine to Vindoline in Catharanthus roseus. Plant Physiology. 109(1).
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The protein is a methyltransferase that catalyzes the methylation of cytosine to 5-methylcytosine (m5C) at position 34 of intron-containing tRNA (Leu)(CAA) precursors. This modification is necessary to stabilize the anticodon-codon pairing and correctly translate the mRNA. NSUN2 is also localized on mitochondria and is capable of introducing post-transcriptional modifications in mitochondrial tRNAs .
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Enzymes are homogeneous catalysts that are essential for life but are also harnessed for industrial processes. A well-studied example is carbonic anhydrase, which catalyzes the release of CO2 into the lungs from the bloodstream. Enzymes possess properties of both homogeneous and heterogeneous catalysts. As such, they are usually regarded as a third, separate category of catalyst.
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Malate dehydrogenase () (MDH) is an enzyme that reversibly catalyzes the oxidation of malate to oxaloacetate using the reduction of NAD+ to NADH. This reaction is part of many metabolic pathways, including the citric acid cycle. Other malate dehydrogenases, which have other EC numbers and catalyze other reactions oxidizing malate, have qualified names like malate dehydrogenase (NADP+).
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In enzymology, a N-methylhydantoinase (ATP-hydrolysing) () is an enzyme that catalyzes the chemical reaction Nucleoside triphosphate-dependent 1-methylhydantoinase, a process for obtaining it and the use - United States Patent 4816393. Inventors: Siedel Joachim, Deeg Rolf, Roder Albert, Ziegenhorn Joachim, Mollering Hans, Gauhl Helmgard. Assignee: Boehringer Mannheim. Application Date: 1985-02-25. Publication Date: 1989-03-28.
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This enzyme participates in arginine and proline metabolism. This enzyme is widely expressed in bacteria, including streptococcus and actinomyces. The bacterial arginine deiminase expression could be regulated by various environmental factors. Recently, a new enzyme that catalyzes the chemical reaction :L-arginine + 2H2O \rightleftharpoons L-ornithine + 2NH3 \+ CO2 was identified in cyanobacteria which should be named as arginine dihydrolase.
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Instead of entering the PG recycling pathway, GlcN-6-P can be converted into fructose-6-phosphate by NagB. This reaction is reversible by the enzyme GlmS, an amidotransferase. The produced fructose-6-phosphate then enters the glycolysis pathway. Glycolysis catalyzes the production of pyruvate, leading to the citric acid cycle and allowing for the production of amino acids.
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Two specific enzymes participate on the carbon monoxide side of the pathway: CO Dehydrogenase and acetyl-CoA synthase. The former catalyzes the reduction of the CO2 and the latter combines the resulting CO with a methyl group to give acetyl-CoA.Paul A. Lindahl "Nickel- Carbon Bonds in Acetyl-Coenzyme A Synthases/Carbon Monoxide Dehydrogenases" Met. Ions Life Sci.
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The Calvin cycle showing the role of ribulose-1,5-bisphosphate. The enzyme ribulose (RuBisCO) catalyzes the reaction between RuBP and carbon dioxide. The product is the highly unstable six-carbon intermediate known as 3-keto-2-carboxyarabinitol 1,5-bisphosphate. This six-carbon intermediate decays virtually instantaneously into two molecules of 3-phosphoglycerate (3-PGA) (see figure).
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Inner mitochondrial membrane peptidase subunit 2 (IMMP2L) is an enzyme that in humans is encoded by the IMMP2L gene on chromosome 7. This protein catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. IMMP2L processes the nuclear encoded protein DIABLO.
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Pathogens have developed mechanisms that inactivate PAMP-induced signaling pathways through the MAPK networks. Andrea Pitzschke and her colleges claim “AvrPto and AvrPtoB interact with the FLS2 receptor and its co- receptor BAK1. AvrPtoB catalyzes the polyubiquitination and subsequent proteasome-dependent degradation of FLS2” (Pitzschke 3). AvrPto interacts with BAK1 and interrupts the binding of FLS2.
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A proposed mechanism for chorismate mutase. Clark, T., Stewart, J.D. and Ganem, B. Transition-state analogue inhibitors of chlorismate mutase. Tetrahedron 46 (1990) 731–748. © IUBMB 2001 Chorismate mutase is an intramolecular transferase and it catalyzes the conversion of chorismate to prephenate, used as a precursor for L-tyrosine and L-phenylalanine in some plants and bacteria.
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Here, a Rossmann fold domain is inserted at the C-terminal end of the TIM-barrel. Trimethylamine dehydrogenase catalyzes the conversion of trimethylamine to formaldehyde. This reaction requires both a reduced 6-S-cysteinyl Flavin mononucleotide (FMN) cofactor and a reduced iron-sulphur ([4Fe-4S]+) center. FMN is covalently bound within the C-terminal region of the β-barrel.
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Kynurenine-3-monooxygenase catalyzes the hydroxylation of -kynurenine to 3-hydroxy--kynurenine with concomitant interconversion of NADPH to NADP+. The reaction mechanism is not entirely known, but is believed to follow mechanisms related to the flavin-dependent monooxygenases. After -kynurenine binds, NADPH reduces FAD and leaves as NADP+. Oxygen then binds and creates an -kynurenine- FAD-hydroperoxide intermediate.
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The energy coupling mechanisms for proteins of the FNT family have not been extensively characterized. HCO and NO uptakes may be coupled to H+ symport. HCO efflux may be driven by the membrane potential by a uniport mechanism or by H+ antiport. FocA of E. coli catalyzes bidirectional formate transport and may function by a channel-type mechanism.
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In enzymology, a 2,5-diaminovalerate transaminase () is an enzyme that catalyzes the chemical reaction :2,5-diaminopentanoate + 2-oxoglutarate \rightleftharpoons 5-amino-2-oxopentanoate + L-glutamate Thus, the two substrates of this enzyme are 2,5-diaminopentanoate and 2-oxoglutarate, whereas its two products are 5-amino-2-oxopentanoate and L-glutamate. It employs one cofactor, pyridoxal phosphate.
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The two bioactive forms of vitamin are methylcobalamin in cytosol and adenosylcobalamin in mitochondria. Multivitamins often contain cyanocobalamin, which is presumably converted to bioactive forms in the body. Both methylcobalamin and adenosylcobalamin are commercially available as supplement pills. The MMACHC gene product catalyzes the decyanation of cyanocobalamin as well as the dealkylation of alkylcobalamins including methylcobalamin and adenosylcobalamin.
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Menaquinone, K2, includes a range of forms that are synthesized by bacteria in the gut. Vitamin K is synthesized from the molecule chorismate in a nine step conversion process. SHCHC synthase catalyzes the third step in the process.van Oostende C, Widhalm JR, Furt F, Ducluzeau AL, Basset GJC (2011) Phylloquinone (Vitamin K1): function, enzymes and genes.
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In enzymology, a pyrogallol hydroxytransferase () is an enzyme that catalyzes the chemical reaction :1,2,3,5-tetrahydroxybenzene + 1,2,3-trihydroxybenzene \rightleftharpoons 1,3,5-trihydroxybenzene + 1,2,3,5-tetrahydroxybenzene Thus, the two substrates of this enzyme are 1,2,3,5-tetrahydroxybenzene and 1,2,3-trihydroxybenzene (pyrogallol), whereas its two products are 1,3,5-trihydroxybenzene (phloroglucinol) and 1,2,3,5-tetrahydroxybenzene. This enzyme participates in benzoic acid degradation via CoA ligation.
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In enzymology, a selenate reductase () is an enzyme that catalyzes the chemical reaction :selenite + H2O + acceptor \rightleftharpoons selenate + reduced acceptor The 3 substrates of this enzyme are selenite, H2O, and acceptor, whereas its two products are selenate and reduced acceptor. This enzyme belongs to the family of oxidoreductases. The systematic name of this enzyme class is selenite:reduced acceptor oxidoreductase.
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In enzymology, a tetrachloroethene reductive dehalogenase () is an enzyme that catalyzes the chemical reaction. This is a member of reductive dehalogenase enzyme family. :trichloroethene + chloride + acceptor \rightleftharpoons tetrachloroethene + reduced acceptor The 3 substrates of this enzyme are trichloroethene, chloride, and acceptor, whereas its two products are tetrachloroethene and reduced acceptor. This enzyme belongs to the family of oxidoreductases.
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In the blood coagulation pathway, thrombin acts to convert factor XI to XIa, VIII to VIIIa, V to Va, fibrinogen to fibrin, and XIII to XIIIa. Factor XIIIa is a transglutaminase that catalyzes the formation of covalent bonds between lysine and glutamine residues in fibrin. The covalent bonds increase the stability of the fibrin clot. Thrombin interacts with thrombomodulin.
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Ceramide synthase 1 (CerS1) is a ceramide synthase that catalyzes the synthesis of C18 ceramide in a fumonisin B1-independent manner, and is primarily expressed in the brain. It can also be found in low levels in skeletal muscle and the testis. Within the cell, CerS1 is located in the endoplasmic reticulum (ER) and golgi apparatus membrane.
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Luciferase can function in two different pathways: a bioluminescence pathway and a CoA-ligase pathway. In both pathways, luciferase initially catalyzes an adenylation reaction with MgATP. However, in the CoA-ligase pathway, CoA can displace AMP to form luciferyl CoA. Fatty acyl-CoA synthetase similarly activates fatty acids with ATP, followed by displacement of AMP with CoA.
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Glycine decarboxylase is the P-protein of the glycine cleavage system in eukaryotes. The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha- amino group of glycine through its pyridoxal phosphate cofactor. Carbon dioxide is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
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In enzymology, a glutamate synthase (ferredoxin) () is an enzyme that catalyzes the chemical reaction :2 L-glutamate + 2 oxidized ferredoxin \rightleftharpoons L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+ Thus, the two substrates of this enzyme are L-glutamate and oxidized ferredoxin, whereas its 4 products are L-glutamine, 2-oxoglutarate, reduced ferredoxin, and H+.
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It has also been suggested that 9-HN is initiated by 3-hydroxy-3-methylglutaric acid (HMG). This latter theory was not supported by feeding of [3-14C] or [3,6-13C2]-HMG. It is proposed that MmpB to catalyzes the synthesis of 9-HN (Figure 5). MmpB contains a KS, KR, DH, 3 ACPs, and a thioesterase (TE) domain.
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In enzymology, a glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) () is an enzyme that catalyzes the chemical reaction :D-glyceraldehyde 3-phosphate + phosphate + NADP+ \rightleftharpoons 3-phospho-D-glyceroyl phosphate + NADPH + H+ The 3 substrates of this enzyme are D-glyceraldehyde 3-phosphate, phosphate, and NADP+, whereas its 3 products are 3-phospho-D-glyceroyl phosphate, NADPH, and H+.
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In enzymology, a nitrous oxide reductase also known as nitrogen:acceptor oxidoreductase (N2O-forming) is an enzyme that catalyzes the final step in bacterial denitrification, the reduction of nitrous oxide to dinitrogen. : N2O + 2 reduced cytochome c N2 \+ H2O + 2 cytochrome c It plays a critical role in preventing release of a potent greenhouse gas into the atmosphere.
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In enzymology, a N5-(carboxyethyl)ornithine synthase () is an enzyme that catalyzes the chemical reaction :N5-(L-1-carboxyethyl)-L-ornithine + NADP+ \+ H2O \rightleftharpoons L-ornithine + pyruvate + NADPH + H+ The 3 substrates of this enzyme are N5-(L-1-carboxyethyl)-L-ornithine, NADP+, and H2O, whereas its 4 products are L-ornithine, pyruvate, NADPH, and H+.
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Hedgehog acyltransferase (HHAT), also called skinny hedgehog homology in humans, is a human gene. The HHAT gene encodes an enzyme that catalyzes N-terminal palmitoylation of sonic hedgehog. Mutations in HHAT produce a phenotype that is similar to loss of hedgehog function. Finally the HHAT protein shares a short but significant sequence similarity to membrane-bound O-acyltransferases.
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The synthesis of histidine in E. coli is a complex pathway involving several enzymes. Synthesis begins with phosphorylation of 5-phosphoribosyl-pyrophosphate (PRPP), catalyzed by ATP-phosphoribosyl transferase. Phosphoribosyl-ATP converts to phosphoribosyl-AMP (PRAMP). His4 then catalyzes the formation of phosphoribosylformiminoAICAR-phosphate, which is then converted to phosphoribulosylformimino-AICAR-P by the His6 gene product.
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The rapid actions of ACTH include stimulation of cholesterol delivery to the mitochondria where the P450scc enzyme is located. P450scc catalyzes the first step of steroidogenesis that is cleavage of the side-chain of cholesterol. ACTH also stimulates lipoprotein uptake into cortical cells. This increases the bioavailability of cholesterol in the cells of the adrenal cortex.
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The possibility of a PEP/pyruvate transporter has also been put forward. X-ray structures of PEPCK provide insight into the structure and the mechanism of PEPCK enzymatic activity. The mitochondrial isoform of chicken liver PEPCK complexed with Mn2+, Mn2+-phosphoenolpyruvate (PEP), and Mn2+-GDP provides information about its structure and how this enzyme catalyzes reactions. Delbaere et al.
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Stearoyl–CoA (black) held in a kinked conformation by SCD1's binding pocket which determines which bond is desaturated. () Stearoyl-CoA desaturase (SCD; EC 1.14.19.1) is an iron-containing enzyme that catalyzes a rate-limiting step in the synthesis of unsaturated fatty acids. The principal product of SCD is oleic acid, which is formed by desaturation of stearic acid.
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An additional class of acyl-CoA dehydrogenase was discovered that catalyzes α,β-unsaturation reactions with steroid-CoA thioesters in certain types of bacteria. This class of ACAD was demonstrated to form α2β2 heterotetramers, rather than the usual α4 homotetramer, a protein architecture that evolved in order to accommodate a much larger steroid-CoA substrate. ACADs are classified as .
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In enzymology, an isopiperitenone Delta-isomerase () is an enzyme that catalyzes the chemical reaction :isopiperitenone \rightleftharpoons piperitenone Hence, this enzyme has one substrate, isopiperitenone, and one product, piperitenone. This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases transposing C=C bonds. The systematic name of this enzyme class is isopiperitenone Delta8-Delta4-isomerase.
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Cinnamomum subavenium is an evergreen tree from South and East Asia that can become tall. Leaves of Cinnamomum subavenium are an important spice. It is also a Chinese herb that has been suggested for use as a skin whitening agent. The plant contains substances which inhibit production of tyrosinase an enzyme which catalyzes the production of melanin.
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PM20D1 catalyzes the biosynthesis of N-fatty acyl amino acids from free fatty acids and free amino acids. Consequently PM20D1 is involved in the generation of potent bioactive lipid metabolites from two abundant cellular energy precursors. PM20D1 is involved in energy homeostasis. In mice, PM20D1 is highly expressed and secreted into the blood by brown fat.
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The protein encoded by this gene is a member of the ubiquitin- conjugating enzyme family. Ubiquitin-conjugating enzyme catalyzes the covalent attachment of ubiquitin to other proteins. This protein is a part of the large multiprotein complex, which is required for ubiquitin-mediated degradation of cell cycle G1 regulators, and for the initiation of DNA replication.
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Cytidine deaminase is an enzyme that in humans is encoded by the CDA gene. This gene encodes an enzyme involved in pyrimidine salvaging. The encoded protein forms a homotetramer that catalyzes the irreversible hydrolytic deamination of cytidine and deoxycytidine to uridine and deoxyuridine, respectively. It is one of several deaminases responsible for maintaining the cellular pyrimidine pool.
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It employs one cofactor, magnesium. Delta-cadinene synthase, a sesquiterpene cyclase, is an enzyme expressed in plants that catalyzes a cyclization reaction in terpenoid biosynthesis. The enzyme cyclizes farnesyl diphosphate to delta-cadinene and releases pyrophosphate. Delta-cadinene synthase is one of the key steps in the synthesis of gossypol, a toxic terpenoid produced in cotton seeds.
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This gene encodes a 1-phosphatidylinositol 4-kinase which catalyzes the first committed step in the biosynthesis of phosphatidylinositol 4,5-bisphosphate. The mammalian PI 4-kinases have been classified into two types, II and III, based on their molecular mass, and modulation by detergent and adenosine. Two transcript variants encoding different isoforms have been described for this gene.
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Spermidine synthase is an enzyme () that catalyzes the transfer of the propylamine group from S-adenosylmethioninamine to putrescine in the biosynthesis of spermidine. The systematic name is S-adenosyl 3-(methylthio)propylamine:putrescine 3-aminopropyltransferase and it belongs to the group of aminopropyl transferases. It does not need any cofactors. Most spermidine synthases exist in solution as dimers.
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CYP17 catalyzes two sequential reactions: (a) the conversion of pregnenolone and progesterone to their 17α-hydroxy derivatives by its 17α-hydroxylase activity, and (b) the subsequent formation of dehydroepiandrosterone (DHEA) and androstenedione, respectively, by its 17,20-lyase activity. DHEA and androstenedione are androgens and precursors of testosterone. Inhibition of CYP17 activity thus decreases circulating levels of testosterone.
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6-phosphofructokinase, muscle type is an enzyme that in humans is encoded by the PFKM gene on chromosome 12. Three phosphofructokinase isozymes exist in humans: muscle, liver and platelet. These isozymes function as subunits of the mammalian tetramer phosphofructokinase, which catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate. Tetramer composition varies depending on tissue type.
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In enzymology, a microsomal epoxide hydrolase (mEH) () is an enzyme that catalyzes the hydrolysis reaction between an epoxide and water to form a diol. 237x237px This enzyme plays a role in the uptake of bile salts within the large intestine. It functions as a Na+ dependent transporter. This enzyme participates in metabolism of xenobiotics by cytochrome p450.
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The aspartate metabolic pathway is involved in both storage of asparagine and in synthesis of aspartate-family amino acids. Homoserine dehydrogenase catalyzes an intermediate step in this nitrogen and carbon storage and utilization pathway. (Refer to figure 3). In photosynthetic organisms, glutamine, glutamate, and aspartate accumulate during the day and are used to synthesize other amino acids.
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ERG11 or Sterol 14-demethylase is a fungal cytochrome P450 enzyme originally from Saccharomyces cerevisiae, belongs to family CYP51, with the CYP Symbol CYP51F1. ERG11 catalyzes the C14-demethylation of lanosterol to 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol which is the first step of biosynthesis of the zymosterol, zymosterol will be further converted into Ergosterol.
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Synthesis and degradation of cADPR by enzymes of the CD38 family involve, respectively, the formation and the hydrolysis of the N1-glycosidic bond. In 2009, the first enzyme able to hydrolyze the phosphoanhydride linkage of cADPR, i.e. the one between the two phosphate groups, was reported. The SARM1 enzyme also catalyzes the formation of cADPR from NAD+.
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UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminephosphotransferase is an enzyme that in humans is encoded by the DPAGT1 gene. Mutations in DPAGT1 cause myasthenia. The protein encoded by this gene is an enzyme that catalyzes the first step in the dolichol-linked oligosaccharide pathway (also see Genetic pathway) for glycoprotein biosynthesis. This enzyme belongs to the glycosyltransferase family 4.
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In order to prepare the cell for a future signaling event, the calcium pathway must be tightly regulated. ITP3K seems to play an important role in termination of the signal. As mentioned, ITP3K catalyzes the phosphorylation of IP3 to make IP4. Unlike IP3, IP4 does not cause opening of calcium channels on the endoplasmic reticulum or sarcoplasmic reticulum.
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The most conserved region in all these proteins is centred on a serine residue which has been shown to participate, with a histidine and an aspartic acid residue, in a charge relay system. Such a region is also present in lipases of prokaryotic origin and in lecithin-cholesterol acyltransferase () (LCAT), which catalyzes fatty acid transfer between phosphatidylcholine and cholesterol.
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TMEJ is often described as alternative NHEJ, but differs in that it lacks a requirement for the Ku heterodimer, and it can only act on resected DNA ends. Following annealing of short (i.e., a few nucleotides) regions on the DNA overhangs, DNA polymerase theta catalyzes template-dependent DNA synthesis across the broken ends, stabilizing the paired structure.
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Choline kinase alpha is an enzyme that in humans is encoded by the CHKA gene. The major pathway for the biosynthesis of phosphatidylcholine occurs via the CDP-choline pathway. The protein encoded by this gene is the initial enzyme in the sequence and may play a regulatory role. The encoded protein also catalyzes the phosphorylation of ethanolamine.
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Chloroperoxidases are enzymes that catalyzes the chlorination of organic compounds. This enzyme combines the inorganic substrates chloride and hydrogen peroxide to produce the equivalent of Cl+, which replaces a proton in hydrocarbon substrate: :R-H + Cl− \+ H2O2 \+ H+ → R-Cl + 2 H2O The source of "Cl+" is hypochlorous acid (HOCl). Many organochlorine compounds are biosynthesized in this way.
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Ceramide glucosyltransferase is an enzyme that in humans is encoded by the UGCG gene. Glycosphingolipids (GSLs) are a group of membrane components that contain lipid and sugar moieties. They are present in essentially all animal cells and are believed to have important roles in various cellular processes. UDP-glucose ceramide glucosyltransferase catalyzes the first glycosylation step in glycosphingolipid biosynthesis.
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TunH then catalyzes the hydrolysis of UDP from UDP-N-acetyl-tunicamine. Another molecule of UDP- GlcNAc is introduced, and a β-1,1 glycosidic bond is subsequently formed, catalyzed by TunD. The resulting molecule is deacetylated by TunE. TunL and a fatty acyl-ACP ligase are used to load metabolic fatty acids onto the acyl carrier protein, TunK.
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The protein encoded by this gene is an enzyme that synthesizes the prenyl side-chain of coenzyme Q, or ubiquinone, one of the key elements in the respiratory chain. The gene product catalyzes the formation of all trans-polyprenyl pyrophosphates from isopentyl diphosphate in the assembly of polyisoprenoid side chains, the first step in coenzyme Q biosynthesis.
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N-acyl phosphatidylethanolamine phospholipase D (NAPE-PLD) is an enzyme that catalyzes the release of N-acylethanolamine (NAE) from N-acyl- phosphatidylethanolamine (NAPE). This is a major part of the process that converts ordinary lipids into chemical signals like anandamide and oleoylethanolamine. In humans, the NAPE-PLD protein is encoded by the NAPEPLD gene.See for in-depth coverage.
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The GM2 gangliosidoses are a group of three related genetic disorders that result from a deficiency of the enzyme beta-hexosaminidase. This enzyme catalyzes the biodegradation of fatty acid derivatives known as gangliosides. The diseases are better known by their individual names. Beta-hexosaminidase is a vital hydrolytic enzyme, found in the lysosomes, that breaks down lipids.
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Inositol monophosphatase 3 also known as inositol monophosphatase domain- containing protein 1 (IMPAD1) is an enzyme that in humans is encoded by the IMPAD1 gene. This gene encodes a member of the inositol monophosphatase family. The encoded protein is localized to the Golgi apparatus and catalyzes the hydrolysis of phosphoadenosine phosphate (PAP) to adenosine monophosphate (AMP).
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Common Impact is an American nonprofit organization headquartered in Boston, Massachusetts. It catalyzes a new, connected economy by aligning business and social purpose, connecting business professionals to local nonprofits that need assistance in information technology, marketing, human resources, operations and finance. Common Impact's model for social change involves social innovation, employee engagement, and corporate social responsibility.
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Nucleosome Remodeling Factor (NURF) is an ATP-dependent chromatin remodeling complex first discovered in Drosophila melanogaster (fruit fly) that catalyzes nucleosome sliding in order to regulate gene transcription. It contains an ISWI ATPase, making it part of the ISWI family of chromatin remodeling complexes. NURF is highly conserved among eukaryotes and is involved in transcriptional regulation of developmental genes.
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This gene encodes one of two non-identical subunits for ribonucleotide reductase. This reductase catalyzes the formation of deoxyribonucleotides from ribonucleotides. Synthesis of the encoded protein (M2) is regulated in a cell-cycle dependent fashion. Transcription from this gene can initiate from alternative promoters, which results in two isoforms that differ in the lengths of their N-termini.
