Glycosylases (EC 3.2) are enzymes that hydrolyze glycosyl compounds. They are a type of hydrolase (EC 3). In turn, glycosylases are divided into two groups: glycosidases—enzymes that hydrolyze O- and S-glycosyl compounds (EC 3.2.1) -- and enzymes that hydrolyze N-glycosyl compounds (EC 3.2.2).
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Some 10 years later, ABHD9 was defined to possess the ability to hydrolyze certain fatty acid epoxides.
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The enzyme trypsin can hydrolyze a phosphate-containing peptone. It is used to form a type of organic adhesive.
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This means that L. fusiformis can hydrolyze urea to produce ammonia and CO2.Brink, Benita. "Urease Test Protocol." ASM MicrobeLibrary.
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It has a melting point of around 99 °C. Like most acid anhydrides, it can hydrolyze in the presence of water.
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Ruminants such as cows are able to hydrolyze cellulose into cellobiose and then glucose because of symbiotic bacteria that produce cellulases.
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They also secrete the enzymes disaccharidase and peptidase that hydrolyze disaccharides and polypeptides to monosaccharides and dipeptides to amino acids, respectively.
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Guanylate-binding proteins, such as GBP6, are induced by interferon and hydrolyze GTP to both GDP and GMP (Olszewski et al., 2006 [PubMed 16689661]).
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Because Ti(IV) is a "hard cation", the sulfides of titanium are unstable and tend to hydrolyze to the oxide with release of hydrogen sulfide.
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Toxicity does not seem to constitute a problem in cattle, as the rumen harbors protozoa that hydrolyze OTA. However, contamination of milk is a possibility.
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The primary function of DPEP1 is to hydrolyze various dipeptides in renal metabolism. Specifically, it has been found to hydrolyze glutathione and its conjugates such as leukotriene D (Kozak and Tate, 1982). Several pieces of evidence suggest that DPEP1 is also responsible for the hydrolysis of the beta-lactam ring of various THM-class antibiotics, such as penem and carbapenem (Campbell et al., 1984).
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This is a family of alpha-L-arabinofuranosidases () (CAZY GH_62). These enzymes hydrolyze aryl alpha-L-arabinofuranosides and cleaves arabinosyl side chains from arabinoxylan and arabinan.
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Sodium sulfide affords trithiocarbonate: :Na2S + CS2 → [Na+]2[CS32−] Carbon disulfide does not hydrolyze readily, although the process is catalyzed by an enzyme carbon disulfide hydrolase.
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Some organisms, such as Citrobacter, Providencia, and Serratia, have the ability to become resistant through the development of cephalosporinases (these enzymes hydrolyze cephalosporins and render them inactive).
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The capacity to hydrolyze organophosphates is not unique to bacteria. A few fungi and cyanobacteria species have been found to also hydrolyze OPs. Moreover, through sequence homology searches of whole genomes, several other bacterial species were identified that also contain sequences from the same gene family as opd, including pathogenic bacteria such as Escherichia coli (yhfV) and Mycobacterium tuberculosis. The gene sequence encoding the enzyme (opd) in Flavobacterium sp.
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Silanols are generally synthesized by hydrolysis of halosilanes, alkoxysilanes, or aminosilanes. Chlorosilanes are the most common reactants: :R3Si-Cl + H2O → R3Si-OH + HCl The hydrolysis of fluorosilanes requires more forcing reagents, i.e. alkali. The alkoxysilanes (silyl ethers) of the type R3Si(OR') are slow to hydrolyze. Compared to the silyl ethers, silyl acetates are faster to hydrolyze, with the advantage that the released acetic acid is less aggressive.
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ENPP1 has broad specificity and cleaves a variety of substrates, including phosphodiester bonds of nucleotides and nucleotide sugars. ENPP1 protein may function to hydrolyze nucleoside 5' triphosphates to their corresponding monophosphates and may also hydrolyze diadenosine polyphosphates. The main substrate of ENNP1 is adenosine triphosphate (ATP), which is cleaved into adenosine monophosphate (AMP) and diphosphate. Another notable nucleotide substrate is nicotinamide adenine dinucleotide (NAD+) which can be hydrolyzed to produce AMP.
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Cold solutions of dilute sulphuric or hydrochloric acids are used to hydrolyze the starch, however, this has the disadvantage of also affecting the cellulose fiber in cotton fabrics.
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In an illustrative case, acids accelerate (catalyze) the hydrolysis of esters: :CH3CO2CH3 \+ H2O CH3CO2H + CH3OH At neutral pH, aqueous solutions of most esters do not hydrolyze at practical rates.
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Furthermore, H. larsenii was shown to form indole, hydrolyze gelatin, starch, and Tweens 40 and 80; produce acid from glycerol, maltose, glucose, fructose, and sucrose; and form H2S from thiosulfate.
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Alpha sub-unit of this complex activates the PLC enzyme (PLC-beta) which hydrolyze the PIP2 into DAG. This hydrolysis leads to opening of TRP channels and influx of calcium.
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F1 has a water-soluble part that can hydrolyze ATP. FO on the other hand has mainly hydrophobic regions. FO F1 creates a pathway for protons movement across the membrane.
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E. malodoratus does not produce methylcarbinol or hydrolyze arginine. In carbohydrate and raffinose broths, E. malodoratus forms acid. It does not form endospores thus separating it from bacilli and clostridia species.
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43, 10602–10616, The next steps in the sequence of the hydration reaction involve the generated hydroxide ions as strong nucleophiles, which fully hydrolyze the ring structure in combination with water.
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Along with other species of ectomycorrhizal fungi, C. geophilum produces extracellular enzymes that are able to hydrolyze substrates found in the soil to access and acquire nutrients important to itself and its host plant. The ectomycorrhizas of C. geophilum have been shown to hydrolyze 14C labeled substrate common in plant litters, including hemicellulose and cellulose.Durall, D. M., Todd, A. W., & Trappe, J. M. (1994). Decomposition of 14C‐labelled substrates by ectomycorrhizal fungi in association with Douglas fir.
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G proteins without hydrolytic activity cannot hydrolyze bound GTP. GAPs cannot activate a nonfunctional enzyme, and the G protein is constitutively active, resulting in unregulated cell division and the formation of tumors.
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This gene encodes a member of the palmitoyl protein thioesterase family. The encoded glycosylated lysosomal protein has palmitoyl-CoA hydrolase activity in vitro, but does not hydrolyze palmitate from cysteine residues in proteins.
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Heating the reaction mixture is sufficient to hydrolyze the amide back to the nitrated aniline. In the Wolffenstein–Böters reaction, benzene reacts with nitric acid and mercury(II) nitrate to give picric acid.
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DEAD box, DEAH, and the SKI families of proteins are all referred to as DExD/H box proteins. They are all quite distinct from one another and there is not one protein that belongs to more than one of these families. It is thought that each family may have a specific role in RNA metabolism, for example both DEAD box and DEAH box proteins NTPase activities become stimulated by RNA, but DEAD box proteins specifically hydrolyze ATP whereas DEAH can hydrolyze ATP and other NTPs.
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Some 450 species of snake are venomous. Snake venom is produced by glands below the eye (the mandibular gland) and delivered to the victim through tubular or channeled fangs. Snake venoms contain a variety of peptide toxins, including proteases, which hydrolyze protein peptide bonds, nucleases, which hydrolyze the phosphodiester bonds of DNA, and neurotoxins, which disable signalling in the nervous system. Snake venom causes symptoms including pain, swelling, tissue necrosis, low blood pressure, convulsions, hemorrhage (varying by species of snake), respiratory paralysis, kidney failure, coma and death.
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A combination of Arg-424 and the amino acids that cause the formation of the loop allow the alpha subunit to hydrolyze GM2 gangliosides into GM3 gangliosides by removing the N-acetylgalactosamine (GalNAc) residue from GM2 gangliosides.
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Despite its tendency to hydrolyze, it can be dissolved in alcohols. It is a Lewis acid, as illustrated by its formation of the hexafluorovanadate:Справочник химика / Редкол.: Никольский Б.П. и др.. — 3-е изд., испр. — Л.: Химия, 1971.
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LytC and CwlC are two amidases from the LytC family that hydrolyze the peptidoglycan of the mother cell wall to allow for the release of the mature endospore. CwlC is directly found in the mother cell wall.
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Like most primary enamines, dehydroalanine is unstable. Dehydroalanine hydrolyze to pyruvate. N-Acylated derivatives of dehydroalanine, such as peptides and related compounds, are stable. For example, methyl 2-acetamidoacrylate is the N-acetylated derivative of the ester.
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She carried out the work using four sequential rounds of mutagenesis of the enzyme's gene, expressed by bacteria, through error-prone PCR. After each round she screened the enzymes for their ability to hydrolyze the milk protein casein in the presence of DMF by growing the bacteria on agar plates containing casein and DMF. The bacteria secreted the enzyme and, if it were functional, it would hydrolyze the casein and produce a visible halo. She selected the bacteria that had the biggest halos and isolated their DNA for further rounds of mutagenesis.
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This species also lacks the ability to hydrolyze or metabolize starch, casein, lecithin, alginate or agar. Rarely did this species take up or use either commonly-utilized carbohydrates (e.g. glucose) or amino acids (e.g. glutamine) for its metabolism.
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The organism contains a bacterial microcompartment which is capable of processing propanediol. C. freundii creates a positive MR and negative VP test along with a positive Catalase and negative Oxidase test. C. freundii cannot hydrolyze starch, lipids, or gelatin.
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Punicalagins are water- soluble and hydrolyze into smaller phenolic compounds, such as ellagic acid. There were no toxic effects in rats on a 6% diet of punicalagins for 37 days. In laboratory research, punicalagins had carbonic anhydrase inhibitor activity.
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Simple phosphoranes typically hydrolyze and oxidize readily. They are therefore prepared using air-free techniques. Phosphoranes are more air-stable when they contain an electron withdrawing group attached to the carbon. Some examples are Ph3P=CHCO2R and Ph3P=CHPh.
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It is considered a safer replacement for hydrazoic acid in many reactions. It will however over time hydrolyze to hydrazoic acid and therefore it must be stored free of moisture It has been used in the Oseltamivir total synthesis.
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GTPases are a large family of hydrolase enzymes that bind to the nucleotide guanosine triphosphate (GTP) and hydrolyze it to guanosine diphosphate (GDP). The GTP binding and hydrolysis takes place in the highly conserved G domain common to many GTPases.
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Lipases are used in the degreasing operation to hydrolyze fat particles embedded in the skin. Amylases are used to soften skin, to bring out the grain, and to impart strength and flexibility to the skin. These enzymes are rarely used.
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Phosphodiester bonds, when hydrolyzed, release a considerable amount of free energy. Therefore, nucleic acids tend to spontaneously hydrolyze into mononucleotides. The precursors for RNA are GTP, CTP, UTP and ATP, which is a major source of energy in group-transfer reactions.
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The bacterium is catalase-negative and LAP-positive (like all streptococci), PYR-test and CAMP-test-positive, does not hydrolyze sodium hippurate, and does not grow in bile esculin agar. It does not express any of the known Lancefield antigens.
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Even though the alpha and beta subunits of hexosaminidase A can both cleave GalNAc residues, only the alpha subunit is able to hydrolyze GM2 gangliosides. The alpha subunit contains a key residue, Arg-424, which is essential for binding the N-acetyl-neuramanic residue of GM2 gangliosides. The alpha subunit can hydrolyze GM2 gangliosides because it contains a loop structure consisting of the amino acids: Gly-280, Ser-281, Glu-282, and Pro-283. The loop is absent in the beta subunit, but it serves as an ideal structure for the binding of the GM2 activator protein (GM2AP) in the alpha subunit.
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For C. tropicalis to fully enter and cause infection in the host, it needs some helpers. First, once it is attached onto the host tissues, extracellular enzymes called the proteases will be produced to facilitate the penetration of the pathogen and allow it to interfere with the host defense system. proteases will hydrolyze peptide bonds; secreted aspartic proteases (SAP) support C. tropicalis to be attached and penetrate deep into the tissues to affect the organs. phospholipases will hydrolyze phospholipid; assist to break the epithelial cell membrane structure allowing the hyphal tip to enter into the cytoplasm.