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ADT catalyzes a reaction categorized by two major changes in the structure of the substrate, these being a decarboxylation and a dehydration; the enzyme removes a carboxyl group and a water molecule (respectively). Both potential products of this reaction (L-arogenate and phenylpyruvate) occur at or near the end of the biosynthetic pathway. Total synthesis of L-arogenate has been reported.
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The DH then catalyzes dehydration resulting in an ACP bound triketide. The triketide is then passed via the ACP of module 2 to the KS of module 3 on TylGII via docking domains. Docking domains are large proteins with relatively weak affinities (Kd ≈ 20–100 μM) that are fused to the complementary C and N terminii of interacting polyketide synthase polypeptides.
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In enzymology, a heparin-sulfate lyase () is an enzyme that catalyzes the chemical reaction :Elimination of sulfate; appears to act on linkages between N-acetyl-D-glucosamine and uronate. Product is an unsaturated sugar. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is heparin-sulfate lyase.
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In enzymology, a dihydroxy-acid dehydratase () is an enzyme that catalyzes the chemical reaction :2,3-dihydroxy-3-methylbutanoate \rightleftharpoons 3-methyl-2-oxobutanoate + H2O Hence, this enzyme has one substrate, 2,3-dihydroxy-3-methylbutanoate, and two products, 3-methyl-2-oxobutanoate (α-ketoisovaleric acid) and H2O. This enzyme participates in valine, leucine and isoleucine biosynthesis and pantothenate and coenzyme A (CoA) biosynthesis.
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Galactose oxidase (D-galactose:oxygen 6-oxidoreductase, D-galactose oxidase, beta-galactose oxidase; abbreviated GAO, GAOX, GOase; ) is an enzyme that catalyzes the oxidation of D-galactose in some species of fungi. Galactose oxidase belongs to the family of oxidoreductases. Copper ion is required as a cofactor for galactose oxidase. A remarkable feature of galactose oxidase is that it is a free radical enzyme.
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Diphtheria toxin can be proteolytically cleaved into two fragments: an N-terminal fragment A (catalytic domain), and fragment B (transmembrane and receptor binding domain). Fragment A catalyzes the NAD+ -dependent ADP- ribosylation of elongation factor 2, thereby inhibiting protein synthesis in eukaryotic cells. Fragment B binds to the cell surface receptor and facilitates the delivery of fragment A to the cytosol.
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Type II is present in the quinate pathway of fungi and the shikimate pathway of most bacteria. It catalyzes a trans-dehydration using an enolate intermediate. It is heat stable and has Km values one or two orders of magnitude higher than the Type I Km values. The best studied type I enzyme is from Escherichia coli (gene aroD) and related bacteria.
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Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA is an enzyme that in humans is encoded by the MAN1A1 gene. This gene encodes a class I mammalian Golgi 1,2-mannosidase which is a type II transmembrane protein. This protein catalyzes the removal of 3 distinct mannose residues from peptide-bound Man(9)-GlcNAc(2) oligosaccharides and belongs to family 47 of glycosyl hydrolases.
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It is stable to about 100 °C. Copper(II) hydroxide reacts with a solution of ammonia to form a deep blue solution of tetramminecopper [Cu(NH3)4]2+ complex ion. It catalyzes the oxidation of ammonia solutions in presence of dioxygen, giving rise to copper ammine nitrites, such as Cu(NO2)2(NH3)n. Copper(II) hydroxide is mildly amphoteric.
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Acetylcholinesterase (HGNC symbol ACHE; EC 3.1.1.7), also known as AChE or acetylhydrolase, is the primary cholinesterase in the body. It is an enzyme that catalyzes the breakdown of acetylcholine and of some other choline esters that function as neurotransmitters. AChE is found at mainly neuromuscular junctions and in chemical synapses of the cholinergic type, where its activity serves to terminate synaptic transmission.
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In enzymology, a 3-dehydroquinate dehydratase () is an enzyme that catalyzes the chemical reaction :3-dehydroquinate \rightleftharpoons 3-dehydroshikimate + H2O Hence, this enzyme has one substrate, 3-dehydroquinate, and two products, 3-dehydroshikimate and H2O. This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis.
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Glutamine-dependent NAD(+) synthetase is an enzyme that in humans is encoded by the NADSYN1 gene. Nicotinamide adenine dinucleotide (NAD) is a coenzyme in metabolic redox reactions, a precursor for several cell signaling molecules, and a substrate for protein posttranslational modifications. NAD synthetase (EC 6.3.5.1) catalyzes the final step in the biosynthesis of NAD from nicotinic acid adenine dinucleotide (NaAD).
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Heme oxygenase is a heme-containing member of the heat shock protein (HSP) family identified as HSP32. HO-1 is a 32kDa enzyme contains 288 amino acid residues. HO is located in the endoplasmic reticulum, though it has also been reported in the mitochondria, cell nucleus, and plasma membrane. HO catalyzes the degradation of heme to biliverdin/bilirubin, ferrous iron, and carbon monoxide.
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In enzymology, a phosphoribosyl-ATP diphosphatase () is an enzyme that catalyzes the chemical reaction :1-(5-phosphoribosyl)-ATP + H2O \rightleftharpoons 1-(5-phosphoribosyl)-AMP + diphosphate Thus, the two substrates of this enzyme are 1-(5-phosphoribosyl)-ATP and H2O, whereas its two products are 1-(5-phosphoribosyl)-AMP and diphosphate. This enzyme participates in histidine metabolism. It employs one cofactor, H+.
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SBPase has additional levels of regulation beyond the ferredoxin/thioredoxin system. Mg2+ concentration has a significant impact on the activity of SBPase and the rate of the reactions it catalyzes. SBPase is inhibited by acidic conditions (low pH). This is a large contributor to the overall inhibition of carbon fixation when the pH is low inside the stroma of the chloroplast.
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In enzymology, a phosphoserine phosphatase () is an enzyme that catalyzes the following chemical reaction: :O-phospho-L(or D)-serine + H2O \rightleftharpoons L(or D)-serine + phosphate ion This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is O-phosphoserine phosphohydrolase. This enzyme participates in glycine, serine and threonine metabolism.
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Glycerate kinase is an enzyme that catalyzes the conversion of D-glyceric acid (a.k.a. D-glycerate) to 2-phosphoglycerate. This conversion is an intermediary reaction found in several metabolic pathways, including the degradation (break-down; catabolism) of serine, as well as the breakdown of fructose. A deficiency in glycerate kinase activity leads to the accumulation of D-glyceric acid (a.k.a.
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This gene is a member of the family of dihydroxyacetone kinases, which have a protein structure distinct from other kinases. The product of this gene phosphorylates dihydroxyacetone, and also catalyzes the formation of riboflavin 4',5'-phosphate (aka cyclic FMN) from FAD. Several alternatively spliced transcript variants have been identified, but the full- length nature of only one has been determined.
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In enzymology, a 5-phytase () is an enzyme that catalyzes the chemical reaction :myo-inositol hexakisphosphate + H2O \rightleftharpoons 1L-myo- inositol 1,2,3,4,6-pentakisphosphate + phosphate myo-Inositol hexakisphosphate is also known as phytic acid. These enzymes belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is myo-inositol-hexakisphosphate 5-phosphohydrolase.
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In enzymology, an actinomycin lactonase () is an enzyme that catalyzes the chemical reaction :actinomycin + H2O \rightleftharpoons actinomycinic monolactone Thus, the two substrates of this enzyme are actinomycin and H2O, whereas its product is actinomycinic monolactone. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is actinomycin lactonohydrolase.
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Ribokinase catalyzes the conversion of -ribose to -ribose 5-phosphate. Once converted, -ribose-5-phosphate is available for the manufacturing of the amino acids tryptophan and histidine, or for use in the pentose phosphate pathway. The absorption of -ribose is 88–100% in the small intestines (up to 200 mg/kg·h). One important modification occurs at the C2' position of the ribose molecule.
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This gene encodes a protein which is a member of family 38 of the glycosyl hydrolases. The protein is located in the Golgi apparatus and catalyzes the final hydrolytic step in the asparagine-linked oligosaccharide (N-linked glycosylation) maturation pathway. Mutations in the mouse homolog of this gene have been shown to cause a systemic autoimmune disease similar to human systemic lupus erythematosus.
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ATP synthase subunit delta, mitochondrial, also known as ATP synthase F1 subunit delta or F-ATPase delta subunit is an enzyme that in humans is encoded by the ATP5F1D (formerly ATP5D) gene. This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation.
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In enzymology, a proline—tRNA ligase () is an enzyme that catalyzes the chemical reaction :ATP + L-proline + tRNAPro \rightleftharpoons AMP + diphosphate + L-prolyl-tRNAPro The 3 substrates of this enzyme are ATP, L-proline, and tRNA(Pro), whereas its 3 products are AMP, diphosphate, and L-prolyl-tRNA(Pro). This enzyme participates in arginine and proline metabolism and aminoacyl-trna biosynthesis.
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O-succinylbenzoate CoA ligase (), encoded from the menE gene in Escherichia coli, catalyzes the fifth reaction in the synthesis of menaquinone (vitamin K2). This pathway is called 1, 4-dihydroxy-2-naphthoate biosynthesis I. Vitamin K is a quinone that serves as an electron transporter during anaerobic respiration. This process of anaerobic respiration allows the bacteria to generate the energy required to survive.
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SdCPS2 catalyzes the first committed reaction in the biosynthesis of salvinorin A by producing its characteristic clerodane scaffold. A series of oxygenation, acylation and methylation reactions is then required to complete the biosynthesis of salvinorin A. Biosynthesis of Salvinorin A Similar to many plant-derived psychoactive compounds, salvinorin A is excreted via peltate glandular trichomes, which reside external to the epidermis.
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Like many platinum compounds, chloroplatinic acid is a catalyst (or precatalyst) for hydrogenation and related reactions. As first reported by John Speier and colleagues from Dow Corning, it catalyzes the addition of hydrosilanes to olefins, i.e. hydrosilylation. Early demonstration reactions used isopropanol solutions of trichlorosilane (SiHCl3) with pentenes. Prior work on the addition of silanes to alkenes required radical reactions that were inefficient.
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Many alkenes and ketones undergo hydrogenation, although conditions are forcing: 145°C (500 psi). One obstacle to the use of Shvo's catalyst in the hydrogenation of alkynes is its propensity to bind the alkyne quite tightly, forming a stable complex that gradually poisons the catalyst.Intramolecular reactions proceed as well, illustrated by the conversion of allylic alcohols to ketones. Shvo's catalyst also catalyzes dehydrogenations.
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Edema factor is a calmodulin- dependent adenylate cyclase. Adenylate cyclase catalyzes the conversion of ATP into cyclic AMP (cAMP) and pyrophosphate. The complexation of adenylate cyclase with calmodulin removes calmodulin from stimulating calcium-triggered signaling, thus inhibiting the immune response. To be specific, LF inactivates neutrophils (a type of phagocytic cell) by the process just described so they cannot phagocytose bacteria.
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Cytochrome P450 BM3 is a Prokaryote Cytochrome P450 enzyme originally from Bacillus megaterium, catalyzes the hydroxylation of several long-chain fatty acids at the ω–1 through ω–3 positions. This bacterial enzyme belongs to CYP family CYP102, with the CYP Symbol CYP102A1.This CYP family constitutes a natural fusion between the CYP domain and an NADPH-dependent cytochrome P450 reductase.
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17β-Hydroxysteroid dehydrogenase type 14 also known as 17β-HSD type 14 or 17βHSD14 is an enzyme that in humans is encoded by the HSD17B14 gene. 17βHSD14 catalyzes the stereospecific oxidation and reduction of the 17β carbon atom of androgens and estrogens using NAD(P)(H) as a cofactor. It is primarily expressed in glandular epithelial tissues of breast, ovary, and testis.
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Enoyl Coenzyme A hydratase, short chain, 1, mitochondrial, also known as ECHS1, is a human gene. The protein encoded by this gene functions in the second step of the mitochondrial fatty acid beta-oxidation pathway. It catalyzes the hydration of 2-trans-enoyl-coenzyme A (CoA) intermediates to L-3-hydroxyacyl-CoAs. The gene product is a member of the hydratase/isomerase superfamily.
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Inactivity of NAGS results in N-acetylglutamate synthase deficiency, a form of hyperammonemia. In many vertebrates, N-acetylglutamate is an essential allosteric cofactor of CPS1, the enzyme that catalyzes the first step of the urea cycle. Without NAG stimulation, CPS1 cannot convert ammonia to carbamoyl phosphate, resulting in toxic ammonia accumulation. Carbamoyl glutamate has shown promise as a possible treatment for NAGS deficiency.
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Protein disulfide isomerase, or PDI, is an enzyme in the endoplasmic reticulum (ER) in eukaryotes and the periplasm of bacteria that catalyzes the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold. This allows proteins to quickly find the correct arrangement of disulfide bonds in their fully folded state, and therefore the enzyme acts to catalyze protein folding.
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In enzymology, SEPHCHC synthase (EC ), encoded by menD gene in E. coli, is an enzyme that catalyzes the second step of menaquinone (vitamin K2) biosynthesis. The two substrates of this enzyme are 2-oxoglutarate and isochorismate. The products of this enzyme are 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate and CO2. It belongs to the transferase family.
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Slight differences in isozyme structure result in different activities for the two substrate molecules: FBP and fructose 1-phosphate. Aldolase B exhibits no preference and thus catalyzes both reactions, while aldolases A and C prefer FBP. In humans, aldolase B is encoded by the ALDOB gene located on chromosome 9. The gene is 14,500 base pairs long and contains 9 exons.
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This gene is a member of the prenyltransferase family and encodes a protein with geranylgeranyl diphosphate (GGPP) synthase activity. The enzyme catalyzes the synthesis of GGPP from farnesyl diphosphate and isopentenyl diphosphate. GGPP is an important molecule responsible for the C20-prenylation of proteins and for the regulation of a nuclear hormone receptor. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
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Enzymes are usually named by the kind of substance degraded in the reaction it catalyzes. Amylases are the enzymes that hydrolyses and reduce the molecular weight of amylose and amylopectin molecules in starch, rendering it water-soluble enough to be washed off the fabric. Effective enzymatic desizing require strict control of pH, temperature, water hardness, electrolyte addition and choice of surfactant.
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The mitochondrial dicarboxylate carrier (DIC) is an integral membrane protein encoded by the SLC25A10 gene in humans that catalyzes the transport of dicarboxylates such as malonate, malate, and succinate across the inner mitochondrial membrane in exchange for phosphate, sulfate, and thiosulfate by a simultaneous antiport mechanism, thus supplying substrates for the Krebs cycle, gluconeogenesis, urea synthesis, fatty acid synthesis, and sulfur metabolism.
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Invertase is an enzyme that catalyzes the hydrolysis (breakdown) of sucrose (table sugar) into fructose and glucose. Alternative names for invertase include , saccharase, glucosucrase, beta-h-fructosidase, beta-fructosidase, invertin, sucrase, maxinvert L 1000, fructosylinvertase, alkaline invertase, acid invertase, and the systematic name: beta-fructofuranosidase. The resulting mixture of fructose and glucose is called inverted sugar syrup. Related to invertases are sucrases.
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Lipase member H is an enzyme that in humans is encoded by the LIPH gene. This gene encodes a membrane-bound member of the mammalian triglyceride lipase family. It catalyzes the production of 2-acyl lysophosphatidic acid (LPA), which is a lipid mediator with diverse biological properties that include platelet aggregation, smooth muscle contraction, and stimulation of cell proliferation and motility.
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RNAse T catalyzes the removal of nucleotides from the 3' end of both RNA and DNA. It is inhibited by both double stranded DNA and RNA, as well as cytosine residues on the 3' end of RNA. Two cytosines at the 3' end of RNA appear to remove the activity of RNAse T entirely. This cytosine effect, however, is observed less with ssDNA.
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Pinosylvin synthase is an enzyme that catalyzes the chemical reaction 3 malonyl-CoA + cinnamoyl-CoA → 4 CoA + pinosylvin + 4 CO2 This biosynthesis is noteworthy because plant biosyntheses employing cinnamic acid as a starting point are rare compared to the more common use of p-coumaric acid. Only a few identified compounds, such as anigorufone and curcumin, use cinnamic acid as their start molecule.
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Synthesis of enediyne moiety and convergent assembly: The enediyne is synthesized by 14 enzymes encoded by NcsE to NcsE11 plus NcsF1 and NcsF2. NcsE to NcsE11 constitute another iterative type I PKS, while NcsF1 and NcsF2 have epoxide hydrolase activity. Finally, the building blocks are assembled in a convergent fashion. Ncs6 glycosyltransferase catalyzes the coupling between the enediyne core and the dNDP-deoxyaminosugar.
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URA3 is a gene on chromosome V in Saccharomyces cerevisiae (yeast). Its systematic name is YEL021W. URA3 is often used in yeast research as a "marker gene", that is, a gene to label chromosomes or plasmids. URA3 encodes Orotidine 5'-phosphate decarboxylase (ODCase), which is an enzyme that catalyzes one reaction in the synthesis of pyrimidine ribonucleotides (a component of RNA).
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The chemistry of the Antarctic polar vortex has created severe ozone depletion. The nitric acid in polar stratospheric clouds reacts with chlorofluorocarbons to form chlorine, which catalyzes the photochemical destruction of ozone. Chlorine concentrations build up during the polar winter, and the consequent ozone destruction is greatest when the sunlight returns in spring. These clouds can only form at temperatures below about .
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Serine dehydratase is mostly found in the liver and catalyzes the reaction of turning serine into pyruvate and ammonia. In a diet of increased protein, the activity of serine dehydratase is increased.Mauron, Jean; Mottu, Françoise; Spohr, Georges (1973-01-01). "Reciprocal Induction and Repression of Serine Dehydratase and Phosphoglycerate Dehydrogenase by Proteins and Dietary-Essential Amino Acids in Rat Liver".
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Delta-aminolevulinate synthase 1 also known as ALAS1 is a protein that in humans is encoded by the ALAS1 gene. ALAS1 is an aminolevulinic acid synthase. Delta-aminolevulinate synthase catalyzes the condensation of glycine with succinyl-CoA to form delta-aminolevulinic acid. This nuclear-encoded mitochondrial enzyme is the first and rate-limiting enzyme in the mammalian heme biosynthetic pathway.
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Apixaban is a highly selective, orally bioavailable, and reversible direct inhibitor of free and clot-bound factor Xa. Factor Xa catalyzes the conversion of prothrombin to thrombin, the final enzyme in the coagulation cascade that is responsible for fibrin clot formation. Apixaban has no direct effect on platelet aggregation, but by inhibiting factor Xa, it indirectly decreases clot formation induced by thrombin.
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The twister sister ribozyme (TS) is an RNA structure that catalyzes its own cleavage at a specific site. In other words, it is a self-cleaving ribozyme. The twister sister ribozyme was discovered by a bioinformatics strategy as an RNA Associated with Genes Associated with Twister and Hammerhead ribozymes, or RAGATH. The twister sister ribozyme has a possible structural similarity to twister ribozymes.
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Retinol dehydrogenase 13 (all-trans/9-cis) is a protein that in humans is encoded by the RDH13 gene. This gene encodes a mitochondrial short-chain dehydrogenase/reductase, which catalyzes the reduction and oxidation of retinoids. The encoded enzyme may function in retinoic acid production and may also protect the mitochondria against oxidative stress. Alternatively spliced transcript variants have been described.
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The acetolactate synthase (ALS) enzyme (also known as acetohydroxy acid synthase, or AHAS) is a protein found in plants and micro-organisms. ALS catalyzes the first step in the synthesis of the branched-chain amino acids (valine, leucine, and isoleucine). A human protein of yet unknown function, sharing some sequence similarity with bacterial ALS, is encoded by the ILVBL (ilvB-like) gene.
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This gene encodes a subunit that catalyzes the oxidative decarboxylation of alpha-ketoglutarate to Succinyl-CoA at its active site in the fourth step of the metabolic citric acid cycle by acting as a base to facilitate the decarboxylation. The main residues responsible for the catalysis are thought to be His 260, Phe 227, Gln685, His 729, Ser302, and His 298.
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AGM1, a characterized structure of PAGM, catalyzes the conversion of N-acetylglucosamine 6-phosphate to N-acetylglucosamine 1-phosphate. AGM1 structure was determined from Candida albicans in the apoform and complex forms with substrate and product. Like other enzymes in the superfamily, it has four domains, with two additional beta-strands in domain four and a circular permutation in domain 1.
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Tafazzin is a protein that in humans is encoded by the TAZ gene. Tafazzin is highly expressed in cardiac and skeletal muscle, and functions as a phospholipid-lysophospholipid transacylase (it belongs to phospholipid:diacylglycerol acyltransferases). It catalyzes remodeling of immature cardiolipin to its mature composition containing a predominance of tetralinoleoyl moieties. Several different isoforms of the tafazzin protein are produced from the TAZ gene.
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ReOCl3(PPh3)2 is a precursor to a variety of other oxo-, nitridio, and hydrido complexes. It converts to ReH7(PPh3)2 by a treatment with LiAlH4. ReOCl3(PPh3)2 catalyzes the selective oxidation of secondary alcohols by DMSO, producing the corresponding ketals.Pombeiro, A. J. L.; Fatima, M.; Crabtree, R. H. "Technetium and Rhenium: Inorganic & Coordination Chemistry" Encyclopedia of Inorganic Chemistry.
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Phosphofructokinase-1 (PFK-1) is one of the most important regulatory enzymes () of glycolysis. It is an allosteric enzyme made of 4 subunits and controlled by many activators and inhibitors. PFK-1 catalyzes the important "committed" step of glycolysis, the conversion of fructose 6-phosphate and ATP to fructose 1,6-bisphosphate and ADP. Glycolysis is the foundation for respiration, both anaerobic and aerobic.
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Samarium(III) oxide is used in optical and infrared absorbing glass to absorb infrared radiation. Also, it is used as a neutron absorber in control rods for nuclear power reactors. The oxide catalyzes the dehydration and dehydrogenation of primary and secondary alcohols.Catalytic properties of samarium oxide with respect to the dehydrogenation and dehydration of alcohols and the dehydrogenation of tetralin.
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In the field of enzymology, a dimethylargininase, also known as a dimethylarginine dimethylaminohydrolase (DDAH), is an enzyme that catalyzes the chemical reaction: :N-omega,N-omega'-methyl-L-arginine + H2O \rightleftharpoons dimethylamine + L-citrulline Thus, the two substrates of this enzyme are N-omega,N-omega'-methyl-L-arginine and H2O, whereas its two products are dimethylamine and L-citrulline.
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This enzyme catalyzes the first step in the degradation of PGE2 and related eicosanoids. So far, eight different mutations are known leading to a dysfunctional HPGD enzyme in PDP patients. Due to these mutations, the binding of the substrate PGE2 to HPGD is disrupted. As a result of this, PGE2 cannot be transferred into PGE-M down and remain present at high concentrations.
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Depending on the species, multiple subunits of dihydrolipoyl transacetylase enzymes can arrange together into either a cubic or dodecahedral shape. These structure then form the catalytic core of the pyruvate dehydrogenase complex which not only catalyzes the reaction that transfers an acetyl group to CoA, but also performs a crucial structural role in creating the architecture of the overall complex.
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Its steric bulk inhibits the group from participating in nucleophilic addition, such as in a Williamson ether synthesis or an SN2 reaction. Substrates that are deprotonated by potassium t-butoxide include terminal acetylenes and active methylene compounds. It is useful in dehydrohalogenation reactions. Potassium tert-butoxide catalyzes the reaction of hydrosilanes and heterocyclic compounds to give the silyl derivatives, with release of H2.
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The reaction catalyzed by transaldolase Enzymes that transfer aldehyde or ketone groups and included in EC 2.2. This category consists of various transketolases and transaldolases. Transaldolase, the namesake of aldehyde transferases, is an important part of the pentose phosphate pathway. The reaction it catalyzes consists of a transfer of a dihydroxyacetone functional group to glyceraldehyde 3-phosphate (also known as G3P).
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DHODA catalyzes the oxidation of dihydroorotate to orotate, which is part of the de novo uridine 5'-monophosphate (UMP) synthesis pathway. This oxidation is mediated by flavin mononucleotide (FMN). Here, β-sheets and extended loops enclose the active site forming a cavity, while also hosting several catalytic residues. The Methylophilus methylotrophus trimethylamine dehydrogenase () TIM barrel is an example of a complete domain insertion.
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In enzymology, a 3-demethylubiquinone-9 3-O-methyltransferase () is an enzyme that catalyzes the chemical reaction :S-adenosyl-L-methionine + 3-demethylubiquinone-9 \rightleftharpoons S-adenosyl-L-homocysteine + ubiquinone-9 Thus, the two substrates of this enzyme are S-adenosyl methionine and 3-demethylubiquinone-9, whereas its two products are S-adenosylhomocysteine and ubiquinone-9. This enzyme participates in ubiquinone biosynthesis.
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Elevated alkaline phosphatase occurs when levels of alkaline phosphatase (ALP) exceed the reference range. This group of enzymes has a low substrate specificity and catalyzes the hydrolysis of phosphate esters in a basic environment. The major function of alkaline phosphatase is transporting across cell membranes. Alkaline phosphatases are present in many human tissues, including bone, intestine, kidney, liver, placenta and white blood cells.
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Wilkinson's catalyst also catalyzes many other hydrofunctionalization reactions including hydroacylation, hydroboration, and hydrosilylation of alkenes. Hydroborations have been studied with catecholborane and pinacolborane. It is also active for the hydrosilylation of alkenes. In the presence of strong base and hydrogen, Wilkinson's catalyst forms reactive Rh(I) species with superior catalytic activities on the hydrogenation of internal alkynes and functionalized tri- substituted alkenes.
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In enzymology, a 4-hydroxybenzoyl-CoA reductase () is an enzyme found in some bacteria and archaea that catalyzes the chemical reaction :benzoyl-CoA + acceptor + H2O \rightleftharpoons 4-hydroxybenzoyl-CoA + reduced acceptor The 3 substrates of this enzyme are benzoyl-CoA, acceptor, and H2O, whereas its two products are 4-hydroxybenzoyl-CoA and reduced acceptor. This enzyme participates in benzoate degradation via coa ligation.
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Overall reaction catalysed by thymidine kinase. After creation of the dTMP molecule, another kinase, thymidylate kinase, can act upon dTMP to create the diphosphate form, dTDP. Nucleoside diphosphate kinase catalyzes production of thymidine triphosphate, dTTP, which is used in DNA synthesis. Because of this, thymidine kinase activity is closely correlated with the cell cycle and used as a tumor marker in clinical chemistry.
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AzM also may undergo glutathione- catalyzed dearylation which forms DMPDT and glutathione-conjugated mercaptomethyl benzazimide (reaction 5 in figure 2) Gutoxon, the compound that mainly causes AzM to be toxic, can also be detoxified. Gutoxon can again be detoxified with the help of CYP450. CYP450 catalyzes the oxidative cleavage of gutoxon, which than yields DMP and MMBA (reaction 6 in figure 2).
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A competitive inhibitor and substrate cannot bind to the enzyme at the same time. Often competitive inhibitors strongly resemble the real substrate of the enzyme. For example, the drug methotrexate is a competitive inhibitor of the enzyme dihydrofolate reductase, which catalyzes the reduction of dihydrofolate to tetrahydrofolate. The similarity between the structures of dihydrofolate and this drug are shown in the accompanying figure.
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In enzymology, a DAHP synthase () is an enzyme that catalyzes the chemical reaction :phosphoenolpyruvate + D-erythrose 4-phosphate + H2O \rightleftharpoons 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate The three substrates of this enzyme are phosphoenolpyruvate, D-erythrose 4-phosphate, and H2O, whereas its two products are 3-deoxy-D-arabino- hept-2-ulosonate 7-phosphate and phosphate.
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Acetyl-CoA carboxylase (ACCase) is an enzyme which catalyzes a key metabolic step in the synthesis of oils in algae. The program was the first to isolate this enzyme from a diatom. The researchers discovered the transformation system for diatoms. They wanted to know if increasing the level of ACCase activity in the cells would lead to higher oil production.
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Triosephosphate isomerase is an enzyme that in humans is encoded by the TPI1 gene. This gene encodes an enzyme, consisting of two identical proteins, which catalyzes the isomerization of glyceraldehyde 3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP) in glycolysis and gluconeogenesis. Mutations in this gene are associated with triosephosphate isomerase deficiency. Pseudogenes have been identified on chromosomes 1, 4, 6 and 7.
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GLS2 is a part of the glutaminase family. The protein encoded by this gene is a mitochondrial phosphate-activated glutaminase that catalyzes the hydrolysis of glutamine to stoichiometric amounts of glutamate and ammonia. Originally thought to be liver-specific, this protein has been found in other tissues as well. Alternative splicing results in multiple transcript variants that encode different isoforms.
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GlcNAc-1-phosphotransferase catalyzes the N-linked glycosylation of asparagine residues with a molecule called mannose-6-phosphate (M6P). M6P acts as an indicator of whether a hydrolase should be transported to the lysosome or not. Once a hydrolase indicates an M6P, it can be transported to a lysosome. Surprisingly some lysosomal enzymes are only tagged at a rate of 5% or lower.
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In enzymology, a N-acetylneuraminate 7-O(or 9-O)-acetyltransferase () is an enzyme that catalyzes the chemical reaction :acetyl-CoA + N-acetylneuraminate \rightleftharpoons CoA + N-acetyl-7-O(or 9-O)-acetylneuraminate Thus, the two substrates of this enzyme are acetyl-CoA and N-acetylneuraminate, whereas its 3 products are CoA, N-acetyl-7-O-acetylneuraminate, and N-acetyl-9-O-acetylneuraminate.
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Dihydroxyacetone kinase in complex with a non-hydrolyzable ATP analog (AMP- PNP). Coordinates from PDB ID:1UN9. In biochemistry, a kinase is an enzyme that catalyzes the transfer of phosphate groups from high-energy, phosphate- donating molecules to specific substrates. This process is known as phosphorylation, where the substrate gains a phosphate group and the high- energy ATP molecule donates a phosphate group.
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Enhancer of zeste homolog 2 (EZH2) is a histone-lysine N-methyltransferase enzyme (EC 2.1.1.43) encoded by EZH2 gene, that participates in histone methylation and, ultimately, transcriptional repression. EZH2 catalyzes the addition of methyl groups to histone H3 at lysine 27, by using the cofactor S-adenosyl-L-methionine. Methylation activity of EZH2 facilitates heterochromatin formation thereby silences gene function.
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Ribonucleic acid (RNA) functions in converting genetic information from genes into the amino acid sequences of proteins. The three universal types of RNA include transfer RNA (tRNA), messenger RNA (mRNA), and ribosomal RNA (rRNA). Messenger RNA acts to carry genetic sequence information between DNA and ribosomes, directing protein synthesis. Ribosomal RNA is a major component of the ribosome, and catalyzes peptide bond formation.
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First, chorismate is converted to anthranilate by the alpha-subunit of anthranilate synthase (ASA). Anthranilate reacts with 5-phosphoribose pyrrophosphate to produce 5-phosphoribosylanthranilate. Then this intermediate is converted to indole glycerol phosphate, which interacts with the alpha-subunit of tryptophan (TSA) synthase to yield indole. The beta-subunit of tryptophan synthase (TSB) catalyzes condensation of indole with serine, leading to tryptophan.
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For many decades the enzyme was thought to catalyze the following reaction: :NH2OH + H2O -> NO2^- + 5 H+ + 4e^- Recent work in the field, however, reveals that this enzyme catalyzes an entirely different reaction: :NH2OH -> NO + 3H+ + 3e^- Subsequent oxidation of the nitric oxide to nitrite caused by reaction with oxygen accounts for the reactivity previous described by Hooper et al.
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In enzymology, a 6,7-dihydropteridine reductase (, also Dihydrobiopterin reductase) is an enzyme that catalyzes the chemical reaction :a 5,6,7,8-tetrahydropteridine + NAD(P)+ \rightleftharpoons a 6,7-dihydropteridine + NAD(P)H + H+ The 3 substrates of this enzyme are a 5,6,7,8-tetrahydropteridine (Tetrahydrobiopterin), NAD+, and NADP+, whereas its 4 products are a 6,7-dihydropteridine (Dihydrobiopterin), NADH, NADPH, and H+. This enzyme participates in folate biosynthesis.
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In enzymology, a 2-hydroxy-1,4-benzoquinone reductase () is an enzyme that catalyzes the chemical reaction :2-hydroxy-1,4-benzoquinone + NADH + H+ \rightleftharpoons 1,2,4-trihydroxybenzene + NAD+ The 3 substrates of this enzyme are 2-hydroxy-1,4-benzoquinone, NADH, and H+, whereas its two products are 1,2,4-trihydroxybenzene and NAD+. This enzyme participates in gamma- hexachlorocyclohexane degradation and 1,4-dichlorobenzene degradation.
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In enzymology, a glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) () is an enzyme that catalyzes the chemical reaction :D-glyceraldehyde 3-phosphate + phosphate + NAD+ \rightleftharpoons 3-phospho-D-glyceroyl phosphate + NADH + H+ The 3 substrates of this enzyme are D-glyceraldehyde 3-phosphate, phosphate, and NAD+, whereas its 3 products are 3-phospho-D- glyceroyl phosphate, NADH, and H+. This enzyme participates in glycolysis / gluconeogenesis.
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Biotinidase deficiency is not due to inadequate biotin, but rather to a deficiency in the enzymes that process it. Biotinidase catalyzes the cleavage of biotin from biocytin and biotinyl- peptides (the proteolytic degradation products of each holocarboxylase) and thereby recycles biotin. It is also important in freeing biotin from dietary protein-bound biotin. General symptoms include decreased appetite and growth.
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Nicotinamide mononucleotide adenylyltransferase 3 (NMNAT3) is an enzyme that in humans is encoded by the NMNAT3 gene. NMNAT3 is the third of three protein isoforms of nicotinamide-nucleotide adenylyltransferase (NMNAT) found in humans. As with the other NMNATs, NMNAT3 is an enzyme that catalyzes nicotinamide adenine dinucleotide (NAD) synthesis. NMNAT3 levels are highest in liver, heart, skeletal muscle, and erythrocytes.
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Human red blood cell infected by the malaria parasite Plasmodium falciparum, showing a residual body with brown hemozoin. During its intraerythrocytic asexual reproduction cycle Plasmodium falciparum consumes up to 80% of the host cell hemoglobin. The digestion of hemoglobin releases monomeric α-hematin (ferriprotoporphyrin IX). This compound is toxic, since it is a pro-oxidant and catalyzes the production of reactive oxygen species.
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This gene encodes a member of the cytosolic phospholipase A2 group IV family. The enzyme catalyzes the hydrolysis of membrane phospholipids to release arachidonic acid which is subsequently metabolized into eicosanoids. Eicosanoids, including prostaglandins and leukotrienes, are lipid-based cellular hormones that regulate hemodynamics, inflammatory responses, and other intracellular pathways. The hydrolysis reaction also produces lysophospholipids that are converted into platelet- activating factor.
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Mechanism for how sucrase-isomaltase catalyzes the conversion of isomaltose to two glucose molecules This enzyme catalyses the following chemical reaction : Hydrolysis of (1->6)-alpha-D- glucosidic linkages in some oligosaccharides produced from starch and glycogen by enzyme EC 3.2.1.1. Hydrolysis uses water to cleave chemical bonds. Sucrase- isomaltase’s mechanism results in a net retention of configuration at the anomeric center.
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The chylomicron at this stage is then considered mature. Via apolipoprotein C-II, mature chylomicrons activate lipoprotein lipase (LPL), an enzyme on endothelial cells lining the blood vessels. LPL catalyzes the hydrolysis of triacylglycerol that ultimately releases glycerol and fatty acids from the chylomicrons. Glycerol and fatty acids can then be absorbed in peripheral tissues, especially adipose and muscle, for energy and storage.
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Aromatase inhibitors (AIs) are a class of drugs used in the treatment of breast cancer in postmenopausal women and gynecomastia in men. They may also be used off-label to reduce estrogen conversion when using external testosterone. They may also be used for chemoprevention in high risk women. Aromatase is the enzyme that catalyzes a key aromatization step in the synthesis of estrogen.
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DMS, a product of DMSOR, is a component of the sulfur cycle. DMS is oxidized to Methanesulfonates, which nucleate cloud condensation over open oceans, where the alternative source of nucleation, dust, is absent. Cloud formation is a key component in increasing earth's albedo and regulating atmospheric temperature, thus this enzyme and the reaction it catalyzes could prove helpful on the climate control frontier.
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In enzymology, a 16-hydroxysteroid epimerase () is an enzyme that catalyzes the chemical reaction :16alpha-hydroxysteroid \rightleftharpoons 16beta- hydroxysteroid Hence, this enzyme has one substrate, 16alpha-hydroxysteroid, and one product, 16beta-hydroxysteroid. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on other compounds. The systematic name of this enzyme class is 16-hydroxysteroid 16-epimerase.
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In enzymology, an acetoin racemase () is an enzyme that catalyzes the chemical reaction :(S)-acetoin \rightleftharpoons (R)-acetoin This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on hydroxy acids and derivatives. The systematic name of this enzyme class is acetoin racemase. This enzyme is also called acetylmethylcarbinol racemase. This enzyme participates in butanoate metabolism.
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In enzymology, a cycloeucalenol cycloisomerase () is an enzyme that catalyzes the chemical reaction :cycloeucalenol \rightleftharpoons obtusifoliol Hence, this enzyme has one substrate, cycloeucalenol, and one product, obtusifoliol. This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is cycloeucalenol lyase (cyclopropane-decyclizing). This enzyme is also called cycloeucalenol---obtusifoliol isomerase.
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Peptidyl-glycine alpha-amidating monooxygenase is an enzyme that catalyzes the conversion of glycine amides to amides and glyoxylate. The enzyme is involved in the biosynthesis of many signaling peptides and some fatty acid amides. In humans, the enzyme is encoded by the PAM gene. This transformation is achieved by conversion of a prohormone to the corresponding amide (C(O)NH2).
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Citrate is an intermediate in the TCA cycle (aka TriCarboxylic Acid cycle, or Krebs cycle, Szent-Györgyi), a central metabolic pathway for animals, plants, and bacteria. Citrate synthase catalyzes the condensation of oxaloacetate with acetyl CoA to form citrate. Citrate then acts as the substrate for aconitase and is converted into aconitic acid. The cycle ends with regeneration of oxaloacetate.
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In enzymology, an UDP-glucosamine 4-epimerase () is an enzyme that catalyzes the chemical reaction :UDP-glucosamine \rightleftharpoons UDP-galactosamine Hence, this enzyme has one substrate, UDP-glucosamine, and one product, UDP- galactosamine. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is UDP-glucosamine 4-epimerase.
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In enzymology, a maleylpyruvate isomerase () is an enzyme that catalyzes the chemical reaction :3-maleylpyruvate \rightleftharpoons 3-fumarylpyruvate Hence, this enzyme has one substrate, 3-maleylpyruvate, and one product, 3-fumarylpyruvate. This enzyme belongs to the family of isomerases, specifically cis-trans isomerases. The systematic name of this enzyme class is 3-maleylpyruvate cis-trans-isomerase. This enzyme participates in tyrosine metabolism.
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In enzymology, a maltose epimerase () is an enzyme that catalyzes the chemical reaction :alpha-maltose \rightleftharpoons beta-maltose Hence, this enzyme has one substrate, alpha-maltose, and one product, beta-maltose. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is maltose 1-epimerase.
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Calcium-transporting ATPase type 2C member 1 is an enzyme that in humans is encoded by the ATP2C1 gene. This gene encodes one of the SPCA proteins, a Ca2+ ion-transporting P-type ATPase. This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of the calcium. Defects in this gene cause Hailey-Hailey disease, an autosomal dominant disorder.
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In enzymology, a neoxanthin synthase () is an enzyme that catalyzes the chemical reaction: :violaxanthin \rightleftharpoons neoxanthin Hence, this enzyme has one substrate, violaxanthin, and one product, neoxanthin. This enzyme belongs to the family of isomerases, specifically a class of other intramolecular oxidoreductases. The systematic name of this enzyme class is violaxanthin---neoxanthin isomerase (epoxide-opening). This enzyme is also called NSY.
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This enzyme is a main control point for the regulation of gluconeogenesis. The cytosolic enzyme encoded by this gene, along with GTP, catalyzes the formation of phosphoenolpyruvate from oxaloacetate, with the release of carbon dioxide and GDP. The expression of this gene can be regulated by insulin, glucocorticoids, glucagon, cAMP, and diet. A mitochondrial isozyme of the encoded protein also has been characterized.
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The protein encoded by this gene belongs to a subfamily of the phosphotransferases. This encoded enzyme is responsible for the third and last step in L-serine formation. It catalyzes magnesium-dependent hydrolysis of L-phosphoserine and is also involved in an exchange reaction between L-serine and L-phosphoserine. Deficiency of this protein is thought to be linked to Williams syndrome.
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Glutaryl-CoA dehydrogenase (GCDH) is an enzyme encoded by the GCDH gene on chromosome 19. The protein belongs to the acyl-CoA dehydrogenase family (ACD). It catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor.
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Malachite green can also be used as a saturable absorber in dye lasers, or as a pH indicator between pH 0.2–1.8. However, this use is relatively rare. Leuco-malachite green (LMG) is used as a detection method for latent blood in forensic science. Hemoglobin catalyzes the reaction between LMG and hydrogen peroxide, converting the colorless LMG into malachite green.
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In enzymology, a tetrahydroxypteridine cycloisomerase () is an enzyme that catalyzes the chemical reaction :tetrahydroxypteridine \rightleftharpoons xanthine-8-carboxylate Hence, this enzyme has one substrate, tetrahydroxypteridine, and one product, xanthine-8-carboxylate. This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is tetrahydroxypteridine lyase (isomerizing). It employs one cofactor, NAD+.
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In enzymology, a threonine racemase () is an enzyme that catalyzes the chemical reaction :L-threonine \rightleftharpoons D-threonine Hence, this enzyme has one substrate, L-threonine, and one product, D-threonine. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is threonine racemase.
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The BCKD enzyme complex catalyzes one step in breaking down amino acids. Those amino acids being leucine, isoleucine, and valine. The BCKD enzyme complex can be found in the mitochondria, an organelle known as the powerhouse of the cell. All three amino acids can be found in protein-rich foods and when broken down, they can be used for energy.
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Calcium-dependent phospholipase A2 is an enzyme that in humans is encoded by the PLA2G5 gene. This gene is a member of the secretory phospholipase A2 family. It is located in a tightly-linked cluster of secretory phospholipase A2 genes on chromosome 1. The encoded enzyme catalyzes the hydrolysis of membrane phospholipids to generate lysophospholipids and free fatty acids including arachidonic acid.
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1-Phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-3 is an enzyme that in humans is encoded by the PLCB3 gene. The gene codes for the enzyme phospholipase C β3. The enzyme catalyzes the formation of inositol 1,4,5-trisphosphate and diacylglycerol from phosphatidylinositol 4,5-bisphosphate. This reaction uses calcium as a cofactor and plays an important role in the intracellular transduction of many extracellular signals.
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Thymidine phosphorylase () is an enzyme that is encoded by the TYMP gene and catalyzes the reaction: :thymidine + phosphate \rightleftharpoons thymine + 2-deoxy-alpha-D-ribose 1-phosphate Thymidine phosphorylase is involved in purine metabolism, pyrimidine metabolism, and other metabolic pathways. Variations in thymidine phosphorylase and the TYMP gene that encode it are associated with mitochondrial neurogastrointestinal encephalopathy (MNGIE) syndrome and bladder cancer.
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In enzymology, a lipopolysaccharide N-acetylglucosaminyltransferase () is an enzyme that catalyzes the chemical reaction :UDP-N-acetyl-D-glucosamine + lipopolysaccharide \rightleftharpoons UDP + N-acetyl-D- glucosaminyllipopolysaccharide Thus, the two substrates of this enzyme are UDP-N-acetyl-D-glucosamine and lipopolysaccharide, whereas its two products are UDP and N-acetyl-D-glucosaminyllipopolysaccharide. This enzyme participates in lipopolysaccharide biosynthesis and glycan structures - biosynthesis 2.
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NAMPT catalyzes the following chemical reaction: :nicotinamide + 5-phosphoribosyl-1-pyrophosphate (PRPP) \rightleftharpoons nicotinamide mononucleotide (NMN) + pyrophosphate (PPi) Thus, the two substrates of this enzyme are nicotinamide and 5-phosphoribosyl-1-pyrophosphate (PRRP), whereas its two products are nicotinamide mononucleotide and pyrophosphate. This enzyme belongs to the family of glycosyltransferases, to be specific, the pentosyltransferases. This enzyme participates in nicotinate and nicotinamide metabolism.
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Alpha-(1,6)-fucosyltransferase is an enzyme that in humans is encoded by the FUT8 gene. This enzyme belongs to the family of fucosyltransferases. The product of this gene catalyzes the transfer of fucose from GDP-fucose to N-linked type complex glycopeptides. This enzyme is distinct from other fucosyltransferases which catalyze alpha1-2, alpha1-3, and alpha1-4 fucose addition.
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APH(3') is primarily found in certain species of gram-positive bacteria. APH(3') catalyzes the phosphorylation of kanamycin A, a 4,6-disubstituted aminoglycoside, at the 3'-hydroxyl group. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:kanamycin 3'-O-phosphotransferase.
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In enzymology, a galactinol-raffinose galactosyltransferase () is an enzyme that catalyzes the chemical reaction :alpha-D-galactosyl-(1→3)-1D-myo-inositol + raffinose \rightleftharpoons myo-inositol + stachyose Thus, the two substrates of this enzyme are α-D-galactosyl-(1→3)-1D-myo-inositol and raffinose, whereas its two products are myo-inositol and stachyose. This enzyme participates in galactose metabolism.
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DNA primase is an enzyme involved in the replication of DNA and is a type of RNA polymerase. Primase catalyzes the synthesis of a short RNA (or DNA in some organisms) segment called a primer complementary to a ssDNA (single-stranded DNA) template. After this elongation, the RNA piece is removed by a 5' to 3' exonuclease and refilled with DNA.
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Myristicin also has potential chemoprotective properties. In mouse liver and small intestine mucosa, myristicin induced higher levels of glutathione S-transferase (GST), which catalyzes a reaction that detoxifies activated carcinogens. This indicates that myristicin may act as an inhibitor of tumorigenesis. It is still unknown how much the tendency of myristicin to induce apoptosis in cells contributes to its chemoprotective abilities.
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The oxalate anion is equivalent to two molecules of carbon dioxide to which two electrons have been added. Removal of these electrons in a redox reaction may permit liberation of carbon dioxide. An oxalate degrading enzyme is a type of enzyme that catalyzes the biodegradation of oxalate. Enzymes in this class include oxalate oxidase, oxalate decarboxylase, oxalyl-CoA decarboxylase, and formyl-CoA transferase.
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In enzymology, a D-2-hydroxyglutarate dehydrogenase () is an enzyme that catalyzes the chemical reaction :(R)-2-hydroxyglutarate + acceptor \rightleftharpoons 2-oxoglutarate + reduced acceptor Thus, the two substrates of this enzyme are (R)-2-hydroxyglutarate and acceptor, whereas its two products are 2-oxoglutarate and reduced acceptor. The enzyme activity has been confirmed in animals as well as in plants .
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Gamma-glutamyl hydrolase is an enzyme that catalyses the following chemical reaction: : Hydrolysis of a gamma-glutamyl bond This lysosomal or secreted, thiol-dependent peptidase, most active at acidic pH. In humans, gamma-glutamyl hydrolase is encoded by the GGH gene. This gene catalyzes the hydrolysis of folylpoly-gamma-glutamates and antifolylpoly-gamma-glutamates by the removal of gamma-linked polyglutamates and glutamate.