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Pancreatic alpha-amylase 1HNY Amylases are a group of extracellular enzymes (glycoside hydrolases) that catalyze the hydrolysis of starch into maltose. These enzymes are grouped into three classes based on their amino acid sequences, mechanism of reaction, method of catalysis and their structure. The different classes of amylases are α-amylases, β-amylases, and glucoamylases. The α-amylases hydrolyze starch by randomly cleaving the 1,4-a-D-glucosidic linkages between glucose units, β-amylases cleave non- reducing chain ends of components of starch such as amylose, and glucoamylases hydrolyze glucose molecules from the ends of amylose and amylopectin.
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Ulocladium botrytis has cellulolytic ability and contains a cellulose-degrading enzyme complex that can degrade recalcitrant plant litter under alkaline conditions, a trait that is uncommon in other cellulolytic systems. This fungus' ability to hydrolyze cellulose in the solid form is best at a pH of 6.0, as this pH allows maximal growth of U. botrytis under alkaline conditions. In contrast, its ability to hydrolyze liquid cellulose under alkaline conditions is best at a pH of 8.0. Additionally, a new tyrosine kinase (p56tck) inhibitor called ulocladol, with the molecular formula C16H14O7, was found in ethyl acetate extract from U. botrytis.
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Xylanimonas cellulosilytica is a Gram-positive, xylanolytic, aerobic, coccoid and non-motile bacterium from the genus of Xylanimonas which has been isolated from a decayed tree (Ulmus nigra) in Salamanca in Spain. Xylanimonas cellulosilytica has the ability to hydrolyze cellulose and xylan.
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The cells are very short and can occur singly or in masses. These cells are inert in most biochemical tests. They do not hydrolyze starch or aesculin. They cannot reduce nitrate nor do they grow in the presence or absence of carbohydrates.
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Oxalyl chloride reacts with water giving off gaseous products only: hydrogen chloride (HCl), carbon dioxide (CO2), and carbon monoxide (CO). : In this, it is quite different from other acyl chlorides which hydrolyze with formation of hydrogen chloride and the original carboxylic acid.
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Carbapenemases represent type of ESBL which are able to hydrolyze carbapenem antibiotics that are considered as the last-resort treatment for ESBL-producing bacteria. KPC, NDM-1, VIM and OXA-48 carbapenemases have been increasingly reported worldwide as causes of hospital-acquired infections.
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Examples can be found in the Nicolaou taxol total synthesis. tert-Butyldimethylsilyl chloride reacts with alcohols in the presence of base to give tert-butyldimethylsilyl ethers: :(Me3C)Me2SiCl + ROH → (Me3C)Me2SiOR + HCl These silyl ethers hydrolyze much more slowly than the trimethylsilyl ethers.
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Lipases and carboxyl esterases that hydrolyze triglycerides have demonstrated enzymatic activity towards wax esters. Kinetic data show that EPA and DHA provided as wax esters reaches a maximal concentration at approximately 20 h post-consumption, and may indicate delayed absorption of the fatty acids.
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For example, if the arginine of the arginine finger is substituted by lysine, possibly due to a missense mutation, the αR364K mutant results. In the αR364K mutant, the ability of ATP synthase to hydrolyze ATP is decreased around a thousandfold compared to the wild type.
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Quinolone resistance genes are frequently located on the same plasmid as the ESBL genes. Examples of resistance mechanisms include different Qnr proteins, aminoglycose acetyltransferase aac(6')-Ib-cr that is able to hydrolyze ciprofloxacin and norfloxacin, as well as efflux transporters OqxAB and QepA.
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Small GTPases (), also known as small G-proteins, are a family of hydrolase enzymes that can bind and hydrolyze guanosine triphosphate (GTP). They are a type of G-protein found in the cytosol that are homologous to the alpha subunit of heterotrimeric G-proteins, but unlike the alpha subunit of G proteins, a small GTPase can function independently as a hydrolase enzyme to bind to and hydrolyze a guanosine triphosphate (GTP) to form guanosine diphosphate (GDP). The best-known members are the Ras GTPases and hence they are sometimes called Ras subfamily GTPases. A typical G-protein is active when bound to GTP and inactive when bound to GDP (i.e.
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Inorganic materials with highly charged anions are often susceptible to protonolysis. Derivatives of nitride (N3−), phosphides (P3−), and silicides (Si4−) hydrolyze to give ammonia, phosphine, and silane. Analogous reactions occur with molecular compounds with M-NR2, M-PR2, and M-SiR3 bonds.Greenwood, N. N.; & Earnshaw, A. (1997).
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After ruling out other causes, the authors tentatively attributed the positive results in the first trial to "chance". AstraZeneca then terminated the development programme. PBN and its derivatives hydrolyze and oxidize in vitro to form respectively MNP-OH (AKA, NtBHA) and its parent spin-trap MNP.
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In peptone-yeast extract-iron agar, A. italicus produces H2S. Within a skim milk agar medium, it was able to hydrolyze casein. Other notable physiological characteristics include its ability to liquefy gelatin, produce tyrosinase, and peptonization without coagulation. The optimal temperature ranges between 28 and 37 °C.
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The most successful enrichments of this species come from proprionate and organic acids. Under photoheterotrophic conditions, R. capsulatus strain B10 is capable of using acetate as its sole carbon source, but the mechanisms of this have not been identified. The strains studied do not hydrolyze gelatin.
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Arylsulfonic acids are susceptible to hydrolysis, the reverse of the sulfonation reaction. Whereas benzene sulfonic acid hydrolyzes above 200 ″C, most related derivatives are easier to hydrolyze. Thus, heating aryl sulfonic acids in aqueous acid produces the parent arene. This reaction is employed in several scenarios.
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Aminopeptidases hydrolyze N-terminal amino acids of proteins or peptide substrates. Major histocompatibility complex (MHC) class I molecules rely on aminopeptidases such as ERAP1 and LRAP to trim precursors to antigenic peptides in the endoplasmic reticulum (ER) following cleavage in the cytoplasm by tripeptidyl peptidase II (TPP2).
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Silicon tetrabromide is the inorganic compound with the formula SiBr4. This colorless liquid has a suffocating odor due to its tendency to hydrolyze with release of hydrogen bromide.Encyclopedia of Inorganic Chemistry; King, B. R.; John Wiley & Sons Ltd.: New York, NY, 1994; Vol 7, pp 3779-3782.
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This method results in oligogalacturonides. Exo-PGs hydrolyze at the non-reducing end of the polymer, generating a monosaccharide galacturonic acid. Occasionally, organisms employ both methods. In addition to different modes of action, PG polymorphism allows fungal PGs to more effectively degrade a wider range of plant tissues.
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Several bacteria from the genus Amycolatopsis are able to enzymatically hydrolyze the ester bonds of poly-lactic acid (PLA) films in aquatic medium. So far, it is one of the few known bacteria able to biodegrade the bioplastic outside compost facilities in a relatively short period of time.
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This method of synthesizing amides is industrially important, and has laboratory applications as well.Wade 2010, pp. 964–965. In the presence of a strong acid catalyst, carboxylic acids can condense to form acid anhydrides. The condensation produces water, however, which can hydrolyze the anhydride back to the starting carboxylic acids.
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DUE-B's hydrolyze ATP In order to function. Also possess similar sequence to aminoacyl-tRNA synthetase, and were previously classified a such. DUE-Bs form homodimers that create an extended beta-sheet secondary structure extending across it. Two of these homodimers come together to form the overall asymmetric DUE-B structure.
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Aminoacylase 2 deficiency - also known as Canavan's disease - is another rare disease caused by a mutation in the ASPA gene (on chromosome 17) that leads to a deficiency in the enzyme aminoacylase 2. Aminoacylase 2 is known for the fact that it can hydrolyze N-acetylaspartate while aminoacylase 1 cannot.
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Other significant compounds produced include of B-galactosidase, 4-hydroxyradianthin and Curvularone A. The species is able to produce large amounts of B-galactosidase, which can hydrolyze lactose in acid whey. C. inaequalis also contains 4-hydroxyradianthin and Curvularone A compounds which have been identified as potential anti-tumor agents.
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This makes it hard to excrete TEPP. Many enzymes hydrolyze TEPP, especially the phosphotriesterases (PTEs). In the serum and the liver, there is a significant higher PTE activity found than in other tissues of mammals. PTEs are responsible for the cleavage of the bond between the phosphorus atom and the leaving group.
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Invertases and sucrases hydrolyze sucrose to give the same mixture of glucose and fructose. Invertases cleave the O-C(fructose) bond, whereas the sucrases cleave the O-C(glucose) bond. For industrial use, invertase is usually derived from yeast. It is also synthesized by bees, which use it to make honey from nectar.
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Dipeptidase 2 (DPEP2) is a protein which in humans is encoded by the DPEP2 gene. DPEP2 belongs to the membrane-bound dipeptidase (EC 3.4.13.19) family. These enzymes hydrolyze a variety of dipeptides, including leukotriene D4, the beta-lactam ring of some antibiotics, and cystinyl-bis-glycine (cys-bis-gly) formed during glutathione degradation.
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Water is a common reagent in enzymatic catalysis. Esters and amides are slow to hydrolyze in neutral water, but the rates are sharply affected by metalloenzymes, which can be viewed as large coordination complexes. Acrylamide is prepared by the enzyme-catalyzed hydrolysis of acrylonitrile. US demand for acrylamide was as of 2007.
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Detoxification can take place by removing one glucose residue. Other fungal species hydrolyze tomatine to the less toxic aglycon tomatidine by removing all the sugar residues. Tomatidine can still inhibit some fungal species, but is less toxic than tomatine. The metabolic pathway of hydrolysis of tomatine is different for different types of fungi.
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The species was discovered during a survey for bacteria with keratinase activity. T. terrae was the second species added to the genus Terrabacter after the type species, T. tumescens, was added to the novel genus in 1989. T. terrae can grow in the 15-40 °C range, and is able to hydrolyze keratin.
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L. fusiformis can hydrolyze casein and gelatin. It can also utilize acetate, citrate, formate, lactate, and succinate as carbon sources. From a metabolic standpoint, L. fusiformis and Lysinibacillus sphaericus are nearly identical. As of now, the only known factor that distinguishes these two species is that L. fusiformis is positive for urease.
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Complexes of oxophilic metals typically are prone to hydrolysis. For example, the high valent chlorides hydrolyze rapidly to give oxides: :TiCl4 \+ 2 H2O → TiO2 \+ 4 HCl These reactions proceed via oxychloride intermediates. For example, WOCl4 results from the partial hydrolysis of tungsten hexachloride. Hydroxide- containing intermediates are rarely observed for oxophilic metals.
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ABCA12 is an ATP-binding cassette transporter (ABC transporter), which are members of a large family of proteins that hydrolyze ATP to transport cargo across cell membranes. ABCA12 is thought to be a lipid transporter in keratinocytes necessary for lipid transport into lamellar granules during the formation of the lipid barrier in the skin.
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Enterococcus colonies (black) growing on BEA Bile salts are the selective ingredient, while esculin is the differential component. Enterococcus hydrolyze esculin to products that react with ferric citrate in the medium to produce insoluble iron salts, resulting in the blackening of the medium. Test results must be interpreted in conjunction with gram stain morphology.
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Bile Esculin Agar is used primarily to differentiate Enterococcus from Streptococcus. Members of the genus Enterococcus are capable of growing in the presence of 40% bile (oxgall) and hydrolyzing esculin to glucose and esculetin. Esculetin combines with ferric ions to produce a black complex. For some purposes, certain bacteria are able to hydrolyze aesculin.
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These compounds are stable while solid and may be used in powdered, granular, or tablet form. When added in small amounts to pool water or industrial water systems, the chlorine atoms hydrolyze from the rest of the molecule, forming hypochlorous acid (HOCl), which acts as a general biocide, killing germs, microorganisms, algae, and so on.
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The sulfite process is acidic and one of the drawbacks is that the acidic conditions hydrolyze some of the cellulose, which means that sulfite pulp fibers are not as strong as kraft pulp fibers. The yield of pulp (based on wood used) is higher than for kraft pulping and sulfite pulp is easier to bleach.
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They also hydrolyze long-chain fatty acid esters and thioesters. The specific function of this enzyme has not yet been determined; however, it is speculated that carboxylesterases may play a role in lipid metabolism and/or the blood–brain barrier system. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.
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In the Horner–Wadsworth–Emmons reaction and the Seyferth–Gilbert homologation, phosphonates are used in reactions with carbonyl compounds. The Kabachnik–Fields reaction is a method for the preparation of aminophosphonates. These compounds contain a very inert bond between phosphorus and carbon. Consequently, they hydrolyze to give phosphonic and phosphinic acid derivatives, but not phosphate.