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The encoded protein interacts with the polycomb repressive complex PR-DUB which catalyzes the deubiquitination of a lysine residue of histone 2A. Haploinsufficiency of this gene is associated with a syndrome involving microcephaly, intellectual disabilities, severe speech impairment, and seizures. Alternatively spliced transcript variants have been found, but their full-length nature is not determined. [provided by RefSeq, Jul 2017].
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Reactive oxygen species (ROS) are generated in macrophages and osteoclasts from superoxide (O2−.), which forms from the action of NADPH-oxidase on oxygen (O2). They play an essential role in the function of phagocytic cells. TRAP, containing a redox active iron, catalyzes the generation of ROS through Fenton chemistry:Fenton, H.J.H., Oxidation of tartaric acid in presence of iron. J Chem Soc Trans, 1894.
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CDO is responsible for the first major step in metabolism of cysteine. CDO oxidizes to cysteine sulfinic acid (which exists predominantly in the anionic sulfinate form in vivo). Overall, CDO catalyzes the addition of dioxygen (O2) to a thiol, producing a sulfinic acid. More specifically, CDO is part of the group of non-heme iron oxygenases that employ oxygen as an electron acceptor.
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In enzymology, a 1,5-anhydro-D-fructose dehydratase () is an enzyme that catalyzes the chemical reaction :1,5-anhydro-D-fructose \rightleftharpoons 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + HO Hence, this enzyme has one substrate, 1,5-anhydro-D-fructose, and two products, 1,5-anhydro-4-deoxy-D- glycero-hex-3-en-2-ulose and HO. It catalyzes two steps in the anhydrofructose pathway process.IUBMB - Anhydrofructose Pathway This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 1,5-anhydro-D-fructose hydro-lyase (ascopyrone-M-forming). Other names in common use include 1,5-anhydro-D-fructose 4-dehydratase, 1,5-anhydro-D-fructose hydrolyase, 1,5-anhydro-D-arabino-hex-2-ulose dehydratase, AFDH, AF dehydratase, and 1,5-anhydro-D-fructose hydro-lyase.
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In enzymology, a sterol 14-demethylase () is an enzyme that catalyzes the chemical reaction :obtusifoliol + 3 O2 \+ 3 NADPH + 3 H+ \rightleftharpoons 4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + 3 NADP+ \+ 4 H2O The 4 substrates of this enzyme are obtusifoliol, O2, NADPH, and H+, whereas its 4 products are 4alpha-methyl-5alpha- ergosta-8,14,24(28)-trien-3beta-ol, formate, NADP+, and H2O. Ergosterol Although lanosterol 14α-demethylase is present in a wide variety of organisms, this enzyme is studied primarily in the context of fungi, where it plays an essential role in mediating membrane permeability. In fungi, CYP51 catalyzes the demethylation of lanosterol to create an important precursor that is eventually converted into ergosterol. This steroid then makes its way throughout the cell, where it alters the permeability and rigidity of plasma membranes much as cholesterol does in animals.
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The L2HGDH protein catalyzes the following reaction, and requires flavin adenine dinucleotide (FAD) as a co-factor: (S)-2-hydroxyglutarate + acceptor = 2-oxoglutarate + reduced acceptor. L-2-hydroxyglutarate is produced by promiscuous action of malate dehydrogenase on 2-oxoglutarate; the L2HGDH protein is thus an example of a metabolite repair enzyme because it reconverts the useless damage product L-2-hydroxyglutarate back to 2-oxoglutarate.
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GCPII is a class II membrane glycoprotein. It catalyzes the hydrolysis of N-acetylaspartylglutamate (NAAG) to glutamate and N-acetylaspartate (NAA) according to the reaction scheme to the right. Neuroscientists primarily use the term NAALADase in their studies, while those studying folate metabolism use folate hydrolase, and those studying prostate cancer or oncology, PSMA. All of which refer to the same protein glutamate carboxypeptidase II.
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The protein encoded by this gene catalyzes the formation of phosphatidylserine from either phosphatidylcholine or phosphatidylethanolamine. Phosphatidylserine synthase localizes to the mitochondria-associated membrane of the endoplasmic reticulum, where it serves a structural role as well as a signaling role. Defects in this gene are a cause of Lenz-Majewski hyperostotic dwarfism. Two transcript variants encoding different isoforms have been found for this gene.
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In enzymology, a xylose isomerase () is an enzyme that catalyzes the interconversion of D-xylose and D-xylulose. This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The isomerase has now been observed in nearly a hundred species of bacteria. Xylose-isomerases are also commonly called fructose-isomerases due to their ability to interconvert glucose and fructose.
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Crystals of a DNase protein. A deoxyribonuclease (DNase, for short) is an enzyme that catalyzes the hydrolytic cleavage of phosphodiester linkages in the DNA backbone, thus degrading DNA. Deoxyribonucleases are one type of nuclease, a generic term for enzymes capable of hydrolyzing phosphodiester bonds that link nucleotides. A wide variety of deoxyribonucleases are known, which differ in their substrate specificities, chemical mechanisms, and biological functions.
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A reductase then catalyzes the reduction of the ketone on the norsolorinic acid side-chain to yield averantin. Averantin is converted to averufin via a two different enzymes, a hydroxylase and an alcohol dehydrogenase. This will oxygenate and cyclize averantin's side chain to form the ketal in averufin. From this point on the biosynthetic pathway of aflatoxin B1 becomes much more complicated, with several major skeletal changes.
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Most of the enzymes have not been characterized and there may be several more intermediates that are still unknown. However, what is known is that averufin is oxidized by a P450-oxidase, AvfA, in a Baeyer-Villiger oxidation. This opens the ether rings and upon rearrangement versiconal acetate is formed. Now an esterase, EstA, catalyzes the hydrolysis of the acetyl, forming the primary alcohol in versiconal.
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In 2015, researchers worked with a lithium carbon fluoride battery. They incorporated a solid lithium thiophosphate electrolyte wherein the electrolyte and the cathode worked in cooperation, resulting in capacity 26 percent. Under discharge, the electrolyte generates a lithium fluoride salt that further catalyzes the electrochemical activity, converting an inactive component to an active one. More significantly, the technique was expected to substantially increase battery life.
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The different types of beta-ketoacyl-ACP synthases in type II FAS are called FabB, FabF, and FabH synthases. FabH catalyzes the quintessential ketoacyl synthase reaction with malonyl ACP and acetyl CoA. FabB and FabF catalyze other related reactions. Given that their function is necessary for proper biological function surrounding lipoprotein, phospholipid, and lipopolysaccharide synthesis, they have become a target in antibacterial drug development.
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Antizyme inhibitor 1 is a protein that in humans is encoded by the AZIN1 gene. Ornithine decarboxylase (ODC) catalyzes the conversion of ornithine to putrescine in the first and apparently rate-limiting step in polyamine biosynthesis. Ornithine decarboxylase antizymes play a role in the regulation of polyamine synthesis by binding to and inhibiting ornithine decarboxylase. The protein encoded by this gene is highly similar to ODC.
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A mutase is an enzyme of the isomerase class that catalyzes the movement of a functional group from one position to another within the same molecule. In other words, mutases catalyze intramolecular group transfers. Examples of mutases include bisphosphoglycerate mutase, which appears in red blood cells and phosphoglycerate mutase, which is an enzyme integral to glycolysis. In glycolysis, it changes 3-phosphoglycerate to 2-phosphoglycerate.
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In enzymology, a trimetaphosphatase () is an enzyme that catalyzes the chemical reaction :trimetaphosphate + H2O \rightleftharpoons triphosphate Thus, the two substrates of this enzyme are trimetaphosphate and H2O, whereas its product is triphosphate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is trimetaphosphate hydrolase. This enzyme is also called inorganic trimetaphosphatase.
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This gene encodes a microsomal beta-glucosidase that catalyzes the hydrolysis of bile acid 3-O-glucosides as endogenous compounds. Studies to determine subcellular localization of this protein in the liver indicated that the enzyme was mainly enriched in the microsomal fraction where it appeared to be confined to the endoplasmic reticulum. This putative transmembrane protein is thought to play a role in carbohydrate transport and metabolism.
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ALOX12B, like most of the other lipoxygenases, possesses dioxygenase (EC 1.13.11) activity: it catalyzes the incorporate dioxygen (i.e. molecular oxygen [O2]) into a single substrate. Owing to this activity, the enzyme adds (O2) in the form of a hydroperoxyl (HO2) residue to arachidonic acid at its 12th carbon thereby forming 12(R)-hydroperoxy-5Z,8Z,10E,14Z-icosatetraenoic acid (also termed 12(R)-HpETE or 12R-HpETE).
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In enzymology, a choline-sulfatase () is an enzyme that catalyzes the chemical reaction :choline sulfate + H2O \rightleftharpoons choline + sulfate Thus, the two substrates of this enzyme are choline sulfate and H2O, whereas its two products are choline and sulfate. This enzyme belongs to the family of hydrolases, specifically those acting on sulfuric ester bonds. The systematic name of this enzyme class is choline-sulfate sulfohydrolase.
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In enzymology, a dihydrocoumarin hydrolase () is an enzyme that catalyzes the chemical reaction :dihydrocoumarin + H2O \rightleftharpoons melilotate Thus, the two substrates of this enzyme are dihydrocoumarin and H2O, whereas its product is melilotate. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is dihydrocoumarin lactonohydrolase. This enzyme participates in fluorene degradation.
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Beta-ureidopropionase is an enzyme that in humans is encoded by the UPB1 gene. This gene encodes a protein that belongs to the CN hydrolase family. Beta- ureidopropionase catalyzes the last step in the pyrimidine degradation pathway. The pyrimidine bases uracil and thymine are degraded via the consecutive action of dihydropyrimidine dehydrogenase (DHPDH), dihydropyrimidinase (DHP) and beta-ureidopropionase (UP) to beta-alanine and beta-aminoisobutyric acid, respectively.
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Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial (MMSDH) is an enzyme that in humans is encoded by the ALDH6A1 gene. This protein belongs to the aldehyde dehydrogenases family of proteins. This enzyme plays a role in the valine and pyrimidine catabolic pathways. The product of this gene, a mitochondrial methylmalonate semialdehyde dehydrogenase, catalyzes the irreversible oxidative decarboxylation of malonate and methylmalonate semialdehydes to acetyl- and propionyl-CoA.
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Ornithine decarboxylase antizyme 2 is an enzyme that in humans is encoded by the OAZ2 gene. Ornithine decarboxylase catalyzes the conversion of ornithine to putrescine in the first and apparently rate-limiting step in polyamine biosynthesis. The ornithine decarboxylase antizymes play a role in the regulation of polyamine synthesis by binding to and inhibiting ornithine decarboxylase. Antizyme expression is auto-regulated by polyamine-enhanced translational frameshifting.
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In enzymology, a S-succinylglutathione hydrolase () is an enzyme that catalyzes the chemical reaction :S-succinylglutathione + H2O \rightleftharpoons glutathione + succinate Thus, the two substrates of this enzyme are S-succinylglutathione and H2O, whereas its two products are glutathione and succinate. This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name of this enzyme class is S-succinylglutathione hydrolase.
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In enzymology, a sugar-phosphatase () is an enzyme that catalyzes the chemical reaction :sugar phosphate + H2O \rightleftharpoons sugar + phosphate Thus, the two substrates of this enzyme are sugar phosphate and H2O, whereas its two products are sugar and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is sugar-phosphate phosphohydrolase.
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In enzymology, a monomethyl-sulfatase () is an enzyme that catalyzes the chemical reaction :monomethyl sulfate + H2O \rightleftharpoons methanol + sulfate Thus, the two substrates of this enzyme are monomethyl sulfate and H2O, whereas its two products are methanol and sulfate. This enzyme belongs to the family of hydrolases, specifically those acting on sulfuric ester bonds. The systematic name of this enzyme class is monomethyl-sulfate sulfohydrolase.
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In enzymology, a phenylacetyl-CoA hydrolase () is an enzyme that catalyzes the chemical reaction :phenylglyoxylyl-CoA + H2O \rightleftharpoons phenylglyoxylate + CoA Thus, the two substrates of this enzyme are phenylglyoxylyl-CoA and H2O, whereas its two products are phenylglyoxylate and CoA. This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name of this enzyme class is phenylglyoxylyl-CoA hydrolase.
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In enzymology, a bile-acid-CoA hydrolase () is an enzyme that catalyzes the chemical reaction :deoxycholoyl-CoA + H2O \rightleftharpoons CoA + deoxycholate Thus, the two substrates of this enzyme are deoxycholoyl-CoA and H2O, whereas its two products are CoA and deoxycholate. This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name of this enzyme class is deoxycholoyl-CoA hydrolase.
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The protein encoded by this gene is a class III pyridoxal- phosphate-dependent mitochondrial aminotransferase. It catalyzes the conversion of glyoxylate to glycine using L-alanine as the amino donor.[provided by RefSeq, Dec 2008]. ##Evidence-Data-START## Transcript exon combination :: AJ292204.1, AB193309.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support ERS025084, ERS025088 [ECO:0000350] ##Evidence- Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito.
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When there is excess glucose, coenzyme A is used in the cytosol for synthesis of fatty acids. This process is implemented by regulation of acetyl-CoA carboxylase, which catalyzes the committed step in fatty acid synthesis. Insulin stimulates acetyl-CoA carboxylase, while epinephrine and glucagon inhibit its activity. During cell starvation, coenzyme A is synthesized and transports fatty acids in the cytosol to the mitochondria.
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Para-hydroxybenzoate—polyprenyltransferase, mitochondrial is an enzyme that in humans is encoded by the COQ2 gene. CoQ (ubiquinone) serves as a redox carrier in the mitochondrial respiratory chain and is a lipid-soluble antioxidant. COQ2, or parahydroxybenzoate-polyprenyltransferase (EC 2.5.1.39), catalyzes one of the final reactions in the biosynthesis of CoQ, the prenylation of parahydroxybenzoate with an all-trans polyprenyl group (Forsgren et al.
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Pyrroline-5-carboxylate reductase 1, mitochondrial is an enzyme that in humans is encoded by the PYCR1 gene. This gene encodes an enzyme that catalyzes the NAD(P)H-dependent conversion of pyrroline-5-carboxylate to proline. This enzyme may also play a physiologic role in the generation of NADP(+) in some cell types. The protein forms a homopolymer and localizes to the mitochondrion.
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The complex is then recruited into cholesterol-rich lipid rafts. Calcium influx by itself has many negative effects on target cells, such as deregulation of cellular signalling. The adenylate cyclase domain has intrinsic enzymatic activity. Translocation of the AC domain into the cell starts the main process by which this toxin influences target cells: the AC domain binds calmodulin, and catalyzes unregulated production of cAMP from ATP.
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Calf-intestinal alkaline phosphatase (CIAP/CIP) is a type of alkaline phosphatase that catalyzes the removal of phosphate groups from the 5' end of DNA strands. This enzyme is frequently used in DNA sub-cloning, as DNA fragments that lack the 5' phosphate groups cannot ligate. This prevents recircularization of the linearized DNA vector and improves the yield of the vector containing the appropriate insert.
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In enzymology, an acetylpyruvate hydrolase () is an enzyme that catalyzes the chemical reaction :acetylpyruvate + H2O \rightleftharpoons acetate + pyruvate Thus, the two substrates of this enzyme are acetylpyruvate and H2O, whereas its two products are acetate and pyruvate. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-carbon bonds in ketonic substances. The systematic name of this enzyme class is 2,4-dioxopentanoate acetylhydrolase.
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ALT catalyzes the transfer of an amino group from L-alanine to α-ketoglutarate, the products of this reversible transamination reaction being pyruvate and L-glutamate. :L-alanine + α-ketoglutarate ⇌ pyruvate + L-glutamate 600px ALT (and all aminotransferases) require the coenzyme pyridoxal phosphate, which is converted into pyridoxamine in the first phase of the reaction, when an amino acid is converted into a keto acid.
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Alanine transaminase (ALT) is a transaminase enzyme (). It is also called alanine aminotransferase (ALAT) and was formerly called serum glutamate- pyruvate transaminase or serum glutamic-pyruvic transaminase (SGPT) and was first characterized in the mid-1950s by Arthur Karmen and colleagues. ALT is found in plasma and in various body tissues but is most common in the liver. It catalyzes the two parts of the alanine cycle.
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In enzymology, a lysine-tRNA ligase () is an enzyme that catalyzes the chemical reaction :ATP + L-lysine + tRNALys \rightleftharpoons AMP + diphosphate + L-lysyl-tRNALys The 3 substrates of this enzyme are ATP, L-lysine, and tRNA(Lys), whereas its 3 products are AMP, diphosphate, and L-lysyl-tRNA(Lys). This enzyme participates in 3 metabolic pathways: lysine biosynthesis, aminoacyl-trna biosynthesis, and amyotrophic lateral sclerosis (als).
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In enzymology, a 4-(2-carboxyphenyl)-2-oxobut-3-enoate aldolase () is an enzyme that catalyzes the chemical reaction :(3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate + H2O \rightleftharpoons 2-formylbenzoate + pyruvate Thus, the two substrates of this enzyme are (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate and H2O, whereas its two products are 2-formylbenzoate and pyruvate. This enzyme participates in naphthalene and anthracene degradation.
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In enzymology 1,4-dihydroxy-2-naphthoyl-CoA synthase () is an enzyme that catalyzes the sixth step in the biosynthesis of phylloquinone and menaquinone, the two forms of vitamin K. In E. coli, 1,4-dihydroxy-2-naphthoyl-CoA synthase, formerly known as naphthoate synthase, is encoded by menB and uses O-succinylbenzoyl-CoA as a substrate and converts it to 1,4-dihydroxy-2-naphthoyl-CoA.
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The biosynthesis of (R)-prunasin in E. cladocalyx, the sugar gum tree, has been shown to synthesize (R)-prunasin using an additional intermediate, phenylacetonitrile, using CYP706C55. The pathway proceeds similarly to the pathway in Prunus species, where the multifunctional CYP79A125 catalyzes the conversion of L-phenylalanine to phenylacetaldoxime. Then, CYP706C55 catalyzyes the dehydration of phenylacetaldoxime to phenylacetonitrile. Phenylacetonitrile is then hydroxylated by CYP71B103 to mandelonitrile.
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The Shvo catalyst is an organoruthenium compound that catalyzes the hydrogenation. The compound is of academic interest as an early example of a catalyst for transfer hydrogenation that operates by an "outer sphere mechanism.". Related derivatives are known where p-tolyl replaces some of the phenyl groups. Shvo's catalyst represents a subset of homogeneous hydrogenation catalysts that involves both metal and ligand in its mechanism.
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Choline kinase beta (CK), also known as Ethanolamine kinase (EK), Choline kinase-like protein , choline/ethanolamine kinase beta (CKEKB), or Choline/ethanolamine kinase is a protein encoded by the CHKB gene. This gene is found on chromosome 22 in humans. The encoded protein plays a key role in phospholipid biosynthesis. Choline kinase (CK) and ethanolamine kinase (EK) catalyzes the first step in phosphatidylethanolamine biosynthesis.
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In addition it, produces β-cyclodextrin glucanotransferase that catalyzes the conversion, degradation, and cyclization of starch into β-cyclodextrin. Brevibacillus brevis forms Gram-positive (variable) rods with optimal growth of 35-55 °C. It is a motile spore-former with positive catalase activity, amylase negative, casein negative, gelatinase positive, and indole negative, and most are citrate users. Some strains are capable of oxidizing carbon monoxide aerobically.
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Michael Elgin, former high school track star, now in his thirties, is floundering. He keeps life's realities at bay by having too many cocktails a few nights too often. One night, he crashes into a tree, emerges unscathed but catalyzes those who care into organizing an intervention. Michael comes home to find the group waiting: his friends, co-workers, parents, his wife, his new girlfriend.
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Nepicastat (INN, codenamed SYN117, RS-25560-197) is an inhibitor of dopamine beta-hydroxylase, an enzyme that catalyzes the conversion of dopamine to norepinephrine. It has been studied as a possible treatment for congestive heart failure, and appears to be well tolerated as such. As of 2012, clinical trials to assess nepicastat as a treatment for post-traumatic stress disorder (PTSD) and cocaine dependence have been completed.
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Creatine kinase U-type, mitochondrial, also called ubiquitous mitochondrial creatine kinase (uMtCK), is in humans encoded by CKMT1A gene. CKMT1A catalyzes the reversible transfer of the γ-phosphate group of ATP to the guanidino group of Cr to yield ADP and PCr. The impairment of CKMT1A has been reported in ischaemia, cardiomyopathy, and neurodegenerative disorders. Overexpression of CKMT1A has been reported related with several tumors.
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CRC Press, S. 113–146, : Through the Luebering–Rapoport pathway bisphosphoglycerate mutase catalyzes the transfer of a phosphoryl group from C1 to C2 of 1,3-BPG, giving 2,3-BPG. 2,3-bisphosphoglycerate, the most concentrated organophosphate in the erythrocyte, forms 3-PG by the action of bisphosphoglycerate phosphatase. The concentration of 2,3-BPG varies proportionately with the pH, since it is inhibitory to catalytic action of bisphosphoglyceromutase.
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Galactosylceramide sulfotransferase is an enzyme that in humans is encoded by the GAL3ST1 gene. Sulfonation, an important step in the metabolism of many drugs, xenobiotics, hormones, and neurotransmitters, is catalyzed by sulfotransferases. The product of this gene is galactosylceramide sulfotransferase which catalyzes the conversion between 3'-phosphoadenylylsulfate + a galactosylceramide to adenosine 3',5'-bisphosphate + galactosylceramide sulfate. Activity of this sulfotransferase is enhanced in renal cell carcinoma.
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Bile acid-CoA:amino acid N-acyltransferase is an enzyme that in humans is encoded by the BAAT gene. The protein encoded by this gene is a liver enzyme that catalyzes the transfer of the bile acid moiety from the acyl-CoA thioester to either glycine or taurine, the second step in the formation of bile acid-amino acid conjugates which serve as detergents in the gastrointestinal tract.
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An oxidase is an enzyme that catalyzes an oxidation-reduction reaction, especially one involving dioxygen (O2) as the electron acceptor. In reactions involving donation of a hydrogen atom, oxygen is reduced to water (H2O) or hydrogen peroxide (H2O2). Some oxidation reactions, such as those involving monoamine oxidase or xanthine oxidase, typically do not involve free molecular oxygen. The oxidases are a subclass of the oxidoreductases.
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3-Aminophthalic acid is a product of the oxidation of luminol. The reaction requires the presence of a catalyst. A mixture of luminol and hydrogen peroxide is used in forensics. When the mixture is sprayed on an area that contains blood, the iron in the hemoglobin in the blood catalyzes a reaction between the mixture, resulting in 3-aminophthalate which gives out light by chemiluminescence.
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Carbon dioxide (CO2) is produced in tissues as a byproduct of normal metabolism. It dissolves in the solution of blood plasma and into red blood cells (RBC), where carbonic anhydrase catalyzes its hydration to carbonic acid (H2CO3). Carbonic acid then spontaneously dissociates to form bicarbonate Ions (HCO3−) and a hydrogen ion (H+). In response to the decrease in intracellular pCO2, more CO2 passively diffuses into the cell.
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This pathway involves exchange of information between a damaged chromosome and another homologous chromosome in the same cell. It depends on the RecA protein that catalyzes strand exchange and the ADN protein that acts as a presynaptic nuclease. HR is an accurate repair process and is the preferred pathway during logarithmic growth. The NHEJ pathway for repairing double-strand breaks involves the rejoining of the broken ends.
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Anthrax lethal factor endopeptidase (, lethal toxin) is an enzyme that catalyzes the hydrolysis of mitogen-activated protein kinase kinases. This enzyme is a component of the lethal factor produced by the bacterium Bacillus anthracis. The preferred cleavage site can be denoted by BBBBxHxH, in which B denotes a basic amino acid Arg or Lys, H denotes a hydrophobic amino acid, and x is any amino acid.