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TiCl4 is a Lewis acid as implicated by its tendency to hydrolyze. With the ether THF, TiCl4 reacts to give yellow crystals of TiCl4(THF)2. With chloride salts, TiCl4 reacts to form sequentially [Ti2Cl9]−, [Ti2Cl10]2− (see figure above), and [TiCl6]2−. The reaction of chloride ions with TiCl4 depends on the counterion.
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The racemic diamine can also be used for the preparation of specific polyamides and after reaction with phosgene to form 2-methylpentane diisocyanate as a reaction component in polyurethanes. Nitrilases regioselectively hydrolyze the ω-nitrile group in α, ω-dinitriles without detectable amide intermediate directly to the carboxyl group. 4-cyanopentanoic acid is formed in high yield.
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The cauxin found in seminal fluid is produced by epidydimal cells. The concentration in seminal fluid is much lower than its concentration of urine. The role of cauxin as an esterase allows it to hydrolyze specific monoacylglycerols, suggesting that it is involved in lipid transfer and metabolism. It is also theorized to play a role in fertilization.
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Chymotrypsin-like elastase family member 1 (CELA1) also known as elastase-1 (ELA1) is an enzyme that in humans is encoded by the CELA1 gene. Elastases form a subfamily of serine proteases that hydrolyze many proteins in addition to elastin. Humans have six elastase genes which encode the structurally similar proteins elastase 1, 2, 2A, 2B, 3A, and 3B.
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Alkali metal ions may migrate through plastic packaging and influence the functioning of semiconductors. Chlorinated hydrocarbon residues may hydrolyze and release corrosive chlorides; these are problems that occur after years. Polar molecules may dissipate high-frequency energy, causing parasitic dielectric losses. Above the glass transition temperature of PCBs, the resin matrix softens and becomes susceptible contaminant diffusion.
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Diallyl disulfide can be readily oxidized to allicin with hydrogen peroxide or peracetic acid. Allicin in turn can hydrolyze giving diallyl disulfide and trisulfide. Reaction of diallyl disulfide with liquid sulfur gives a mixture containing diallyl polysulfides with as many as 22 sulfur atoms in a continuous chain. When diallyl disulfide is heated it decomposes giving a complex mixture.
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The strains of Cedecea appear to be similar to those of Serratia. Both Cedecea and Serratia are lipase positive and resistant to colistin and cephalothin; however, Cedecea is unable to hydrolyze gelatin or DNA.Farmer III, J. J., Sheth, N. K., Hudzinski, J. A., Rose, H. D., Asbury, M. F. (1982). Bacteremia due to Cedecea neteri sp. nov.
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Acetyl chloride is not expected to exist in nature, because contact with water would hydrolyze it into acetic acid and hydrogen chloride. In fact, if handled in open air it releases white "smoke" resulting from hydrolysis due to the moisture in the air. The smoke is actually small droplets of hydrochloric acid and acetic acid formed by hydrolysis.
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Propane-1,3-sultone Cyclic sulfonic esters are called sultones.R. J. Cremlyn “An Introduction to Organosulfur Chemistry” John Wiley and Sons: Chichester (1996) One example is propane-1,3-sultone. Some sultones are short-lived intermediates, used as strong alkylating agents to introduce a negatively charged sulfonate group. In the presence of water, they slowly hydrolyze to the hydroxy sulfonic acids.
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Acyl-protein thioesterases are enzymes that cleave off lipid modifications on proteins, located on the sulfur atom of cysteine residues linked via a thioester bond. Acyl-protein thioesterases are part of the α/β hydrolase superfamily of proteins and have a conserved catalytic triad. For that reason, acyl-protein thioesterases are also able to hydrolyze oxygen-linked ester bonds.
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Acylphosphatase can hydrolyze the phosphoenzyme intermediate of different membrane pumps, particularly the Ca2+/Mg2+-ATPase from sarcoplasmic reticulum of skeletal muscle. Two isoenzymes have been isolated, called muscle acylphosphatase and erythrocyte acylphosphatase on the basis of their tissue localization. This gene encodes the muscle-type isoform (MT). An increase of the MT isoform is associated with muscle differentiation.
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Ectonucleoside triphosphate diphosphohydrolase 2 is an enzyme that in humans is encoded by the ENTPD2 gene. The protein encoded by this gene is the type 2 enzyme of the ecto-nucleoside triphosphate diphosphohydrolase family (E-NTPDase). E-NTPDases are a family of ecto-nucleosidases that hydrolyze 5'-triphosphates. This ecto-ATPase is an integral membrane protein.
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CwlC is found in the mother cell wall and functions for the lysis of the mother cell wall. CwlC does not have a signal sequence but participates in late sporulation and is present in the cell wall. It was found in B. subtilis that CwlC is able to hydrolyze both vegetative cell walls and spore peptidoglycan.
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This fact, in combination with the bile salt deficiency and low pH throughout the gastrointestinal tract of the neonate, demands that lingual lipase be the main enzyme catalyzing the hydrolysis of dietary fat. This enzyme activity has been seen as early as 26 weeks gestational age, with ability to hydrolyze dietary fats variable according to digestive tract maturity.
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G. candidum reduces the bitterness in Camembert cheese through the activity of the aminopeptidases that hydrolyze low molecular weight hydrophobic peptides. Aminopeptidases also contributes an aroma in traditional Norman Camembert. The fungus also neutralizes the curd by catabolizing lactic acid produced by bacteria. G. candidum prepares the cheese for colonization of other acid sensitive bacteria such as Brevibacterium.
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Cellulases and hemicellulases (including xylanases) are also used in the paper and pulp industry to de-ink recycled fibers, modify coarse mechanical pulp, and for the partial or complete hydrolysis of pulp fibers. Cellulases and hemicellulases are used in these industrial applications due to their ability to hydrolyze the cellulose and hemicellulose components found in these materials.
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When a photon enters the eye, it is sent to the back of the eye and is absorbed by rods and cones. These cells are excited by the photon and as a response hydrolyze the GTP and cGMP. This finding proved to be the rate limiting step. This causes gated channels to close and create a polarity.