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Carbonyl reductase [NADPH] 3 is an enzyme that in humans is encoded by the CBR3 gene. Carbonyl reductase 3 catalyzes the reduction of a large number of biologically and pharmacologically active carbonyl compounds to their corresponding alcohols. The enzyme is classified as a monomeric NADPH- dependent oxidoreductase. CBR3 contains three exons spanning 11.2 kilobases and is closely linked to another carbonyl reductase gene - CBR1.
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Fructose malabsorption is a digestive disorder in which absorption of fructose is impaired by deficient fructose carriers in the small intestine's enterocytes. Three autosomal recessive disorders impair fructose metabolism in liver cells. The most common is caused by mutations in the gene encoding hepatic fructokinase, an enzyme that catalyzes the first step in the metabolism of dietary fructose. Inactivation of the hepatic fructokinase results in asymptomatic fructosuria.
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Isocitrate lyase family is a family of evolutionarily related proteins. Isocitrate lyase () is an enzyme that catalyzes the conversion of isocitrate to succinate and glyoxylate. This is the first step in the glyoxylate bypass, an alternative to the tricarboxylic acid cycle in bacteria, fungi and plants. A cysteine, a histidine and a glutamate or aspartate have been found to be important for the enzyme's catalytic activity.
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FTase inhibitors have shown efficacy as anti- parasitic agents, as well. FTase is also believed to play an important role in development of progeria and various forms of cancers. Farnesyltransferase catalyzes the chemical reaction :farnesyl diphosphate + protein-cysteine \rightleftharpoons S-farnesyl protein + diphosphate Thus, the two substrates of this enzyme are farnesyl diphosphate and protein-cysteine, whereas its two products are S-farnesyl protein and diphosphate.
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Mitochondrial-processing peptidase subunit alpha is an enzyme that in humans is encoded by the PMPCA gene. This gene PMPCA encoded a protein that is a member of the peptidase M16 family. This protein is located in the mitochondrial matrix and catalyzes the cleavage of the leader peptides of precursor proteins newly imported into the mitochondria, though it only functions as part of a heterodimeric complex.
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GDP dissociates from inactive GTPases very slowly. The binding of GEFs to their GTPase substrates catalyzes the dissociation of GDP, allowing a GTP molecule to bind in its place. GEFs function to promote the dissociation of GDP. After GDP has disassociated from the GTPase, GTP generally binds in its place, as the cytosolic ratio of GTP is much higher than GDP at 10:1.
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Barnase catalyzes hydrolysis at diribonucleotide GpN sites. Cleavage occurs in two steps using a general acid-base mechanism: a cyclic intermediate is formed during the first transesterification step, which is then hydrolysed to release the cleaved RNA. The two most important residues involved in catalysis are Glu73 and His102, which are both essential for enzymatic activity. Glu73 is the general base whilst His102 is the general acid.
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The protein encoded by this gene belongs to the sulfotransferase 2 family. It is localized to the golgi membrane, and catalyzes the transfer of sulfate to the C4 hydroxyl of beta-1,4-linked N-acetylgalactosamine (GalNAc) flanked by glucuronic acid residue in chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices.
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ATP citrate lyase is responsible for catalyzing the conversion of citrate and Coenzyme A (CoA) to acetyl-CoA and oxaloacetate, driven by hydrolysis of ATP. In the presence of ATP and CoA, citrate lyase catalyzes the cleavage of citrate to yield acetyl CoA, oxaloacetate, adenosine diphosphate (ADP), and orthophosphate (Pi): :citrate + ATP + CoA → oxaloacetate + Acetyl-CoA + ADP + Pi This enzyme was formerly given the EC number 4.1.3.8.
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The LCAD enzyme catalyzes most of fatty acid beta-oxidation by forming a C2-C3 trans-double bond in the fatty acid. MCAD works on long-chain fatty acids, typically between C4 and C12-acylCoA. Fatty acid oxidation has proven to spare glucose in fasting conditions, and is also required for amino acid metabolism, which is essential for the maintenance of adequate glucose production.
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They have attracted interest because they reduce levels of the enzyme stearoyl-CoA 9-desaturase (SCD), which catalyzes the biodesaturation of stearic acid to oleic acid. At least one review indicates that CPFA are carcinogenic, co- carcinogenic, and have medical and other effects on animals;L. O. Hanus, P. Goldshlag, V. M. Dembitsky (2008). IDENTIFICATION OF CYCLOPROPYL FATTY ACIDS IN WALNUT (JUGLANS REGIA L.) OIL.
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In the beginning of the hepatitis C virus life cycle, virions bind to specific receptors on hepatocytes. The virus is internalized and the nucleocapsid is released into the cytoplasm of the hepatocyte after binding with the receptor. The NS5B protein, which is an RNA dependent RNA polymerase, catalyzes hepatitis C virus replication. The hepatitis C virus can cause acute infection but most patients are asymptomatic upon exposure.
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Heterodimer model of prion propagation Fibril model of prion propagation. The first hypothesis that tried to explain how prions replicate in a protein-only manner was the heterodimer model. This model assumed that a single PrPSc molecule binds to a single PrPC molecule and catalyzes its conversion into PrPSc. The two PrPSc molecules then come apart and can go on to convert more PrPC.
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Thiopurine methyltransferase (TPMT) catalyzes the S-methylation of thiopurines, thereby regulating the balance between cytotoxic thioguanine nucleotide and inactive metabolites in hematopoietic cells. TPMT is highly involved in 6-MP metabolism and TMPT activity and TPMT genotype is known to affect the risk of toxicity. Excessive levels of 6-MP can cause myelosuppression and myelotoxicity. Related patent litigation arose in Mayo Collaborative Services v.
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Gamma-glutamyl carboxylase is an enzyme that catalyzes the posttranslational modification of vitamin K-dependent proteins. Many of these vitamin K-dependent proteins are involved in coagulation so the function of the encoded enzyme is essential for hemostasis. Most gla domain-containing proteins depend on this carboxylation reaction for posttranslational modification. In humans, the gamma-glutamyl carboxylase enzyme is most highly expressed in the liver.
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Desacetoxyvindoline is a terpene idole alkaloid produced by the plant Catharanthus roseus. Desacetoxyvindoline is a product formed by the methylation of the nitrogen on the indole ring by the enzyme 3-hydroxy-16-methoxy-2,3-dihydrotabersonine N-methyltransferase (NMT).Liscombe, Usera and O’connor (2010) Homolog of tocopherol C methyltransferases catalyzes N methylation in anticancer alkaloid biosynthesis. Proceedings of the National Academy of Sciences. 107(44).
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Lactate has long been considered a byproduct resulting from glucose breakdown through glycolysis during anaerobic metabolism. Glycolysis requires the coenzyme NAD+, and reduces it to NADH. As a means of regenerating NAD+ to allow glycolysis to continue, lactate dehydrogenase catalyzes the conversion of pyruvate to lactate in the cytosol, oxidizing NADH to NAD+. Lactate is then transported from the peripheral tissues to the liver.
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Ribalet, François, Mauro Bastianini, Charles Vidoudez, Francesco Acri, John Berges, Adrianna Ianora, Antonio Miralto, Georg Pohnert, Giovanna Romano, Thomas Wichard, and Raffaella Casotti. "Phytoplankton Cell Lysis Associated with Polyunsaturated Aldehyde Release in the Northern Adriatic Sea." PLoS ONE 9.1 (2014): n. pag. Web. # The enzyme lipoxygenase then catalyzes the reaction of fatty acids to polyunsaturated aldehydes, which are then directly exposed to the grazing zooplankton.
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Serine dehydratase or L-serine ammonia lyase (SDH) is in the β-family of pyridoxal phosphate-dependent (PLP) enzymes. SDH is found widely in nature, but its structural and chemical properties vary greatly among species. SDH is found in yeast, bacteria, and the cytoplasm of mammalian hepatocytes. The reaction it catalyzes is the deamination of L-serine to yield pyruvate, with the release of ammonia.
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The results of immunohistochemistry and multiple sequence alignment supports the cause of MO being a mutation in EXT1 gene. However, the exact molecular mechanism of multiple osteochondroma remains unclear. The EXT1 gene encodes the endoplasmic reticulum-resident type II transmembrane glycosyltransferase, which catalyzes polymerization of heparin sulfate chain at the endoplasmic reticulum and the Golgi apparatus. Heparin sulfate regulates signal transduction during chondrocyte differentiation, ossification, and apoptosis.
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In enzymology, a 1,6-alpha-D-mannosidase () is an enzyme that catalyzes the chemical reaction of separating the 1,6-linked alpha-D-mannose residues in alpha-D-Manp-(1->6)-D-Manp. This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is 1,6-alpha-mannosyl alpha-D- mannohydrolase.
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The serine family of amino acid includes: serine, cysteine, and glycine. Most microorganisms and plants obtain the sulfur for synthesizing methionine from the amino acid cysteine. Furthermore, the conversion of serine to glycine provides the carbons needed for the biosynthesis of the methionine and histidine. During serine biosynthesis, the enzyme phosphoglycerate dehydrogenase catalyzes the initial reaction that oxidizes 3-phospho-D- glycerate to yield 3-phosphonooxypyruvate.
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Sphingosine kinase (SphK) is a conserved lipid kinase that catalyzes formation sphingosine-1-phosphate (S1P) from the precursor sphingolipid sphingosine. Sphingolipid metabolites, such as ceramide, sphingosine and sphingosine-1-phosphate, are lipid second messengers involved in diverse cellular processes. There are two forms of SphK, SphK1 and SphK2. SphK1 is found in the cytosol of eukaryotic cells, and migrates to the plasma membrane upon activation.
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However, there is a fitness cost associated with increased insecticide resistance. Pesticide-resistant codling moths are less fecund, less fertile, slower in development, lighter in weight, and have a shorter life span compared to non-resistant moths. This is believed to be caused by increase in the metabolically costly activities of oxidase and glutathione-S-transferase. Oxidase is an enzyme that catalyzes oxidation-reduction reactions.
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Angiotensin-converting enzyme (ACE) is an enzyme that catalyzes the conversion of angiotensin-I (Ang-I) to angiotensin-II (Ang-II). Ang-II is a peptide hormone which increases blood pressure by initiating vasoconstriction and aldosterone secretion. ROCK increases ACE expression and activity in pulmonary hypertension. By inhibiting ROCK with fasudil, circulating ACE and Ang-II are reduced, leading to a decrease in pulmonary vascular pressure.
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The protein encoded by this gene is a glutathione-independent prostaglandin D synthase that catalyzes the conversion of prostaglandin H2 (PGH2) to prostaglandin D2 (PGD2). PGD2 functions as a neuromodulator as well as a trophic factor in the central nervous system. PGD2 is also involved in smooth muscle contraction/relaxation and is a potent inhibitor of platelet aggregation. This gene is preferentially expressed in brain.
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Tissue plasminogen activator (abbreviated tPA or PLAT) is a protein involved in the breakdown of blood clots. It is a serine protease () found on endothelial cells, the cells that line the blood vessels. As an enzyme, it catalyzes the conversion of plasminogen to plasmin, the major enzyme responsible for clot breakdown. Human tPA has a molecular weight of ~70 kDa in the single-chain form.
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In enzymology, a 5-methyltetrahydropteroyltriglutamate—homocysteine S-methyltransferase () is an enzyme that catalyzes the chemical reaction :5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine \rightleftharpoons tetrahydropteroyltri-L-glutamate + L-methionine Thus, the two substrates of this enzyme are 5-methyltetrahydropteroyltri-L-glutamate and L-homocysteine, whereas its two products are tetrahydropteroyltri-L-glutamate and L-methionine. This enzyme participates in methionine metabolism. It has 2 cofactors: orthophosphate, and zinc.
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Mutations in the hexokinase gene can lead to a hexokinase deficiency which can cause nonspherocytic hemolytic anemia. Phosphofructokinase, or PFK, catalyzes the conversion of fructose-6-phosphate to fructose-1,6-bisphosphate and is an important point in the regulation of glycolysis. High levels of ATP, H+, and citrate inhibit PFK. If citrate levels are high, it means that glycolysis is functioning at an optimal rate.
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In enzymology, a 5beta-cholestane-3alpha,7alpha-diol 12alpha-hydroxylase () is an enzyme that catalyzes the chemical reaction :5beta- cholestane-3alpha,7alpha-diol + NADPH + H+ \+ O2 \rightleftharpoons 5beta- cholestane-3alpha,7alpha,12alpha-triol + NADP+ \+ H2O The 4 substrates of this enzyme are 5beta-cholestane-3alpha,7alpha-diol, NADPH, H+, and O2, whereas its 3 products are 5beta-cholestane-3alpha,7alpha,12alpha-triol, NADP+, and H2O.
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MLCL AT-1 catalyzes the transfer of the fatty acid chain attached to a coenzyme A molecule to an available hydroxyl group on MLCL, producing cardiolipin. This lipid remodeling is separate from the cardiolipin synthesis pathway, and is essential to maintain its unique unsaturated fatty acyl composition. MLCL AT-1 typically utilizes linoleoyl coenzyme A, preferred to oleoyl coenzyme A, which is preferred to palmitoyl coenzyme A.
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In the first, the substrate binds reversibly to the enzyme, forming the enzyme- substrate complex. This is sometimes called the Michaelis–Menten complex in their honor. The enzyme then catalyzes the chemical step in the reaction and releases the product. This work was further developed by G. E. Briggs and J. B. S. Haldane, who derived kinetic equations that are still widely used today.
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Working from the non-reducing end, β-amylase catalyzes the hydrolysis of the second α-1,4 glycosidic bond, cleaving off two glucose units (maltose) at a time. During the ripening of fruit, β-amylase breaks starch into maltose, resulting in the sweet flavor of ripe fruit. β-amylase is present in an inactive form prior to seed germination. Many microbes also produce amylase to degrade extracellular starches.
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Histamine N-methyltransferase (HNMT, HMT) is an enzyme involved in the metabolism of histamine. It is one of two enzymes involved in the metabolism of histamine in mammals, the other being diamine oxidase (DAO). HNMT catalyzes the methylation of histamine in the presence of S-adenosylmethionine (SAM-e) forming N-methylhistamine. The HNMT enzyme is present in most body tissues but is not present in serum.
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In enzymology, a 3-deoxy-8-phosphooctulonate synthase () is an enzyme that catalyzes the chemical reaction :phosphoenolpyruvate + D-arabinose 5-phosphate + H2O \rightleftharpoons 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate The 3 substrates of this enzyme are phosphoenolpyruvate, D-arabinose 5-phosphate, and H2O, whereas its two products are 2-dehydro-3-deoxy-D- octonate 8-phosphate and phosphate. This enzyme participates in lipopolysaccharide biosynthesis.
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In enzymology, a 8-amino-7-oxononanoate synthase () is an enzyme that catalyzes the chemical reaction :6-carboxyhexanoyl-CoA + L-alanine \rightleftharpoons 8-amino-7-oxononanoate + CoA + CO2 Thus, the two substrates of this enzyme are 6-carboxyhexanoyl-CoA and L-alanine, whereas its 3 products are 8-amino-7-oxononanoate, CoA, and CO2. This enzyme participates in biotin metabolism. It employs one cofactor, pyridoxal phosphate.
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RLuc is an oxidoreductase, specifically acting on single donors with O2 as the oxidant. However, this enzyme appears to be unrelated from most other luciferases that act on coelenterazine, such as those from copepods. RLuc catalyzes the chemical reaction Coelenterazine + O2 \rightleftharpoons coelenteramide + CO2 \+ hν In the process, coelenterazine is oxidized with a concurrent loss of CO2, and a photon of blue light is emitted.
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This gene encodes a DNA topoisomerase, an enzyme that controls and alters the topologic states of DNA during transcription. This enzyme catalyzes the transient breaking and rejoining of a single strand of DNA which lets the broken strand rotate around the intact strand, thus altering the topology of DNA. This gene is localized to chromosome 20 and has pseudogenes which reside on chromosomes 1 and 22.
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Alanine dehydrogenase () is an enzyme that catalyzes the chemical reaction :L-alanine + H2O + NAD+ \rightleftharpoons pyruvate + NH3 \+ NADH + H+ The 2 substrates of this enzyme are L-alanine, water, and nicotinamide adenine dinucleotide+ because water is 55M and does not change, whereas its 4 products are pyruvate, ammonia, NADH, and hydrogen ion. This enzyme participates in taurine and hypotaurine metabolism and reductive carboxylate cycle ( fixation).
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In enzymology, a L-aminoadipate-semialdehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction :L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O \rightleftharpoons L-2-aminoadipate + NAD(P)H + H+ The 4 substrates of this enzyme are L-2-aminoadipate 6-semialdehyde, NAD+, NADP+, and H2O, whereas its 4 products are L-2-aminoadipate, NADH, NADPH, and H+. This enzyme participates in lysine biosynthesis and biodegradation.
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GPX1 is ubiquitously expressed in many tissues, where it protects cells from oxidative stress. Within cells, it localizes to the cytoplasm and mitochondria. As a glutathione peroxidase, GPx1 functions in the detoxification of hydrogen peroxide, specifically by catalyzing the reduction of hydrogen peroxide to water. The glutathione peroxidase also catalyzes the reduction of other organic hydroperoxides, such as lipid peroxides, to the corresponding alcohols.
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In enzymology, a pyruvate synthase () is an enzyme that catalyzes the interconversion of pyruvate and acetyl-CoA. It is also called pyruvate:ferredoxin oxidoreductase (PFOR). The relevant equilibrium catalysed by PFOR is: :pyruvate + CoA + oxidized ferredoxin \rightleftharpoons acetyl- CoA + CO2 \+ reduced ferredoxin The 3 substrates of this enzyme are pyruvate, CoA, and oxidized ferredoxin, whereas its 3 products are acetyl-CoA, CO2, and reduced ferredoxin.
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DNA (cytosine-5)-methyltransferase 3A is an enzyme that catalyzes the transfer of methyl groups to specific CpG structures in DNA, a process called DNA methylation. The enzyme is encoded in humans by the DNMT3A gene. This enzyme is responsible for de novo DNA methylation. Such function is to be distinguished from maintenance DNA methylation which ensures the fidelity of replication of inherited epigenetic patterns.
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8-Amino-7-oxopelargonic acid synthase is a pyridoxal 5'-phosphate enzyme. The pimeloyl-CoA could be produced by a modified fatty acid pathway involving a malonyl thioester as the starter. 7,8-Diaminopelargonic acid (DAPA) aminotransferase is unusual in using S-adenosyl methionine (SAM) as the NH2 donor. Dethiobiotin synthetase catalyzes the formation of the ureido ring via a DAPA carbamate activated with ATP.
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EZH2 is the catalytic subunit of Polycomb Repressor Complex 2 (PRC2) which catalyzes methylation of histone H3 at lysine 27 (H3K27me) and mediates gene silencing of target genes via local chromatin reorganization. EZH2 protein is up-regulated in numerous cancers. EZH2 mRNA is up-regulated, on average, 7.5-fold in breast cancer, and between 40% to 75% of breast cancers have over-expressed EZH2 protein.
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In enzymology, a N-methyl-L-amino-acid oxidase () is an enzyme that catalyzes the chemical reaction :an N-methyl-L-amino acid + H2O + O2 \rightleftharpoons an L-amino acid + formaldehyde + H2O2 The 3 substrates of this enzyme are N-methyl-L-amino acid, H2O, and O2, whereas its 3 products are L-amino acid, formaldehyde, and H2O2. It has 2 cofactors: FAD, and Flavoprotein.
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LIG1 encodes DNA ligase I, which functions in DNA replication and the base excision repair process. Eukaryotic DNA ligase 1 catalyzes a reaction that is chemically universal to all ligases. DNA ligase 1 utilizes adenosine triphosphate (ATP) to catalyze the energetically favorable ligation events in both DNA replication and repair. During the synthesis phase (S-phase) of the eukaryotic cell cycle, DNA replication occurs.
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The adenylation activity is catalyzed by the bifunctional adenylyltransferase/adenylyl removal (AT/AR) enzyme. Glutamine and a regulatory protein called PII act together to stimulate adenylation. The regulation of proline biosynthesis can depend on the initial controlling step through negative feedback inhibition. In E. coli, proline allosterically inhibits Glutamate 5-kinase which catalyzes the reaction from L-glutamate to an unstable intermediate L-γ-Glutamyl phosphate.
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Squalene synthase EC (farnesyl-diphosphate farnesyltransferase) (SQS) and Phytoene synthase EC (PSY) are enzymes that share a number of functional similarities. These similarities are also reflected in their primary structure. In particular three well conserved regions are shared by SQS and PSY; they could be involved in substrate binding and/or the catalytic mechanism. SQS catalyzes the conversion of two molecules of farnesyl diphosphate (FPP) into squalene.
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Vacuolar ATPases (V-ATPase) regulate the pH of the subcellular compartments found within the endosomal membrane system. V-ATPases are multiprotein complexes composed of two functional domains, a V0 domain, and a V1 domain. The V1 domain catalyzes the hydrolysis of ATP in order to power the pumping of protons through the V0 channel, which spans the lipid bilayer of endosomal compartments.Guillard, Mailys, et al.
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3-oxo-5α-steroid 4-dehydrogenase 2 is an enzyme that in humans is encoded by the SRD5A2 gene. It is one of three forms of 5α-reductase. Steroid 5α-reductase catalyzes the conversion of the male sex hormone testosterone into the more potent androgen, dihydrotestosterone. This gene encodes a microsomal protein expressed at high levels in androgen-sensitive tissues such as the prostate.
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DMSO reductase is a molybdenum-containing enzyme that catalyzes reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS). This enzyme serves as the terminal reductase under anaerobic conditions in some bacteria, with DMSO being the terminal electron acceptor. During the course of the reaction, the oxygen atom in DMSO is transferred to molybdenum, and then reduced to water. The reaction catalyzed by DMSO reductase.
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DMSO reductase (DMSOR) and other members of the DMSO reductase family are unique to bacteria and archaea. Enzymes of this family in anaerobic oxidative phosphorylation and inorganic- donor-based lithotrophic respiration. These enzymes have been engineered to degrade oxoanions. DMSOR catalyzes the transfer of two electrons and one oxygen atom in the reaction: The active site of DMSOR contains molybdenum, which is otherwise rare in biology.
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Acyl-CoA dehydrogenase, C-2 to C-3 short chain is an enzyme that in humans is encoded by the ACADS gene. This gene encodes a tetrameric mitochondrial flavoprotein, which is a member of the acyl-CoA dehydrogenase family. This enzyme catalyzes the initial step of the mitochondrial fatty acid beta- oxidation pathway. The ACADS gene associated with short-chain acyl-coenzyme A dehydrogenase deficiency.
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In enzymology, an aconitate Delta-isomerase () is an enzyme that catalyzes the chemical reaction :trans-aconitate \rightleftharpoons cis-aconitate Hence, this enzyme has one substrate, trans-aconitate, and one product, cis- aconitate. This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases transposing C=C bonds. The systematic name of this enzyme class is aconitate Delta2-Delta3-isomerase. This enzyme is also called aconitate isomerase.
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In enzymology, an allantoin racemase () is an enzyme that catalyzes the chemical reaction :(S)(+)-allantoin \rightleftharpoons (R)(-)-allantoin Hence, this enzyme has one substrate, (S)(+)-allantoin, and one product, (R)(-)-allantoin. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on other compounds. The systematic name of this enzyme class is allantoin racemase. This enzyme participates in purine metabolism.
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Compared to the BPPS of Salvia officinalis, LaBPPS showed several differences in amino acid sequence, and the products it catalyzes: in detail, the carbocation intermediates are more stable in LaBPPS than in regular BPPS, leading to a different efficiency of converting GPP into BPP. Given the novelty of LaBPP discovery, further research on this will most likely be of significant use to the perfume and fragrance industry.
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In enzymology, a chalcone isomerase () is an enzyme that catalyzes the chemical reaction :a chalcone \rightleftharpoons a flavanone Hence, this enzyme has one substrate, a chalcone, and one product, a flavanone. This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is flavanone lyase (decyclizing). This enzyme is also called chalcone-flavanone isomerase.
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Ecto-5-prime-nucleotidase (5-prime-ribonucleotide phosphohydrolase; EC 3.1.3.5) catalyzes the conversion at neutral pH of purine 5-prime mononucleotides to nucleosides, the preferred substrate being AMP. The enzyme consists of a dimer of 2 identical 70-kD subunits bound by a glycosyl phosphatidyl inositol linkage to the external face of the plasma membrane. The enzyme is used as a marker of lymphocyte differentiation.
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In enzymology, an ent-copalyl diphosphate synthase () is an enzyme that catalyzes the chemical reaction: The partial cyclization of geranylgeranyl pyrophosphate to ent-copalyl pyrophosphate is catalyzed by ent-copalyl diphosphate synthase. Hence, this enzyme has one substrate, geranylgeranyl pyrophosphate, and one product, ent-copalyl pyrophosphate. This enzyme participates in gibberellin biosynthesis. This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases.
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In enzymology, a proline racemase () is an enzyme that catalyzes the chemical reaction :L-proline \rightleftharpoons D-proline Hence, this enzyme has two substrates, L- and D-proline, and two products, D- and L- proline. This enzyme belongs to the family of proline racemases acting on free amino acids. The systematic name of this enzyme class is proline racemase. This enzyme participates in arginine and proline metabolism.
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In enzymology, a copalyl diphosphate synthase () is an enzyme that catalyzes the chemical reaction :geranylgeranyl diphosphate \rightleftharpoons (+)-copalyl diphosphate Hence, this enzyme has one substrate, geranylgeranyl diphosphate, and one product, (+)-copalyl diphosphate. This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is (+)-copalyl-diphosphate lyase (decyclizing). This enzyme participates in diterpenoid biosynthesis.
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In enzymology, a lysine racemase () is an enzyme that catalyzes the chemical reaction :L-lysine ⇌ D-lysine Hence, this enzyme has one substrate, L-lysine, and one product, D-lysine. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is lysine racemase. This enzyme participates in lysine degradation.
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In enzymology, a lysolecithin acylmutase () is an enzyme that catalyzes the chemical reaction :2-lysolecithin \rightleftharpoons 3-lysolecithin Hence, this enzyme has one substrate, 2-lysolecithin, and one product, 3-lysolecithin. This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring acyl groups. The systematic name of this enzyme class is lysolecithin 2,3-acylmutase. This enzyme is also called lysolecithin migratase.
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In enzymology, a methionine racemase () is an enzyme that catalyzes the chemical reaction :L-methionine \rightleftharpoons D-methionine Hence, this enzyme has one substrate, L-methionine, and one product, D-methionine. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is methionine racemase. It employs one cofactor, pyridoxal phosphate.
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In enzymology, a methylitaconate Delta-isomerase () is an enzyme that catalyzes the chemical reaction :methylitaconate \rightleftharpoons 2,3-dimethylmaleate Hence, this enzyme has one substrate, methylitaconate, and one product, 2,3-dimethylmaleate. This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases transposing C=C bonds. The systematic name of this enzyme class is methylitaconate Delta2-Delta3-isomerase. This enzyme is also called methylitaconate isomerase.
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PIAS3 protein also functions as a SUMO (small ubiquitin-like modifier)-E3 ligase which catalyzes the covalent attachment of a SUMO protein to specific target substrates. It directly binds to several transcription factors and either blocks or enhances their activity. Alternatively spliced transcript variants of this gene have been identified, but the full-length nature of some of these variants has not been determined.
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The protein encoded by this gene catalyzes the formation of inositol 1,4,5-trisphosphate and diacylglycerol from phosphatidylinositol 4,5-bisphosphate. This reaction uses calcium as a cofactor and plays an important role in the intracellular transduction of many extracellular signals. This gene is activated by two G-protein alpha subunits, alpha-q and alpha-11. Two transcript variants encoding different isoforms have been found for this gene.
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The primase domain catalyzes the synthesis of short oligoribonucleotides. These oligoribonucleotides, called primers, are complementary to the template strand and used to initiate DNA replication. In T7 system, primase domain of one subunit interacts with primase domain of adjacent subunit. This interaction between primase domains acts as a brake to stop helicase when needed, which ensure the leading stand synthesis in-pace with lagging stand synthesis.
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NAD-dependent malic enzyme, mitochondrial is a protein that in humans is encoded by the ME2 gene. This gene encodes a mitochondrial NAD-dependent malic enzyme, a homotetrameric protein, that catalyzes the oxidative decarboxylation of malate to pyruvate. It had previously been weakly linked to a syndrome known as Friedreich ataxia that has since been shown to be the result of mutation in a completely different gene.
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Phenylalanine ammonia lyase can perform different functions in different species. It is found mainly in some plants and fungi (i.e. yeast). In fungal and yeast cells, PAL plays an important catabolic role, generating carbon and nitrogen. In plants it is a key biosynthetic enzyme that catalyzes the first step in the synthesis of a variety of polyphenyl compounds and is mainly involved in defense mechanisms.
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Catalyzes the first step in the synthesis of DIMBOA, forming indole from indole-3-glycerol phosphate. The enzyme is called indole-3-glycerol phosphate lyase, chloroplast, EC 4.1.2.8 and is located in the chloroplast. The X-ray structure of BX1 protein has been resolved and compared with bacterial TSA (tryptophan synthase alpha subunit, Kulik et al. 2005). Three homologs of the BX1 protein occur in maize.
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Ornithine aminotransferase (OAT) is an enzyme which is encoded in human by the OAT gene located on chromosome 10. The OAT involved in the ultimate formation of the non-essential amino acid proline from the amino acid ornithine. Ornithine aminotransferase forms the initial intermediate in this process. It catalyzes the reverse reaction as well, and is therefore essential in creating ornithine from the starting substrate proline.
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In enzymology, an indolepyruvate C-methyltransferase () is an enzyme that catalyzes the chemical reaction :S-adenosyl-L-methionine + (indol-3-yl)pyruvate \rightleftharpoons S-adenosyl-L-homocysteine + (3S)-3-(indol-3-yl)-3-oxobutanoate Thus, the two substrates of this enzyme are S-adenosyl methionine and (indol-3-yl)pyruvate, whereas its two products are S-adenosylhomocysteine and (3S)-3-(indol-3-yl)-3-oxobutanoate.
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Ioffe, David and Kampf, Arieh (2002) "Bromine, Organic Compounds" in Kirk-Othmer Encyclopedia of Chemical Technology. John Wiley & Sons. . Organobromides are the most common organohalides in nature, even though the concentration of bromide is only 0.3% of that for chloride in sea water, because of the easy oxidation of bromide to the equivalent of Br+, a potent electrophile. The enzyme bromoperoxidase catalyzes this reaction.
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In enzymology, a styrene-oxide isomerase () is an enzyme that catalyzes the chemical reaction :styrene oxide \rightleftharpoons phenylacetaldehyde Hence, this enzyme has one substrate, styrene oxide, and one product, phenylacetaldehyde. This enzyme belongs to the family of isomerases, specifically a class of other intramolecular oxidoreductases. The systematic name of this enzyme class is styrene-oxide isomerase (epoxide-cleaving). This enzyme is also called SOI.
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The proposed RPE65 O-alkyl cleavage mechanism. The residues shown are, clockwise from top left - Phe103, Thr147, His313, His527, His180, His241, and Glu148. RPE65 catalyzes the conversion of all-trans-retinyl ester to 11-cis-retinol through a proposed SN1 O-alkyl bond cleavage. RPE65's combination of an O-alkyl ester cleavage, geometric isomerization, and water addition is currently thought to be unique in biology.
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In enzymology, an ethanolamine ammonia-lyase () is an enzyme that catalyzes the chemical reaction :ethanolamine \rightleftharpoons acetaldehyde + NH3 Hence, this enzyme has one substrate, ethanolamine, and two products, acetaldehyde and NH3. This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is ethanolamine ammonia-lyase (acetaldehyde-forming). This enzyme is also called ethanolamine deaminase.
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This gene encodes adenylyl cyclase 6, which is a membrane-associated enzyme and catalyzes the formation of the secondary messenger cyclic adenosine monophosphate (cAMP). The expression of this gene is found in normal thyroid and brain tissues, as well as some tumors; and its expression is significantly higher in one hyperfunctioning thyroid tumor than in normal thyroid tissue. Alternative splicing generates 2 transcript variants.
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The gene codes for the enzyme phospholipase C β2. The enzyme catalyzes the formation of inositol 1,4,5-trisphosphate and diacylglycerol from phosphatidylinositol 4,5-bisphosphate. This reaction uses calcium as a cofactor and plays an important role in the intracellular transduction of many extracellular signals. This gene is activated by two G-protein alpha subunits, alpha-q and alpha-11, as well as G-beta gamma subunits.
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In enzymology, a DNA beta-glucosyltransferase () is an enzyme that catalyzes the chemical reaction in which a beta-D-glucosyl residue is transferred from UDP-glucose to an hydroxymethylcytosine residue in DNA. It is analogous to the enzyme DNA alpha-glucosyltransferase. This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:DNA beta-D-glucosyltransferase.
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In enzymology, a limonoid glucosyltransferase () is an enzyme that catalyzes the chemical reaction :UDP-glucose + limonin \rightleftharpoons glucosyl- limonin + UDP Thus, the two substrates of this enzyme are UDP-glucose and limonin, whereas its two products are glucosyl-limonin and UDP. This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is uridine diphosphoglucose-limonoid glucosyltransferase.
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XJ-0461, originally designated Warbot Defect B-54296, nicknamed Clank, is an escaped robot from Chairman Drek's robot plant on planet Quartu. After a high-speed chase, he crashes near a plateau on planet Veldin and catalyzes Ratchet's adventure. Clank has many attachments including a helipack, thrusterpack, and hydropack. Under certain circumstances, he can grow into a giant form to fight much larger enemies.
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In enzymology, an UDP-N-acetylglucosamine diphosphorylase () is an enzyme that catalyzes the chemical reaction :UTP + N-acetyl-alpha-D-glucosamine 1-phosphate \rightleftharpoons diphosphate + UDP-N-acetyl-D-glucosamine Thus, the two substrates of this enzyme are UTP and[N-acetyl-alpha-D-glucosamine 1-phosphate, whereas its two products are diphosphate and UDP-N-acetyl-D- glucosamine. This enzyme participates in aminosugars metabolism.
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PGDS protein is a protein that in humans is encoded by the HPGDS gene. Prostaglandin-D synthase is a sigma class glutathione-S-transferase family member. The enzyme catalyzes the conversion of PGH2 to PGD2 and plays a role in the production of prostanoids in the immune system and mast cells. The presence of this enzyme can be used to identify the differentiation stage of human megakaryocytes.
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3-dehydrosphinganine reductase catalyzes the chemical reaction: :sphinganine + NADP+ \rightleftharpoons 3-dehydrosphinganine + NADPH + H+ Thus, the two substrates of this enzyme are sphinganine and NADP+, whereas its 3 products are 3-dehydrosphinganine, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in sphingolipid metabolism.
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In enzymology and molecular biology, a holo-[acyl-carrier-protein] synthase (ACPS, ) is an enzyme that catalyzes the chemical reaction: :CoA-[4'-phosphopantetheine] + apo-acyl carrier protein \rightleftharpoons adenosine 3',5'-bisphosphate + holo-acyl carrier protein This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. It is also known as 4'-phosphopantetheinyl transferase after the group it transfers.
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In enzymology, a 13-hydroxydocosanoate 13-beta-glucosyltransferase () is an enzyme that catalyzes the chemical reaction. This reaction is part of biosynthesis. Extracts for research are frequently obtained from Candida yeasts. :UDP-glucose + 13-hydroxydocosanoate \rightleftharpoons UDP + 13-beta- D-glucosyloxydocosanoate Thus, the two substrates of this enzyme are UDP- glucose and 13-hydroxydocosanoate, whereas its two products are UDP and 13-beta-D-glucosyloxydocosanoate.
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Serine palmitoyltransferase, long chain base subunit 2, also known as SPTLC2, is a protein which in humans is encoded by the SPTLC2 gene. This gene encodes a long chain base subunit of serine palmitoyltransferase. Serine palmitoyltransferase, which consists of two different subunits, is the initial enzyme in sphingolipid biosynthesis. It catalyzes the pyridoxal 5'-phosphate dependent condensation of L-serine and palmitoyl CoA to 3-oxosphinganine.
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Ornithine decarboxylase antizyme is an enzyme that in humans is encoded by the OAZ1 gene. Ornithine decarboxylase catalyzes the conversion of ornithine to putrescine in the first and apparently rate-limiting step in polyamine biosynthesis. The ornithine decarboxylase antizymes play a role in the regulation of polyamine synthesis by binding to and inhibiting ornithine decarboxylase. Antizyme expression is auto-regulated by polyamine-enhanced translational frameshifting.
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In a metabolic or genetic pathway, enzymes catalyze a series of reactions. Each enzyme is regulated or mediated by one gene through its RNA and protein products. At each phase in the pathway, enzyme activity catalyzes a reaction in which a precursor molecule (the substrate) is transformed into its next intermediate state. Failure of the metabolic pathway leads to accumulation of the substrate, with possible harmful effects.
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24-Dehydrocholesterol reductase is a protein that in humans is encoded by the DHCR24 gene. This gene encodes a flavin adenine dinucleotide (FAD)-dependent oxidoreductase, which catalyzes the reduction of the delta-24 double bond of sterol intermediates during cholesterol biosynthesis. The protein contains a leader sequence that directs it to the endoplasmic reticulum membrane. Missense mutations in this gene have been associated with desmosterolosis.
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This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. These enzymes catalyze the conversion of aldehydes and ketones to their corresponding alcohols by utilizing NADH and/or NADPH as cofactors. The enzymes display overlapping but distinct substrate specificity. This enzyme catalyzes the bioreduction of chlordecone, a toxic organochlorine pesticide, to chlordecone alcohol in liver.
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P-type ATPases have a single catalytic subunit of 70 - 140 kDa. The catalytic subunit hydrolyzes ATP, contains the aspartyl phosphorylation site and binding sites for the transported ligand(s) and catalyzes ion transport. Various subfamilies of P-type ATPases also need additional subunits for proper function. Additional subunits that lack catalytic activity are present in the ATPase complexes of P1A, P2A, P2C and P4 ATPases. E.g.
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Folylpolyglutamate synthase, mitochondrial is an enzyme that in humans is encoded by the FPGS gene. This gene encodes the folylpolyglutamate synthetase enzyme. This enzyme has a central role in establishing and maintaining both cytosolic and mitochondrial folylpolyglutamate concentrations and, therefore, is essential for folate homeostasis and the survival of proliferating cells. This enzyme catalyzes the ATP-dependent addition of glutamate moieties to folate and folate derivatives.
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The severity of the disease is correlated with the timing of onset of symptoms, earlier being more severe. Tyrosinemia type I is an autosomal recessive disorder caused by mutations in the both copies of the gene encoding the enzyme fumarylacetoacetate hydrolase (FAH). FAH is a metabolic enzyme that catalyzes the conversion of fumarylacetoacetate to fumarate and acetoacetate. It is expressed primarily in the liver and kidney.
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The coagulation cascade. TF is the cell surface receptor for the serine protease factor VIIa. The best known function of tissue factor is its role in blood coagulation. The complex of TF with factor VIIa catalyzes the conversion of the inactive protease factor X into the active protease factor Xa. Together with factor VIIa, tissue factor forms the tissue factor or extrinsic pathway of coagulation.
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For example, tolerogenic DCs can release or induce enzymes such as indoleamine 2,3-dioxygenase (IDO) or heme oxygenase-1 (HO-1). IDO promotes the degradation of tryptophan to N-formylkynurenin leading to reduced T cell proliferation, whereas HO- 1 catalyzes degradation of hemoglobin resulting in production of monoxide and lower DC immunogenicity. Besides that, tolerogenic DCs also may produce retinoic acid (RA), which induces Treg differentiation.
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Sonic Hedgehog (Shh) is the most potent of the three Hedgehog ligands. Inhibition of Shh expression and activity can thus be an effective way of restricting Hedgehog signaling- mediated tumor progression. RU-SKI 43 inhibits the activity of SHHat, an enzyme that catalyzes the palmitoylation of Shh.Petrova E, Rios-Esteves J, Ouerfelli O, Glickman JF, Resh MD. Inhibitors of Hedgehog acyltransferase block Sonic Hedgehog signaling.
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Chorismate synthase (CS) catalyzes the last step in the shikimate pathway—the formation of chorismate. Two classes of CS are known, both of which require FMN, but are divided on their need for NADPH as a reducing agent. The proposed mechanism for CS involves radical species. The radical flavin species has not been detected spectroscopically without using a substrate analogue, which suggests that it is short-lived.
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Thermolysin (, Bacillus thermoproteolyticus neutral proteinase, thermoase, thermoase Y10, TLN) is a thermostable neutral metalloproteinase enzyme produced by the Gram-positive bacteria Bacillus thermoproteolyticus. It requires one zinc ion for enzyme activity and four calcium ions for structural stability. Thermolysin specifically catalyzes the hydrolysis of peptide bonds containing hydrophobic amino acids. However thermolysin is also widely used for peptide bond formation through the reverse reaction of hydrolysis.
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In enzymology, a methanol dehydrogenase is an enzyme that catalyzes the chemical reaction: :methanol \rightleftharpoons formaldehyde + 2 electrons + 2H+ How the electrons are captured and transported depends upon the kind of methanol dehydrogenase and there are two main types. A common electron acceptor in biological systems is nicotinamide adenine dinucleotide (NAD+) and some enzymes use a related molecule called nicotinamide adenine dinucleotide phosphate (NADP+). An NAD+-dependent methanol dehydrogenase() was first reported in a Gram-positive methylotroph and is an enzyme that catalyzes the chemical reaction :methanol + NAD+ \rightleftharpoons formaldehyde + NADH + H+ Thus, the two substrates of this enzyme are methanol and NAD+, whereas its 3 products are formaldehyde, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is methanol:NAD+ oxidoreductase.
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Arogenate dehydratase (ADT) (EC 4.2.1.91) is an enzyme that catalyzes the chemical reaction : L-arogenate → L-phenylalanine + H2O + CO2 Hence, this enzyme has one substrate, L-arogenate, but 3 products:L-phenylalanine, H2O, and CO2. Certain forms of the protein have the potential to catalyze a second reaction, L-prephenate → L-phenylpyruvate + H2O + CO2 This enzyme participates in phenylalanine, tyrosine, and tryptophan biosynthesis (an example structure is shown to the right.
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In enzymology, a citrate dehydratase () is an enzyme that catalyzes the chemical reaction :citrate \rightleftharpoons cis-aconitate + H2O Hence, this enzyme has one substrate, citrate, and two products, cis-aconitate and H2O. This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is citrate hydro-lyase (cis-aconitate-forming). This enzyme is also called citrate hydro-lyase.
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In enzymology, a cyanamide hydratase () is an enzyme that catalyzes the chemical reaction :urea \rightleftharpoons cyanamide + H2O Hence, this enzyme has one substrate, urea, and two products, cyanamide and H2O. This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is urea hydro- lyase (cyanamide-forming). This enzyme is also called urea hydro-lyase.
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In enzymology, a cadmium-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O \rightleftharpoons ADP + phosphate Thus, the two substrates of this enzyme are ATP and H2O, whereas its two products are ADP and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (heavy-metal-exporting).
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In enzymology, a methylglyoxal synthase () is an enzyme that catalyzes the chemical reaction :dihydroxyacetone phosphate \rightleftharpoons methylglyoxal + phosphate Hence, this enzyme has one substrate, DHAP, and two products, methylglyoxal and phosphate. Attempts to observe reversibility of this reaction have been unsuccessful. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is glycerone-phosphate phosphate-lyase (methylglyoxal-forming).
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In enzymology, an isoprene synthase () is an enzyme that catalyzes the chemical reaction :dimethylallyl pyrophosphate \rightleftharpoons isoprene + diphosphate Hence, this enzyme has one substrate, dimethylallyl pyrophosphate, and two products, isoprene and pyrophosphate. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is dimethylallyl- pyrophosphate pyrophosphate-lyase (isoprene-forming). Other names in common use include ISPC, and ISPS.
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In enzymology, a myrcene synthase () is an enzyme that catalyzes the chemical reaction :geranyl diphosphate \rightleftharpoons myrcene + diphosphate Hence, this enzyme has one substrate, geranyl diphosphate, and two products, myrcene and diphosphate. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is geranyl-diphosphate diphosphate-lyase (myrcene-forming). This enzyme participates in monoterpenoid biosynthesis.
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The salt marsh plant Batis maritima contains the enzyme methyl chloride transferase that catalyzes the synthesis of chloromethane (CH3Cl) from S-adenosine-L-methionine and chloride. This protein has been purified and expressed in E. coli, and seems to be present in other organisms such as white rot fungi (Phellinus pomaceus), red algae (Endocladia muricata), and the ice plant (Mesembryanthemum crystallinum), each of which is a known CH3Cl producer.
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7DHC is known to impair intracellular cholesterol transport. It also increases the degradation of HMG-CoA reductase (the enzyme that catalyzes the rate-limiting step in cholesterol synthesis). 7DHC leads to novel oxysterol and steroid derivatives, and many of their functions or effects are yet unknown. A very important finding with respect to 7DHC is that it is the most reactive lipid for lipid peroxidation, and results in systemic oxidative stress.
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Beta-ketoacyl-ACP synthase III, perhaps the most well known of this family of enzymes, catalyzes a Claisen condensation between acetyl CoA and malonyl ACP. The image below reveals how CoA fits in the active site as a substrate of synthase III. 300px Beta-ketoacyl-ACP synthases I and II only catalyze acyl-ACP reactions with malonyl ACP. Synthases I and II are capable of producing long-chain acyl-ACPs.
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Lanosterol synthase also catalyzes the cyclization of 2,3;22,23-diepoxysqualene to 24(S),25-epoxylanosterol, which is later converted to 24(S),25-epoxycholesterol. Since the enzyme affinity for this second substrate is greater than for the monoepoxy (S)-2,3-epoxysqualene, under partial inhibition conversion of 2,3;22,23-diepoxysqualene to 24(S),25-epoxylanosterol is favored over lanosterol synthesis. This has relevance for disease prevention and treatment (see Disease Relevance, below).
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As mentioned previously, two classes of 3-Dehydroquinate Dehydratase exist, known as types I and II. These two versions have different amino acid sequences and different secondary structures. Type I is present in fungi, plants, and some bacteria, for the biosynthesis of chorismate. It catalyzes the cis-dehydration of 3-Dehydroquinate via a covalent imine intermediate. Type I is heat liable and has Km values in the low micromolar range.
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Microsomal glutathione S-transferase 2 is an enzyme that in humans is encoded by the MGST2 gene. The MAPEG (Membrane-Associated Proteins in Eicosanoid and Glutathione metabolism) family consists of six human proteins, several of which are involved in the production of leukotrienes and prostaglandin E, important mediators of inflammation. This gene encodes a protein that catalyzes the conjugation of leukotriene A4 and reduced glutathione to produce leukotriene C4.
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In enzymology, an acetylene hydratase () is a rare example of an enzyme containing tungsten. It catalyzes the hydration of acetylene to give acetaldehyde: :C2H2 \+ H2O → CH3CHO The W centre is bound to two molybdopterin cofactors. The mechanism is thought to involve attachment of acetylene to the metal followed by nucleophilic attack of water. This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds.
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Formyl-MFR dehydrogenase catalyzes the methanogenesis reaction by reducing carbon dioxide (CO2) to form carboxy-MFR. The structural data obtained from the X-ray structure suggests carbon dioxide (CO2) is reduced to formate (E0’ = -430 mV) at FwdBD's tungstopterin active site to carboxy-MFR by a 4Fe-4S ferredoxin (E = ~ – 500 mV) located 12.4 Å away. Then, it reduces the carboxy-MFR to MFR at its tungsten or molybdenum active site.