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V-type ATPase serves the opposite function as F-type ATPase and is used in plants to hydrolyze ATP to create a proton gradient. Examples of this are lysosomes that use V-type ATPase acidify vesicles or plant vacuoles during process of photosynthesis in the chloroplasts. This process can be regulated through various methods such as pH.
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In addition, some members of the PLD superfamily may employ primary alcohols such as ethanol or 1-butanol in the cleavage of the phospholipid, effectively catalyzing the exchange the polar lipid headgroup. Other members of this family are able hydrolyze other phospholipid substrates, such as cardiolipin, or even the phosphodiester bond constituting the backbone of DNA.
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Animation of the microtubule dynamic instability. Tubulin dimers bound to GTP (red) bind to the growing end of a microtubule and subsequently hydrolyze GTP into GDP (blue). Dynamic instability refers to the coexistence of assembly and disassembly at the ends of a microtubule. The microtubule can dynamically switch between growing and shrinking phases in this region.
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The majority of Streptococcus anginosus strains produce acetoin from glucose, ferment lactose, trehalose, salicin, and sucrose, and hydrolyze esculin and arginine. Carbon dioxide can stimulate growth or is even required for growth in certain strains. Streptococcus anginosus may be beta-hemolytic or nonhemolytic. The small colonies often give off a distinct odor of butterscotch or caramel.
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Another hypothesis is based on the specific binding with receptors and proteins to create intracellular enzyme dependent and independent reactions. Membrane damage by the PLA2 activity allows PLA2 to enter cells and specifically bind to proteins and receptors either agonistic or antagonistic, inducing pharmacological effects non-enzymatically. The intracellular PLA2 could also remain enzymatically active and hydrolyze membrane phospholipids.
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In CMRD, a mutation of this genomic sequence affects the Sar1B enzyme's ability to interact with Guanine Exchange Factors (GEFs) and GTP-Activating Proteins (GAPs). The mutation of exon 6 of the sequence can eliminate the critical chain that is responsible for recognizing guanine. This strips the GTPase of its capability to hydrolyze GTP, its hallmark trait.
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Carboxylesterase 1 is a serine esterase and member of a large multigene carboxylesterase family. It is also part of the alpha/beta fold hydrolase family. These enzymes are responsible for the hydrolysis of ester- and amide-bond-containing xenobiotics and drugs such as cocaine and heroin. They also hydrolyze long-chain fatty acid esters and thioesters.
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The liquid center found in some cordials is made using invertase to hydrolyze sucrose in the filling, a process that can take up to two weeks. This makes it a requirement to age the cordials in storage before consuming them to ensure the filling has become liquid. Some fillings include cherry, strawberry, raspberry and blueberry.LaBau, Elizabeth.
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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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Amylases are secreted proteins that hydrolyze 1,4-alpha-glucoside] bonds in oligosaccharides and polysaccharides, and thus catalyze the first step in digestion of dietary starch and glycogen. The human genome has a cluster of several amylase genes that are expressed at high levels in either salivary gland or pancreas. This gene encodes an amylase isoenzyme produced by the pancreas.
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N-ATPases are a group of F-type ATPases without a delta/OSCP subunit, found in bacteria and a group of archaea via horizontal gene transfer. They transport sodium ions instead of protons and tend to hydrolyze ATP. They form a distinct group that is further apart from usual F-ATPases than A-ATPases are from V-ATPases.
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The soil's pH also has a strong effect on the amount of volatilization. Specifically, highly alkaline soils (pH~8.2 or higher) have proven to increase urea hydrolysis. One study has shown complete hydrolysis of urea within two days of application on such soils. In acidic soils (pH 5.2) the urea took twice as long to hydrolyze.
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Ileum, caecum and colon of rabbit, showing Appendix vermiformis on fully functional caecum. The human vermiform appendix on the vestigial caecum. In modern humans, the appendix is a vestige of a redundant organ that in ancestral species had digestive functions, much as it still does in extant species in which intestinal flora hydrolyze cellulose and similar indigestible plant materials.Darwin, Charles (1871).
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Biochemical tests indicate this microorganism also carries out a weakly positive reaction to the nitrate reductase test. It is positive for urease production, is oxidase negative, and can use glucose, sucrose, and lactose to form acid products. In the presence of lactose, it will also produce gas. S. epidermidis does not possess the gelatinase enzyme, so it cannot hydrolyze gelatin.
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Alkenes add to OsO4 to give diolate species that hydrolyze to cis-diols. The net process is called dihydroxylation. This proceeds via a [3 + 2] cycloaddition reaction between the OsO4 and alkene to form an intermediate osmate ester which rapidly hydrolyses to yield the vicinal diol. As the oxygen atoms are added in a concerted step, the resulting stereochemistry is cis.
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For some of these antimetabolites, the intracellular triphosphate form of the analog is the active compound. SAMHD1 has been shown to be able to hydrolyze arabinose 5’-triphosphates. SAMHD1 has been shown to be a biomarker and influence arabinose C (ara-C; cytarabine) responsiveness. Viral protein x (Vpx) has been proposed to be potential therapy to improve cytarabine therapy for hematological malignancies.
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Type I inositol-1,4,5-trisphosphate 5-phosphatase is an enzyme that in humans is encoded by the INPP5A gene. The protein encoded by this gene is a membrane- associated type I inositol 1,4,5-trisphosphate (InsP3) 5-phosphatase. InsP3 5-phosphatases hydrolyze Ins(1,4,5)P3, which mobilizes intracellular calcium and acts as a second messenger mediating cell responses to various stimulation.
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Kinesins are structurally related to G proteins, which hydrolyze GTP instead of ATP. Several structural elements are shared between the two families, notably the Switch I and Switch II domain. Mobile and self-inhibited conformations of kinesin-1. Self-inhibited conformation:IAK region of the tail (green) binds to motor domains (yellow and orange) to inhibit the enzymatic cycle of kinesin-1.
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PON was identified as an enzyme having organophosphates as its substrates. Reports of the geographic differences in population frequencies of paraoxonase activity and genetic analysis led to uncovering the genetic polymorphism. The name paraoxonase was given because of its ability to hydrolyze paraoxon, a toxic metabolite that comes from pesticide parathion. The 3D crystal structure of PON1 was determined in 2004.