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Branching of the 300x300px FPP is an important metabolic intermediate in the mevalonate pathway that represents a major branch point in terpenoid pathways. FPP is used to form several important classes of compounds in addition to sterols (via squalene), including ubiquinone and dolichols. SQS catalyzes the first committed step in sterol biosynthesis from FPP, and is therefore important for controlling the flux towards sterol vs. non-sterol products.
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In enzymology, a microtubule-severing ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O \rightleftharpoons ADP + phosphate Thus, the two substrates of this enzyme are ATP and H2O, whereas its two products are ADP and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to facilitate cellular and subcellular movement. The systematic name of this enzyme class is ATP phosphohydrolase (tubulin-dimerizing).
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In enzymology, a nucleoplasmin ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O \rightleftharpoons ADP + phosphate Thus, the two substrates of this enzyme are ATP and H2O, whereas its two products are ADP and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to facilitate cellular and subcellular movement. The systematic name of this enzyme class is ATP phosphohydrolase (nucleosome-assembling).
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In enzymology, a guanosine-diphosphatase () is an enzyme that catalyzes the chemical reaction :GDP + H2O \rightleftharpoons GMP + phosphate Thus, the two substrates of this enzyme are GDP and H2O, whereas its two products are GMP and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is GDP phosphohydrolase. This enzyme is also called GDPase.
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Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. FARS2 charges tRNA(Phe) with phenylalanine and catalyzes direct attachment of m-Tyr (an oxidized version of Phe) to tRNA(Phe). This makes it important for mitochondrial translation and for delivery of the misacylated tRNA to the ribosome and incorporation of ROS- damaged amino acid into proteins. Alternative splicing results in multiple transcript variants.
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10-formyltetrahydrofolate dehydrogenase is an enzyme that in humans is encoded by the ALDH1L1 gene. The protein encoded by this gene catalyzes the conversion of 10-formyltetrahydrofolate, NADP, and water to tetrahydrofolate, NADPH, and carbon dioxide. The encoded protein belongs to the aldehyde dehydrogenase family and is responsible for formate oxidation in vivo. Deficiencies in this gene can result in an accumulation of formate and subsequent methanol poisoning.
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In enzymology, a triphosphatase () is an enzyme that catalyzes the chemical reaction :triphosphate + H2O \rightleftharpoons diphosphate + phosphate Thus, the two substrates of this enzyme are triphosphate and H2O, whereas its two products are diphosphate and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus- containing anhydrides. The systematic name of this enzyme class is triphosphate phosphohydrolase. This enzyme is also called inorganic triphosphatase.
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In enzymology, a vesicle-fusing ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O \rightleftharpoons ADP + phosphate Thus, the two substrates of this enzyme are ATP and H2O, whereas its two products are ADP and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to facilitate cellular and subcellular movement. The systematic name of this enzyme class is ATP phosphohydrolase (vesicle-fusing).
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In enzymology, a proteasome ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O \rightleftharpoons ADP + phosphate Thus, the two substrates of this enzyme are ATP and H2O, whereas its two products are ADP and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to facilitate cellular and subcellular movement. The systematic name of this enzyme class is ATP phosphohydrolase (polypeptide-degrading).
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In enzymology, a protein-secreting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O \rightleftharpoons ADP + phosphate Thus, the two substrates of this enzyme are ATP and H2O, whereas its two products are ADP and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (protein-secreting).
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Poly(A) polymerase gamma is an enzyme that in humans is encoded by the PAPOLG gene. This gene encodes a member of the poly(A) polymerase family which catalyzes template-independent extension of the 3' end of a DNA/RNA strand. This enzyme shares 60% identity to the well characterized poly(A) polymerase II (PAPII) at the amino acid level. These two enzymes have similar organization of structural and functional domains.
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In enzymology, a cetraxate benzylesterase () is an enzyme that catalyzes the chemical reaction :cetraxate benzyl ester + H2O \rightleftharpoons cetraxate + benzyl alcohol Thus, the two substrates of this enzyme are cetraxate benzyl ester and H2O, whereas its two products are cetraxate and benzyl alcohol. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is cetraxate- benzyl-ester benzylhydrolase.
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In enzymology, a D-arabinonolactonase () is an enzyme that catalyzes the chemical reaction :D-arabinono-1,4-lactone + H2O \rightleftharpoons D-arabinonate Thus, the two substrates of this enzyme are D-arabinono-1,4-lactone and H2O, whereas its product is D-arabinonate. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is D-arabinono-1,4-lactone lactonohydrolase.
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In enzymology, a deoxylimonate A-ring-lactonase () is an enzyme that catalyzes the chemical reaction :deoxylimonate + H2O \rightleftharpoons deoxylimononic acid D-ring-lactone Thus, the two substrates of this enzyme are deoxylimonate and H2O, whereas its product is deoxylimononic acid D-ring-lactone. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is deoxylimonate A-ring-lactonohydrolase.
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Firefly luciferase catalyzes a reaction that produces visible light in the 550 – 575 nm range. A click-beetle luciferase is also available that produces light at a peak closer to 595 nm. Both luciferases require the addition of an exogenous substrate (luciferin) for the light reaction to occur. Numerous luc- based bioreporters have been constructed for the detection of a wide array of inorganic and organic compounds of environmental concern.
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DNA transposons encode a transposase enzyme between inverted terminal repeats. When expressed, the transposase recognizes the terminal inverted repeats that flank the transposon and catalyzes its excision and reinsertion in a new site. This cut-and-paste mechanism typically reinserts transposons near their original location (within 100kb). DNA transposons are found in bacteria and make up 3% of the human genome and 12% of the genome of the roundworm C. elegans.
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In enzymology, a tannase () is an enzyme that catalyzes the chemical reaction :digallate + H2O \rightleftharpoons 2 gallate Thus, the two substrates of this enzyme are digallate and H2O, whereas its product is gallate. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is tannin acylhydrolase. Other names in common use include tannase S, and tannin acetylhydrolase.
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In enzymology, a S-formylglutathione hydrolase () is an enzyme that catalyzes the chemical reaction :S-formylglutathione + H2O \rightleftharpoons glutathione + formate Thus, the two substrates of this enzyme are S-formylglutathione and H2O, whereas its two products are glutathione and formate. This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name of this enzyme class is S-formylglutathione hydrolase. This enzyme participates in methane metabolism.
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In enzymology, a sinapine esterase () is an enzyme that catalyzes the chemical reaction :sinapoylcholine + H2O \rightleftharpoons sinapate + choline Thus, the two substrates of this enzyme are sinapoylcholine and H2O, whereas its two products are sinapate and choline. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is sinapoylcholine sinapohydrolase. This enzyme is also called aromatic choline esterase.
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In enzymology, an orsellinate-depside hydrolase () is an enzyme that catalyzes the chemical reaction :orsellinate depside + H2O \rightleftharpoons 2 orsellinate Thus, the two substrates of this enzyme are orsellinate depside and H2O, whereas its product is orsellinate. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is orsellinate-depside hydrolase. This enzyme is also called lecanorate hydrolase.
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In enzymology, a phosphoenolpyruvate phosphatase () is an enzyme that catalyzes the chemical reaction :phosphoenolpyruvate + H2O \rightleftharpoons pyruvate + phosphate Thus, the two substrates of this enzyme are phosphoenolpyruvate and H2O, whereas its two products are pyruvate and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is phosphoenolpyruvate phosphohydrolase. This enzyme is also called PEP phosphatase.
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Phosphoglycolate, which is a potent inhibitor of phosphofructokinase and triosephosphate isomerase, must be quickly metabolized and transformed into a useful substrate, and phosphoglycolate phosphatase catalyzes the first step in the regeneration of 3-phosphoglycerate from 2-phosphoglycolate at the expense of energy in the form of ATP. Since the discovery of its activity in plants, it has been purified within human cells and implicated in 2,3-DPG regulation.
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In enzymology, a N-sulfoglucosamine-3-sulfatase () is an enzyme that catalyzes the chemical reaction of cleaving off the 3-sulfate groups of the N-sulfo-D- glucosamine 3-O-sulfate units of heparin. This enzyme belongs to the family of hydrolases, specifically those acting on sulfuric ester bonds. The systematic name of this enzyme class is N-sulfo-3-sulfoglucosamine 3-sulfohydrolase. This enzyme is also called chondroitinsulfatase.
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In enzymology, a 4-pyridoxolactonase () is an enzyme that catalyzes the chemical reaction :4-pyridoxolactone + H2O \rightleftharpoons 4-pyridoxate Thus, the two substrates of this enzyme are 4-pyridoxolactone and H2O, whereas its product is 4-pyridoxate. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is 4-pyridoxolactone lactonohydrolase. This enzyme participates in vitamin B6 metabolism.
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Beta-1,4 N-acetylgalactosaminyltransferase 1 is an enzyme that in humans is encoded by the B4GALNT1 gene. GM2 and GD2 gangliosides are sialic acid- containing glycosphingolipids. GalNAc-T is the enzyme involved in the biosynthesis of G(M2) and G(D2) glycosphingolipids. GalNAc-T catalyzes the transfer of GalNAc into G(M3) and G(D3) by a beta-1,4 linkage, resulting in the synthesis of G(M2) and G(D2), respectively.
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High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A is an enzyme that in humans is encoded by the PDE9A gene. The protein encoded by this gene catalyzes the hydrolysis of cAMP and cGMP to their corresponding monophosphates. The encoded protein plays a role in signal transduction by regulating the intracellular concentration of these cyclic nucleotides. Multiple transcript variants encoding several different isoforms have been found for this gene.
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Probable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase is an enzyme that in humans is encoded by the ALG8 gene. This gene encodes a member of the ALG6/ALG8 glucosyltransferase family. The encoded protein catalyzes the addition of the second glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation of proteins. Mutations in this gene have been associated with congenital disorder of glycosylation type Ih (CDG-Ih).
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Studies on AdPLA have shown lipolysis regulation following a G-protein coupled pathway in WAT. WAT is responsible for releasing fatty acids from stored triacylglycerol as energy sources for other tissues which is regulated predominately by AdPLA over other phospholipase A2 enzymes. Lipolysis is inversely related to AdPLA activity. AdPLA catalyzes the rate- limiting step, production of arachidonic acid, for the production of prostaglandins, specifically prostaglandin E2 (PGE2).
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Glycerol-3-phosphate acyltransferase 1, mitochondrial is an enzyme that in humans is encoded by the GPAM gene. Glycerol-3-phosphate acyltransferase (GPAT; EC 2.3.1.15), which catalyzes the initial and committing step in glycerolipid biosynthesis, is predicted to play a pivotal role in the regulation of cellular triacylglycerol and phospholipid levels. Two mammalian forms of GPAT have been identified on the basis of localization to either the endoplasmic reticulum or mitochondria.
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ATP synthase subunit s, mitochondrial is an enzyme that in humans is encoded by the ATP5S gene. This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, comprising the proton channel.
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In enzymology, a phosphonoacetate hydrolase () is an enzyme that catalyzes the chemical reaction :phosphonoacetate + H2O \rightleftharpoons acetate + phosphate Thus, the two substrates of this enzyme are phosphonoacetate and H2O, whereas its two products are acetate and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-phosphorus bonds. The systematic name of this enzyme class is phosphonoacetate phosphonohydrolase. This enzyme participates in aminophosphonate metabolism.
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In enzymology, a phosphonopyruvate hydrolase () is an enzyme that catalyzes the chemical reaction :3-phosphonopyruvate + H2O \rightleftharpoons pyruvate + phosphate Thus, the two substrates of this enzyme are 3-phosphonopyruvate and H2O, whereas its two products are pyruvate and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-phosphorus bonds. The systematic name of this enzyme class is '. This enzyme is also called PPH'.
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In enzymology, a trithionate hydrolase () is an enzyme that catalyzes the chemical reaction :trithionate + H2O \rightleftharpoons thiosulfate + sulfate + 2 H+ Thus, the two substrates of this enzyme are trithionate and H2O, whereas its 3 products are thiosulfate, sulfate, and H+. This enzyme belongs to the family of hydrolases, specifically those acting on sulfur-sulfur bonds. The systematic name of this enzyme class is trithionate thiosulfohydrolase. This enzyme participates in sulfur metabolism.
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In enzymology, an oxaloacetase () is an enzyme that catalyzes the chemical reaction: :oxaloacetate + H2O \rightleftharpoons oxalate + acetate Thus, the two substrates of this enzyme are oxaloacetate and H2O, whereas its two products are oxalate and acetate. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-carbon bonds in ketonic substances. The systematic name of this enzyme class is oxaloacetate acetylhydrolase. This enzyme is also called oxalacetic hydrolase.
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In enzymology, a phosphoamidase () is an enzyme that catalyzes the chemical reaction :N-phosphocreatine + H2O \rightleftharpoons creatine + phosphate Thus, the two substrates of this enzyme are N-phosphocreatine and H2O, whereas its two products are creatine and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphorus-nitrogen bonds. The systematic name of this enzyme class is phosphamide hydrolase. This enzyme is also called creatine phosphatase.
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In enzymology, an acetone carboxylase () is an enzyme that catalyzes the chemical reaction :acetone + CO2 \+ ATP + 2 H2O \rightleftharpoons acetoacetate + AMP + 2 phosphate The 4 substrates of this enzyme are acetone, CO2, ATP, and H2O, whereas its 3 products are acetoacetate, AMP, and phosphate. This enzyme belongs to the family of ligases, specifically those forming carbon-carbon bonds. The systematic name of this enzyme class is acetone:carbon-dioxide ligase (AMP-forming).
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In enzymology, a dihydroxyfumarate decarboxylase () is an enzyme that catalyzes the chemical reaction :dihydroxyfumarate \rightleftharpoons tartronate semialdehyde + CO2 Hence, this enzyme has one substrate, dihydroxyfumarate, and two products, tartronate semialdehyde and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is dihydroxyfumarate carboxy-lyase (tartronate-semialdehyde-forming). This enzyme is also called dihydroxyfumarate carboxy-lyase.
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In enzymology, a benzylsuccinate synthase () is an enzyme that catalyzes the chemical reaction :benzylsuccinate \rightleftharpoons toluene + fumarate Hence, this enzyme has one substrate, benzylsuccinate, and two products, toluene and fumarate. This enzyme belongs to the family of lyases, specifically in the "catch-all" class of carbon-carbon lyases. The systematic name of this enzyme class is benzylsuccinate fumarate-lyase (toluene-forming). This enzyme is also called benzylsuccinate fumarate-lyase.
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In enzymology, a hydroxypyruvate decarboxylase () is an enzyme that catalyzes the chemical reaction :hydroxypyruvate \rightleftharpoons glycolaldehyde + CO2 Hence, this enzyme has one substrate, hydroxypyruvate, and two products, glycolaldehyde and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is hydroxypyruvate carboxy-lyase (glycolaldehyde-forming). This enzyme is also called hydroxypyruvate carboxy- lyase.
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In enzymology, a stipitatonate decarboxylase () is an enzyme that catalyzes the chemical reaction :stipitatonate \rightleftharpoons stipitatate + CO2 Hence, this enzyme has one substrate, stipitatonate, and two products, stipitatate and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is stipitatonate carboxy-lyase (decyclizing, stipitatate- forming). This enzyme is also called stipitatonate carboxy-lyase (decyclizing).
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In enzymology, a phenylpyruvate decarboxylase () is an enzyme that catalyzes the chemical reaction :phenylpyruvate \rightleftharpoons phenylacetaldehyde + CO2 Hence, this enzyme has one substrate, phenylpyruvate, and two products, phenylacetaldehyde and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is phenylpyruvate carboxy-lyase (phenylacetaldehyde-forming). This enzyme is also called phenylpyruvate carboxy-lyase.
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In enzymology, a carnitine decarboxylase () is an enzyme that catalyzes the chemical reaction :carnitine \rightleftharpoons 2-methylcholine + CO2 Hence, this enzyme has one substrate, carnitine, and two products, 2-methylcholine and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is carnitine carboxy-lyase (2-methylcholine-forming). This enzyme is also called carnitine carboxy-lyase.
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The EC number of 5'-deoxyadenosine deaminase is EC:3.5.4.41. The Enzyme Commission Number is a system of classifying enzymes based on the reactions that the enzyme catalyzes. Due to EC number not being attached to specific enzymes, but rather the enzyme catalyzed reaction, a single EC number could describe a variety of enzymes that catalyze the same reaction. The UniProt id number for 5'-deoxyadenosine deaminase is Q58936.
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Carnitine shuttle activation occurs due to a need for fatty acid oxidation which is required for energy production. During vigorous muscle contraction or during fasting, ATP concentration decreases and AMP concentration increases leading to the activation of AMP-activated protein kinase (AMPK). AMPK phosphorylates acetyl-CoA carboxylase, which normally catalyzes malonyl-CoA synthesis. This phosphorylation inhibits acetyl-CoA carboxylase, which in turn lowers the concentration of malonyl-CoA.
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The first crewed mission to the Moon during the Space Race in the late 1960s was a global success for NASA and the United States. This drama poses the question: "What if the Space Race had never ended?" In an alternate timeline, a Soviet cosmonaut, Alexei Leonov, becomes the first human to land on the Moon. This outcome devastates morale at NASA, but also catalyzes an American effort to catch up.
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L-phenylalanine is first hydroxylated by CYP79D16, followed by a decarboxylation and dehydration, forming the E-oxime phenylacetaldoxime. Next, CYP71AN24 catalyzes the rearrangement of the E-oxime to the Z-oxime followed by a dehydration and a hydroxylation to form mandelonitrile. Finally, UGT85A19 or UGT94AF3 utilize UDP-glucose to glycosylate mandelonitrile, forming (R)-prunasin. After generating (R)-prunasin, the product is further glycosylated into amydgalin by either isoform UGT94AF1 or UGT94AF2.
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Schematic representation of a metabolic branch point. The numbers represent chemical compounds, whereas the letters represent enzymes that catalyze the conversion indicated by the nearby arrow. In this scheme, enzyme c catalyzes the committed step in the biosynthesis of compound 6. In enzymology, the committed step (also known as the first committed step) is an effectively irreversible enzymatic reaction that occurs at a branch point during the biosynthesis of some molecules.
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Purine nucleoside phosphorylase (PNP) also known as PNPase and inosine phosphorylase is an enzyme that in humans is encoded by the NP gene. In enzymology, a purine-nucleoside phosphorylase () is an enzyme that catalyzes the chemical reaction :purine nucleoside + phosphate \rightleftharpoons purine + alpha-D-ribose 1-phosphate Thus, the two substrates of this enzyme are purine nucleoside and phosphate, whereas its two products are purine and alpha-D-ribose 1-phosphate.
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Takamine continued to work for the department of agriculture and commerce until 1887. He then founded the Tokyo Artificial Fertilizer Company, where he later isolated the enzyme takadiastase, an enzyme that catalyzes the breakdown of starch. Takamine developed his diastase from koji, a fungus used in the manufacture of soy sauce and miso. Its Latin name is Aspergillus oryzae, and it is a "designated national fungus" (kokkin) in Japan.
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The average human detection threshold for sucrose is 10 millimoles per liter. For lactose it is 30 millimoles per liter, with a sweetness index of 0.3, and 5-nitro-2-propoxyaniline 0.002 millimoles per liter. “Natural” sweeteners such as saccharides activate the GPCR, which releases gustducin. The gustducin then activates the molecule adenylate cyclase, which catalyzes the production of the molecule cAMP, or adenosine 3', 5'-cyclic monophosphate.
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The NADH-ubiquinone oxidoreductase complex (complex I) of the mitochondrial respiratory chain catalyzes the transfer of electrons from NADH to ubiquinone, and consists of at least 43 subunits. The complex is located in the inner mitochondrial membrane. This gene encodes the 24 kDa subunit of complex I, and is involved in electron transfer. NDUFV2 is an oxidoreductase and a component of the flavoprotein-sulfur (FP) fragment of the enzyme.
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FN3K catalyzes phosphorylation of fructosamines formed by glycation, the nonenzymatic reaction of glucose with primary amines followed by Amadori rearrangement. Phosphorylation of fructosamines may initiate metabolism of the modified amine and result in deglycation of glycated proteins. FN3K is responsible for the formation of fructose 3-phosphate (F3P), a compound identified in the lenses of diabetic rats. The spontaneous decomposition of F3P leads to the formation of 3-deoxyglucosone (3DG).
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1-methylnicotinamide can be produced in the liver by nicotinamide N-methyltransferase. The reaction takes place during the metabolism of NAD (nicotinamide adenine dinucleotide). NNMT (Nicotinamide N-methyltransferase) is an enzyme that in humans is encoded by the NNMT gene. NNMT catalyzes the methylation of nicotinamide and similar compounds using the methyl donor S-adenosyl methionine (SAM-e) to produce S-adenosyl-L- homocysteine (SAH) and 1-methylnicotinamide.
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ALDOC is a key enzyme in the fourth step of glycolysis, as well as in the reverse pathway gluconeogenesis. It catalyzes the reversible conversion of fructose-1,6-bisphosphate to glyceraldehydes-3-phosphate (G3P), or glyceraldehyde, and dihydroxyacetone phosphate (DHAP) by aldol cleavage. As a result, it is a crucial player in ATP biosynthesis. As an aldolase, ALDOC putatively also contributes to other "moonlighting" functions, though its exact involvements remain unclear.
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The human ATP5F1C gene encodes the gamma subunit of an enzyme called mitochondrial ATP synthase. This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes adenosine triphosphate (ATP) synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, F0, comprising the proton channel.
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ATP synthase subunit b, mitochondrial is an enzyme that in humans is encoded by the ATP5PB gene. This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, comprising the proton channel.
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The protein encoded by this gene is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The encoded protein is normally found in the Golgi apparatus but can be proteolytically processed to a soluble form. This protein is a member of glycosyltransferase family 29. Multiple transcript variants encoding several different isoforms have been found for this gene.
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When the PCNA binding site on DNA ligase I is inactive, DNA ligase I's ability to connect Okazaki fragments is severely impaired. Thus, a proposed mechanism follows: after a PCNA-DNA polymerase δ complex synthesizes Okazaki fragments, the DNA polymerase δ is released. Then, DNA ligase I binds to the PCNA, which is clamped to the nicks of the lagging strand, and catalyzes the formation of phosphodiester bonds.
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GalK encodes for a kinase that phosphorylates α-D-galactose to galactose 1-phosphate. Lastly, galM catalyzes the conversion of β-D-galactose to α-D-galactose as the first step in galactose metabolism. The gal operon contains two operators, OE (for external) and OI (for internal). The former is just upstream of the promoter, and the latter is just after the galE gene (the first gene in the operon).
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Mitochondrial-processing peptidase subunit beta is an enzyme that in humans is encoded by the PMPCB gene. This gene is a member of the peptidase M16 family and encodes a protein with a zinc-binding motif. This protein is located in the mitochondrial matrix and catalyzes the cleavage of the leader peptides of precursor proteins newly imported into the mitochondria, though it only functions as part of a heterodimeric complex.
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Starch phosphorylase is a form of phosphorylase similar to glycogen phosphorylase, except that it acts upon starch instead of glycogen. The plant alpha-glucan phosphorylase, commonly called starch phosphorylase (EC 2.4.1.1), is largely known for the phosphorolytic degradation of starch. Starch phosphorylase catalyzes the reversible transfer of glucosyl units from glucose-1-phosphate to the nonreducing end of alpha-1,4-D-glucan chains with the release of phosphate.
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Mutations in UQCRB can result in mitochondrial deficiencies and associated disorders. It is majorly associated with a complex III deficiency, a deficiency in an enzyme complex which catalyzes electron transfer from coenzyme Q to cytochrome c in the mitochondrial respiratory chain. A complex III deficiency can result in a highly variable phenotype depending on which tissues are affected. Most frequent clinical manifestations include progressive exercise intolerance and cardiomyopathy.
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The VLCAD enzyme catalyzes most of fatty acid beta-oxidation by forming a C2-C3 trans-double bond in the fatty acid. VLCAD is specific to very long-chain fatty acids, typically C16-acylCoA and longer. In mice that have VLCAD deficiency, there is little to no protein hyperacetylation in the liver; this implies that the VLCAD protein is also necessary for protein acetylation in this biological system.