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Subcutaneous zygomycosis (also known as "entomophthoromycosis basidiobolae", subcutaneous phycomycosis, and basidiobolomycosis) is a both human and non-human animal disease or lesion caused by the granulomatous infection of subcutaneous tissue by B. ranarum. Several enzymes produced by B. ranarum, including lipase and protease, might hydrolyze and utilize the fatty tissues of the host and contribute to the pathogenesis of the infection.
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There, within one polymeric chain, all the halide atoms lie in one graphite-like plane and form planar pentagons around the protactinium ions. The coordination 7 of protactinium originates from the 5 halide atoms and two bonds to protactinium atoms belonging to the nearby chains. These compounds easily hydrolyze in water. The pentachloride melts at 300 °C and sublimates at even lower temperatures.
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Activators increase the penetration rate; for dichloromethane water is suitable, other choices are amines, strong acids or strong alkalis. The activator's role is to disrupt the molecular and intermolecular bonds in the paint film and assist with weakening this. Its composition depends on the character of the paint to be removed. Mineral acids are used for epoxy resins to hydrolyze their ether bonds.
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Many organisms have metabolic pathways to synthesize and break down purines. Purines are biologically synthesized as nucleosides (bases attached to ribose). Accumulation of modified purine nucleotides is defective to various cellular processes, especially those involving DNA and RNA. To be viable, organisms possess a number of (deoxy)purine phosphohydrolases, which hydrolyze these purine derivatives removing them from the active NTP and dNTP pools.
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Starch molecules, for example, are too large to be absorbed from the intestine, but enzymes hydrolyze the starch chains into smaller molecules such as maltose and eventually glucose, which can then be absorbed. Different enzymes digest different food substances. In ruminants, which have herbivorous diets, microorganisms in the gut produce another enzyme, cellulase, to break down the cellulose cell walls of plant fiber.
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In contrast, the anhydrous halides of the later metals tend to hydrate, not hydrolyze, and they often form hydroxides. Reduced complexes of oxophilic metals tend to generate oxides by reaction with oxygen. Typically the oxide- ligand is bridging, e.g. :2 (C5H5)2TiCl + 1/2 O2 → {(C5H5)2TiCl}2O Only in rare cases do the products of oxygenation feature terminal oxo ligands.
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CaM will then bind to the CNG channel and close it, stopping the sodium and calcium influx. CaMKII will be activated by the presence of CaM, which will phosphorylate ACIII and reduce cAMP production. CaMKII will also activate phosphodiesterase, which will then hydrolyze cAMP. The effect of this negative feedback response inhibits the neuron from further activation when another odor molecule is introduced.
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Due to its availability and low cost, it has been used by criminals to dispose of corpses. Italian serial killer Leonarda Cianciulli used this chemical to turn dead bodies into soap. In Mexico, a man who worked for drug cartels admitted disposing of over 300 bodies with it. Sodium hydroxide is a dangerous chemical due to its ability to hydrolyze protein.
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Many alternative reagents have been developed to complement the use of phthalimides. Most such reagents (e.g. the sodium salt of saccharin and di- tert-butyl-iminodicarboxylate) are electronically similar to the phthalimide salts, consisting of imido nucleophiles. In terms of their advantages, these reagents hydrolyze more readily, extend the reactivity to secondary alkyl halides, and allow the production of secondary amines.
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The "glutamine switch" is an invariant glutamine found in all PDEs, for which the crystal structure has been solved. In PDE2, this residue is the Gln859. It has potential to form hydrogen bonds with the exocyclic amino group of cAMP and the exocyclic carbonyl oxygen of cGMP. In PDEs, which can hydrolyze both cAMP and cGMP, this glutamine is able to rotate freely.
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The energy of an absorbed photon is transferred to electrons in the molecule and briefly changes their configuration (i.e., promotes the molecule from a ground state to an excited state). The excited state represents what is essentially a new molecule. Often excited state molecules are not kinetically stable in the presence of O2 or H2O and can spontaneously decompose (oxidize or hydrolyze).
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The protein precipitate formed in saliva is normally rich in calcium and low in solubility. Also, alpha-amylase contains a significant level of sialic acid. When alpha-amylase combines with saliva, the enzymes hydrolyze and release the sialic acid, forming another water-insoluble precipitate. These two precipitates combine to form an impenetrable layer on the reed, which prevent the reed from fully hydrating.
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Oxidized silicon has been extensively studied as a substrate for the deposition of biomolecules. Piranha solution can be used to increase the surface density of reactive hydroxyl groups on the surface of silicon. The –OH groups can hydrolyze and subsequently form siloxane linkages (Si-O-Si) with organic silane molecules. Preparation of silicon surfaces for silanization involves the removal of surface contaminants.
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The protein binds to phosphoinositide lipids through the PH-GRAM domain, and can hydrolyze phosphatidylinositol(3)-phosphate and phosphatidylinositol(3,5)-biphosphate in vitro. The encoded protein has been observed to have a perinuclear, possibly membrane-bound, distribution in cells, but it has also been found free in the cytoplasm. Multiple transcript variants encoding different isoforms have been found for this gene.
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In fact, zingibain is the only catalogued plant protease with collagenolytic activity. Zingibain may be a preferable meat tenderizer to papain due to the resulting texture of meat produced. While papain can hydrolyze actomyosin, it also breaks down other major tissue proteins, that lead to a mushy meat texture. The specificity of zingibain's binding ensures predominant hydrolyzation of actomyosin and Type I collagen.
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Unlike tissue carnosinase, serum carnosinase also hydrolyzes the GABA metabolite homocarnosine. Homocarnosinosis, a neurological disorder resulting in an excess of homocarnosine in the brain, though unaffected by tissue carnosinase, is caused by a deficiency of serum carnosinase in its ability to hydrolyze homocarnosine. A deficiency of tissue and serum carnosinase, with serum being an indicator, is the underlying metabolic cause of carnosinemia.
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Lactobacillus plantarum strain K21 is a gram-positive bacteria isolated from locally fermented vegetables. It has the ability to hydrolyze bile salt when it is provided as a supplement. K21 also reduces the levels of cholesterol and triglyceride, and inhibits the accumulation of lipid in 3T3-L1 preadipocytes. Furthermore, it reduces the level of plasma leptin, mitigates liver damage and alleviates glucose intolerance.