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As an enolase, ENO3 is a glycolytic enzyme that catalyzes the reversible conversion of 2-phosphoglycerate to phosphoenolpyruvate. This particular isoform is predominantly expressed in adult striated muscle, including skeletal and cardiac muscle. During fetal muscle development, there is a transcriptional switch from expressing ENO1 to ENO3 influenced by muscle innervation and Myo D1. ENO3 is expressed at higher levels in fast-twitch fibers than in slow-twitch fibers.
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D-aspartate oxidase is an enzyme that is encoded by the DDO gene. The protein encoded by this gene is a peroxisomal flavoprotein that catalyzes the oxidative deamination of D-aspartate and N-methyl D-aspartate. Flavin adenine dinucleotide or 6-hydroxyflavin adenine dinucleotide can serve as the cofactor in this reaction. Two (or four, according to ) transcript variants encoding different isoforms have been found for this gene.
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Methylrhenium trioxide serves as a heterogeneous catalyst for a variety of transformations. Supported on Al2O3/SiO2, it catalyzes olefin metathesis at 25 °C. In solution, MTO catalyses for the oxidations with hydrogen peroxide. Terminal alkynes yield the corresponding acid or ester, internal alkynes yield diketones, and alkenes give epoxides. MTO also catalyses the conversion of aldehydes and diazoalkanes into an alkene,Hudson, A. “Methyltrioxorhenium” Encyclopedia of Reagents for Organic Synthesis.
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Arsenic interferes with cellular longevity by allosteric inhibition of an essential metabolic enzyme pyruvate dehydrogenase (PDH) complex, which catalyzes the oxidation of pyruvate to acetyl-CoA by NAD+. With the enzyme inhibited, the energy system of the cell is disrupted resulting in cellular apoptosis. Biochemically, arsenic prevents use of thiamine resulting in a clinical picture resembling thiamine deficiency. Poisoning with arsenic can raise lactate levels and lead to lactic acidosis.
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The hormone receptor without ligand binding interacts with heat shock proteins and prevents the transcription of targeted genes. Aldosterone and cortisol (a glucosteroid) have similar affinity for the mineralocorticoid receptor; however, glucocorticoids circulate at roughly 100 times the level of mineralocorticoids. An enzyme exists in mineralocorticoid target tissues to prevent overstimulation by glucocorticoids. This enzyme, 11-beta hydroxysteroid dehydrogenase type II (Protein:HSD11B2), catalyzes the deactivation of glucocorticoids to 11-dehydro metabolites.
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Galactokinase is an enzyme (phosphotransferase) that facilitates the phosphorylation of α-D-galactose to galactose 1-phosphate at the expense of one molecule of ATP. Galactokinase catalyzes the second step of the Leloir pathway, a metabolic pathway found in most organisms for the catabolism of β-D-galactose to glucose 1-phosphate. First isolated from mammalian liver, galactokinase has been studied extensively in yeast, archaea, plants, and humans.
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The soluble hemoglobins, present in the tentacles, are able to bind O2 and H2S, which are necessary for chemosynthetic bacteria. Due to the capillaries, these compounds are absorbed by bacteria. During the chemosynthesis, the mitochondrial enzyme rhodanase catalyzes the disproportionation reaction of the thiosulfate anion S2O32- to sulfur S and sulfite SO32- . The R. pachyptila’s bloodstream is responsible for absorption of the O2 and nutrients such as carbohydrates.
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The hatchet ribozyme is an RNA structure that catalyzes its own cleavage at a specific site. In other words, it is a self-cleaving ribozyme. Hatchet ribozymes were discovered by a bioinformatics strategy as RNAs Associated with Genes Associated with Twister and Hammerhead ribozymes, or RAGATH. Subsequent biochemical analysis supports the conclusion of a ribozyme function, and determined further characteristics of the chemical reaction catalyzed by the ribozyme.
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The Girlie Show founders, Erin Merryweather, Dawn Tyler Harth, and Marilyn Artus were awarded the "Great Inspirations" award in 2008 by Creative Oklahoma, Inc. (CO) a statewide non- profit organization that promotes and catalyzes creative idea generation in individuals and institutions. This award recognizes individuals that create Oklahomans' creative endeavors, solutions, or activities as both a stimulus and an example for other corporations, organizations, communities, or educational institutions.
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After the uridine nucleotide base is synthesized, the other bases, cytosine and thymine are synthesized. Cytosine biosynthesis is a two-step reaction which involves the conversion of UMP to UTP. Phosphate addition to UMP is catalyzed by a kinase enzyme. The enzyme CTP synthase catalyzes the next reaction step: the conversion of UTP to CTP by transferring an amino group from glutamine to uridine; this forms the cytosine base of CTP.
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Several isozymes of malate dehydrogenase exist. There are two main isoforms in eukaryotic cells. One is found in the mitochondrial matrix, participating as a key enzyme in the citric acid cycle that catalyzes the oxidation of malate. The other is found in the cytoplasm, assisting the malate-aspartate shuttle with exchanging reducing equivalents so that malate can pass through the mitochondrial membrane to be transformed into oxaloacetate for further cellular processes.
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In enzymology, a sepiapterin deaminase () is an enzyme that catalyzes the chemical reaction :sepiapterin + H2O \rightleftharpoons xanthopterin-B2 \+ NH3 Thus, the two substrates of this enzyme are sepiapterin and H2O, whereas its two products are xanthopterin-B2 and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is sepiapterin aminohydrolase.
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In enzymology, a glycosphingolipid deacylase () is an enzyme that catalyzes a chemical reaction that cleaves gangliosides and neutral glycosphingolipids, releasing fatty acids to form the lyso-derivatives. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is glycosphingolipid amidohydrolase. This enzyme is also called glycosphingolipid ceramide deacylase.
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In enzymology, an alkylamidase () is an enzyme that catalyzes the chemical reaction :N-methylhexanamide + H2O \rightleftharpoons hexanoate + methylamine Thus, the two substrates of this enzyme are N-methylhexanamide and H2O, whereas its two products are hexanoate and methylamine. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-methylhexanamide amidohydrolase.
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In enzymology, a diguanidinobutanase () is an enzyme that catalyzes the chemical reaction :1,4-diguanidinobutane + H2O \rightleftharpoons agmatine + urea Thus, the two substrates of this enzyme are 1,4-diguanidinobutane and H2O, whereas its two products are agmatine and urea. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is 1,4-diguanidinobutane amidinohydrolase.
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The other pathway of glycine biosynthesis is known as the glycolytic pathway. This pathway converts serine synthesized from the intermediates of glycolysis to glycine. In the glycolytic pathway, the enzyme serine hydroxymethyltransferase catalyzes the cleavage of serine to yield glycine and transfers the cleaved carbon group of serine onto tetrahydrofolate, forming 5,10-methylene-tetrahydrofolate. Cysteine biosynthesis is a two-step reaction that involves the incorporation of inorganic sulfur.
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This interaction catalyzes the development of an irreversible matrix of glycoalkaloid-sterol complexes (figure 2, part 4). In this way, the sterols from the external membrane are immobilized and membrane budding will arise. Tubular structures are formed, because of the structure of tomatine (figure 2, part 6).Keukens, Erik AJ, et al; Dual specificity of sterol-mediated glycoalkaloid induced membrane disruption; Biochimica et Biophysica Acta (BBA) - Biomembranes 1110.2, 1992; 127-136.
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Pyruvate kinase isozymes R/L is an enzyme that in humans is encoded by the PKLR gene. The protein encoded by this gene is a pyruvate kinase that catalyzes the production of pyruvate and ATP from phosphoenolpyruvate. Defects in this enzyme, due to gene mutations or genetic variations, are the common cause of chronic hereditary nonspherocytic hemolytic anemia (CNSHA or HNSHA). Alternatively spliced transcript variants encoding distinct isoforms have been described.
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Upon oxygen exposure, the bacteria is able to utilize nitrous oxide reductase, an enzyme that catalyzes the last step of denitrification. Aerobic denitrifiers are mainly Gram-negative bacteria in the phylum Proteobacteria. Enzymes NapAB, NirS, NirK and NosZ are located in the periplasm, a wide space bordered by the cytoplasmic and the outer membrane in Gram-negative bacteria. Denitrification can lead to a condition called isotopic fractionation in the soil environment.
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The complex [Ru(o-C6H4PPh2)(H)(CO)(PPh3)2] catalyzes the Murai reaction at room temperature. For [Ru(H)2(H2)2(PR3)2], the active complex is [Ru(H)2(PR3)2]. PMe3) omitted for clarity. After the active form of the ruthenium catalyst complex is generated from 1, acetophenone coordinates to the complex via its carbonyl oxygen and agostically via its ortho C-H bond (2).
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A fragment of yeast rDNA containing the 5S gene, nontranscribed spacer DNA, and part of the 35S gene has localized cis-acting mitotic recombination stimulating activity. This DNA fragment contains a mitotic recombination hotspot, referred to as HOT1. HOT1 expresses recombination-stimulating activity when it is inserted into novel locations in the yeast genome. HOT1 includes an RNA polymerase I (PolI) transcription promoter that catalyzes 35S ribosomal rRNA gene transcription.
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If PARP3 is lost, this results in single-strand breaks, and thus the recruitment of PARP1. A second hypothesis suggests that the two enzyme work together; PARP3 catalyzes mono-ADP ribosylation and short poly-ADP ribosylation and serves to activate PARP1. The PARPs have many protein targets at the site of DNA damage. KU protein and DNA-PKcs are both double-stranded break repair components with unknown sites of ADP- ribosylation.
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Procollagen-proline dioxygenase, commonly known as prolyl hydroxylase, is a member of the class of enzymes known as alpha-ketoglutarate-dependent hydroxylases. These enzymes catalyze the incorporation of oxygen into organic substrates through a mechanism that requires alpha-Ketoglutaric acid, Fe2+, and ascorbate. This particular enzyme catalyzes the formation of (2S, 4R)-4-hydroxyproline, a compound that represents the most prevalent post- translational modification in the human proteome.
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In enzymology, a peptide-aspartate beta-dioxygenase (), a member of the alpha- ketoglutarate-dependent hydroxylases superfamily, is an enzyme that catalyzes the chemical reaction :peptide-L-aspartate + 2-oxoglutarate + O2 \rightleftharpoons peptide-3-hydroxy-L-aspartate + succinate + CO2 The 3 substrates of this enzyme are peptide-L-aspartate, 2-oxoglutarate, and O2, whereas its 3 products are peptide-3-hydroxy-L-aspartate, succinate, and CO2. It employs one cofactor, iron.
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In enzymology, a lathosterol oxidase () is an enzyme that catalyzes the chemical reaction center 5α-cholest-7-en-3β-ol + NAD(P)H + H+ \+ O2 \rightleftharpoons cholesta-5,7-dien-3β-ol + NAD(P)+ + 2 H2O The 5 substrates of this enzyme are 5α-cholest-7-en-3β-ol, NADH, NADPH, H+, and O2, whereas its 4 products are cholesta-5,7-dien-3β-ol (provitamin D3), NAD+, NADP+, and H2O.
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Sphingosine kinase (SK) is a lipid kinase that catalyzes the conversion of sphingosine to sphingosine-1-phosphate (S1P). Sphingolipids are ubiquitous membrane lipids. Upon activation, sphingosine kinase migrates from the cytosol to the plasma membrane where it transfers a γ phosphate (which is the last or terminal phosphate) from ATP or GTP to sphingosine. The S1P receptor is a GPCR receptor, so S1P has the ability to regulate G protein signaling.
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Cholesterol 24-hydroxylase (), also commonly known as cholesterol 24S-hydroxylase, cholesterol 24-monooxygenase, CYP46, or CYP46A1, is an enzyme that catalyzes the conversion of cholesterol to 24S-hydroxycholesterol. It is responsible for the majority of cholesterol turnover in the human central nervous system. The systematic name of this enzyme class is cholesterol,NADPH:oxygen oxidoreductase (24-hydroxylating). This enzyme is a member of the cytochrome P450 (CYP) superfamily of enzymes.
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Cholesterol-24 hydroxylase mechanism. The heme molecule forms an oxyferryl intermediate that abstract a hydrogen from cholesterol. The subsequent alkyl intermediate then reacts with the activated oxygen to form the final product. Cholesterol-24 hydroxylase catalyzes the following reaction: :cholesterol + NADPH + H+ \+ O2 \rightleftharpoons (24S)-24-hydroxycholesterol + NADP+ \+ H2O The 4 substrates of this enzyme are cholesterol, NADPH, H+, and O2, and its 3 products are 24S-hydroxycholesterol, NADP+, and H2O.
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DBH primarily contributes to catecholamine and trace amine biosynthesis. It also participates in the metabolism of xenobiotics related to these substances; for example, the human DBH enzyme catalyzes the beta- hydroxylation of amphetamine and para-hydroxyamphetamine, producing norephedrine and para-hydroxynorephedrine respectively. DBH has been implicated as correlating factor in conditions associated with decision making and addictive drugs, e.g., alcoholism and smoking, attention deficit hyperactivity disorder, schizophrenia, and Alzheimer's disease.
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Huperzine A is extracted from Huperzia serrata. It is a reversible acetylcholinesterase inhibitor and NMDA receptor antagonist that crosses the blood-brain barrier. Acetylcholinesterase is an enzyme that catalyzes the breakdown of the neurotransmitter acetylcholine and of some other choline esters that function as neurotransmitters. The structure of the complex of huperzine A with acetylcholinesterase has been determined by X-ray crystallography (PDB code: 1VOT; see the 3D structure).
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The salt marsh plant Batis maritima contains the enzyme methyl chloride transferase that catalyzes the synthesis of CH3Cl from S-adenosine-L-methionine and chloride. This protein has been purified and expressed in E. coli, and seems to be present in other organisms such as white rot fungi (Phellinus pomaceus), red algae (Endocladia muricata), and the ice plant (Mesembryanthemum crystallinum), each of which is a known CH3Cl producer.
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In enzymology, a pyridoxine 5'-phosphate synthase () is an enzyme that catalyzes the chemical reaction :1-deoxy-D-xylulose 5-phosphate + 3-hydroxy-1-aminoacetone phosphate \rightleftharpoons pyridoxine-5'-phosphate + phosphate + 2 H2O The two substrates of this enzyme are 1-deoxy-D-xylulose 5-phosphate (DXP) and 3-hydroxy-1-aminoacetone phosphate (HAP), whereas its 3 products are H2O, phosphate, and pyridoxine-5'-phosphate (a vitamer of pyridoxal phosphate).
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The pre-mRNA contains specific sequence elements that are recognized and utilized during spliceosome assembly. These include the 5' end splice site, the branch point sequence, the polypyrimidine tract, and the 3' end splice site. The spliceosome catalyzes the removal of introns, and the ligation of the flanking exons. Introns typically have a GU nucleotide sequence at the 5' end splice site, and an AG at the 3' end splice site.
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In enzymology, an anthranilate N-benzoyltransferase () is an enzyme that catalyzes the chemical reaction :benzoyl-CoA + anthranilate \rightleftharpoons CoA + N-benzoylanthranilate Thus, the two substrates of this enzyme are benzoyl-CoA and anthranilate, whereas its two products are CoA and N-benzoylanthranilate. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is benzoyl-CoA:anthranilate N-benzoyltransferase.
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In enzymology, an anthranilate N-malonyltransferase () is an enzyme that catalyzes the chemical reaction :malonyl-CoA + anthranilate \rightleftharpoons CoA + N-malonylanthranilate Thus, the two substrates of this enzyme are malonyl-CoA and anthranilate, whereas its two products are CoA and N-malonylanthranilate. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is malonyl-CoA:anthranilate N-malonyltransferase.
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Acyl-CoA cholesterol acyl transferase , more simply referred to as ACAT, also known as sterol O-acyltransferase (SOAT), belongs to the class of enzymes known as acyltransferases. The role of this enzyme is to transfer fatty acyl groups from one molecule to another. ACAT is an important enzyme in bile acid biosynthesis. In nearly all mammalian cells, ACAT catalyzes the intracellular esterification of cholesterol and formation of cholesteryl esters.
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Eu(fod)3 serves as a Lewis acid catalyst in organic synthesis including stereoselective Diels-Alder and aldol addition reactions. For example, Eu(fod)3 catalyzes the cyclocondensations of substituted dienes with aromatic and aliphatic aldehydes to yield dihydropyrans, with high selectivity for the endo product.Wenzel, T.J.; Ciak, J.M.; "Europium, tris(6,6,7,7,8,8,8-heptafluoro-2,2-dimethyl-3,5-octanedianato)" in Encyclopedia of Reagents for Organic Synthesis, 2004. John Wiley & Sons, Ltd.
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2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase, also known as SHCHC synthase, is encoded by the menH gene in E.coli and functions in the synthesis of vitamin K. The specific step in the synthetic pathway that SHCHC synthase catalyzes is the conversion of 5-enolpyruvoyl-6-hydroxy-2-succinylcyclohex-3-ene-1-carboxylate to (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate and pyruvate.
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Lysosomes, a part of an animal cells, helps break down large molecules into smaller ones that can be reused. GlcNAc-1-phosphotransferase catalyzes the N-linked glycosylation of asparagine residues with a molecule called mannose-6-phosphate (M6P). M6P acts as indicator whether a hydrolase should be transported to the lysosome or not. Once a hydrolase has the indication from an M6P, it can be transported to a lysosome.
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In enzymology, a xylitol oxidase () is an enzyme that catalyzes the chemical reaction :xylitol + O2 \rightleftharpoons xylose + H2O2 Thus, the two substrates of this enzyme are xylitol and O2, whereas its two products are xylose and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is xylitol:oxygen oxidoreductase.
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In enzymology, a glucoside 3-dehydrogenase () is an enzyme that catalyzes the chemical reaction :sucrose + acceptor \rightleftharpoons 3-dehydro-alpha-D- glucosyl-beta-D-fructofuranoside + reduced acceptor Thus, the two substrates of this enzyme are sucrose and acceptor, whereas its two products are 3-dehydro-alpha-D-glucosyl-beta-D-fructofuranoside and reduced acceptor. This enzyme participates in galactose metabolism and starch and sucrose metabolism. It employs one cofactor, FAD.
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In enzymology, a 1-hydroxy-2-naphthoate 1,2-dioxygenase () is an enzyme that catalyzes the chemical reaction :1-hydroxy-2-naphthoate + O2 \rightleftharpoons (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate Thus, the two substrates of this enzyme are 1-hydroxy-2-naphthoate and O2, whereas its product is (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate. This enzyme participates in naphthalene and anthracene degradation. It employs one cofactor, iron.
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Arsenate reductase (glutaredoxin) () is an enzyme that catalyzes the chemical reaction :arsenate + glutaredoxin \rightleftharpoons arsenite + glutaredoxin disulfide + H2O Thus, the two substrates of this enzyme are arsenate and glutaredoxin, whereas its 3 products are arsenite, glutaredoxin disulfide, and water. This enzyme belongs to the family of oxidoreductases, specifically those acting on phosphorus or arsenic in donor with disulfide as acceptor. The systematic name of this enzyme class is glutaredoxin:arsenate oxidoreductase.
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In enzymology, a NAD(P)+ transhydrogenase (Re/Si-specific () is an enzyme that catalyzes the chemical reaction :NADPH + NAD+ \rightleftharpoons NADP+ \+ NADH Thus, the two substrates of this enzyme are NADPH and NAD+, whereas its two products are NADP+ and NADH. This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with NAD+ or NADP+ as acceptor. This enzyme participates in nicotinate and nicotinamide metabolism.
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Sup35p is the Saccharomyces cerevisiae (a yeast) eukaryotic translation release factor. More specifically, it is the yeast eukaryotic release factor 3 (eRF3), which forms the translation termination complex with eRF1 (Sup45p in yeast). This complex recognizes and catalyzes the release of the nascent polypeptide chain when the ribosome encounters a stop codon. While eRF1 recognizes stop codons, eRF3 facilitates the release of the polypeptide chain through GTP hydrolysis.
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As with other statins, atorvastatin is a competitive inhibitor of HMG-CoA reductase. Unlike most others, however, it is a completely synthetic compound. HMG-CoA reductase catalyzes the reduction of 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) to mevalonate, which is the rate-limiting step in hepatic cholesterol biosynthesis. Inhibition of the enzyme decreases de novo cholesterol synthesis, increasing expression of low-density lipoprotein receptors (LDL receptors) on hepatocytes.
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Chromium(III) fluoride finds some applications as a mordant in textiles and as a corrosion inhibitor. Chromium(III) fluoride catalyzes the fluorination of chlorocarbons by HF.Mallikarjuna R. V. N.; Subramanian M. A. Fluoroolefin Manufacturing U.S. Patent 6,031,14, August 6, 1998; n.a. Ruh R. P.; Davis R. A. Proceess for Fluorinating Aliphatic Halohydrocarbons with a Chromium Fluoride catalyst and process for preparing the catalyst. U.S. Patent 2,745,886, May 15, 1956; n.a.
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Group I introns are also found inserted into genes of a wide variety of bacteriophages of Gram- positive bacteria. However, their distribution in the phage of Gram-negative bacteria is mainly limited to the T4, T-even and T7-like bacteriophages. Both intron-early and intron-late theories have found evidences in explaining the origin of group I introns. Some group I introns encode homing endonuclease (HEG), which catalyzes intron mobility.
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The cytochrome b6f complex (EC 1.10.99.1) (also called plastoquinol—plastocyanin reductase) is an enzyme related to Complex III but found in the thylakoid membrane in chloroplasts of plants, cyanobacteria, and green algae. This proton pump is driven by electron transport and catalyzes the transfer of electrons from plastoquinol to plastocyanin. The reaction is analogous to the reaction catalyzed by Complex III (cytochrome bc1) of the mitochondrial electron transport chain.
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In enzymology, an alanine racemase () is an enzyme that catalyzes the chemical reaction :L-alanine \rightleftharpoons D-alanine Hence, this enzyme has one substrate, L-alanine, and one product, D-alanine. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is alanine racemase. This enzyme is also called L-alanine racemase.
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In enzymology, an aspartate racemase () is an enzyme that catalyzes the chemical reaction :L-aspartate \rightleftharpoons D-aspartate Hence, this enzyme has one substrate, L-aspartate, and one product, D-aspartate. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is aspartate racemase. Other names in common use include D-aspartate racemase, and McyF.
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In enzymology, a 2-methyleneglutarate mutase () is an enzyme that catalyzes the chemical reaction :2-methyleneglutarate \rightleftharpoons 2-methylene-3-methylsuccinate Hence, this enzyme has one substrate, 2-methyleneglutarate, and one product, 2-methylene-3-methylsuccinate. This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The systematic name of this enzyme class is 2-methyleneglutarate carboxy-methylenemethylmutase. This enzyme is also called alpha-methyleneglutarate mutase.
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In enzymology, a 3-(hydroxyamino)phenol mutase () is an enzyme that catalyzes the chemical reaction :3-hydroxyaminophenol \rightleftharpoons aminohydroquinone Hence, this enzyme has one substrate, 3-hydroxyaminophenol, and one product, aminohydroquinone. This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring hydroxy groups. The systematic name of this enzyme class is 3-(hydroxyamino)phenol hydroxymutase. Other names in common use include 3-hydroxylaminophenol mutase, and 3HAP mutase.
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In enzymology, a diaminopimelate epimerase () is an enzyme that catalyzes the chemical reaction :LL-2,6-diaminoheptanedioate \rightleftharpoons meso- diaminoheptanedioate Hence, this enzyme has one substrate, LL-2,6-diaminoheptanedioate, and one product, meso-diaminoheptanedioate. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is LL-2,6-diaminoheptanedioate 2-epimerase. This enzyme participates in lysine biosynthesis.
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In enzymology, a L-arabinose isomerase () is an enzyme that catalyzes the chemical reaction :L-arabinose \rightleftharpoons L-ribulose Hence, this enzyme has one substrate, L-arabinose, and one product, L-ribulose. This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is L-arabinose aldose-ketose-isomerase. This enzyme participates in pentose and glucuronate interconversions.
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