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Even though the alpha and beta subunits of lysosomal hexosaminidase can both cleave GalNAc residues, only the alpha subunit is able to hydrolyze GM2 gangliosides because of a key residue, Arg-424, and a loop structure that forms from the amino acid sequence in the alpha subunit. The loop in the alpha subunit, consisting of Gly-280, Ser-281, Glu-282, and Pro-283 which is absent in the beta subunit, serves as an ideal structure for the binding of the GM2 activator protein (GM2AP), and arginine is essential for binding the N-acetyl- neuraminic acid residue of GM2 gangliosides. The GM2 activator protein transports GM2 gangliosides and presents the lipids to hexosaminidase, so a functional hexosaminidase enzyme is able to hydrolyze GM2 gangliosides into GM3 gangliosides by removing the N-acetylgalactosamine (GalNAc) residue from GM2 gangliosides.
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However, the only mammals that have cauxin present in urine are cats. It is also the first carboxylesterase to be found in urine. Cauxin has been shown to hydrolyze 3-methylbutanol-cysteinylglycine (3-MBCG) in the urine into felinine which then slowly degrades into the putative, sulfur-containing cat pheromone 3-mercapto-3-methylbutan-1-ol (MMB). This pheromone is used to mark territory with urine.
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Another way that Foxp3 helps keep the autoimmune system at homeostasis is through its regulation of the expression of suppression- mediating molecules. For instance, Foxp3 is able to facilitate the translocation of extracellular adenosine into the cytoplasm. It does this by recruiting CD39, a rate-limiting enzyme that's vital in tumor suppression to hydrolyze ATP to ADP in order to regulate immunosuppression on different cell populations.
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In most GTPases, the specificity for the base guanine versus other nucleotides is imparted by the base-recognition motif, which has the consensus sequence [N/T]KXD. Note that while tubulin and related structural proteins also bind and hydrolyze GTP as part of their function to form intracellular tubules, these proteins utilize a distinct tubulin domain that is unrelated to the GTPase domain used by signaling GTPases.
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The Weimberg pathway is an oxidative pathway where the D-xylose is oxidized to D-xylono-lactone by a D-xylose dehydrogenase followed by a lactonase to hydrolyze the lactone to D-xylonic acid. A xylonate dehydratase is splitting off a water molecule resulting in 2-keto 3-deoxy- xylonate. A second dehydratase forms the 2-keto glutarate semialdehyde which is subsequently oxidised to 2-ketoglutarate.
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Cellulose pulp may also be treated with strong acid to hydrolyze the amorphous fibril regions, thereby producing short rigid cellulose nanocrystals a few 100 nm in length. These nanocelluloses are of high technological interest due to their self-assembly into cholesteric liquid crystals, production of hydrogels or aerogels, use in nanocomposites with superior thermal and mechanical properties, and use as Pickering stabilizers for emulsions.
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Enzymes like proteases, lipases, and amylases have an important role in the soaking, dehairing, degreasing, and bating operations of leather manufacturing. Proteases are the most commonly used enzymes in leather production. The enzyme must not damage or dissolve collagen or keratin, but should hydrolyze casein, elastin, albumin, globulin-like proteins, and nonstructural proteins that are not essential for leather making. This process is called bating.
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The disulfide bridge between Cys42-Cys58 forms part of the fibrinogen recognition subsite S’ that is recognized as crucial for thrombin's ability to hydrolyze alpha- and beta-chains. Mutations within the S’ site have shown a decrease in the thrombin-facilitated fibrinogenolysis. However, the lack of a Cys, and therefore disulfide bridge in that region, in cerastocytin has no effect on fibrin clot formation or platelet aggregation.
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Soil microorganisms transform heptachlor by epoxidation, hydrolysis, and reduction. When the compound was incubated with a mixed culture of organisms, chlordene (hexachlorocyclopentadine, its precursor) formed, which was further metabolized to chlordene epoxide. Other metabolites include 1-hydroxychlordene, 1-hydroxy-2,3-epoxychlordene, and heptachlor epoxide. Soil microorganisms hydrolyze heptachlor to give ketochlordene. Rats metabolize heptachlor to the epoxide 1-exo-1-hydroxyheptachlor epoxide and 1,2-dihydrooxydihydrochlordene.
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The Z-ring forms from smaller subunits of FtsZ filaments. These filaments may pull on each other and tighten to divide the cell. Super-resolution image of Z-rings (green) at different stages of constriction in two E. coli cells. FtsZ has the ability to bind to GTP and also exhibits a GTPase domain that allows it to hydrolyze GTP to GDP and a phosphate group.
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At least 10 different enzymes or proteins participate in the initiation phase of replication. They open the DNA helix at the origin and establish a prepriming complex for subsequent reactions. The crucial component in the initiation process is the DnaA protein, a member of the AAA+ ATPase protein family (ATPases associated with diverse cellular activities). Many AAA+ ATPases, including DnaA, form oligomers and hydrolyze ATP relatively slowly.
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CTAB formed micelles in the solution and these micelles further formed a two dimensional hexagonal mesostructure. The silicon precursor began to hydrolyze between the micelles and finally filled the gap with silicon dioxide. The template could be further removed by calcination and left a pore structure behind. These pores mimicked exactly the structure of mesoscale soft template and led to highly ordered mesoporous silica materials.
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Four varieties of bacteria have been found in the bee bread of the larva: Bacillus circulans, B. coagulans, B. firmus, and B. megaterium. Only the Bacillus genus has been found in the samples taken. Together, these four species were able to hydrolyze starch, ferment glucose, convert nitrates to nitrites, and produce dihydroxyacetone from glycerol. This group of bacteria also lowers the pH of the bee bread.
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Studies have shown that at temperatures above 70 °C, and high humidity, polycarbonate will hydrolyze to Bis-phenol A (BPA). This condition is similar to that observed in most incinerators. After about 30 days at 85°C / 96% RH, surface crystals are formed which for 70% consisted of BPA. BPA is a compound that is currently on the list of potential environmental hazardous chemicals.
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Under normal circumstances, caspases recognize tetra- peptide sequences on their substrates and hydrolyze peptide bonds after aspartic acid residues. Caspase 3 and caspase 7 share similar substrate specificity by recognizing tetra-peptide motif Asp-x-x-Asp. The C-terminal Asp is absolutely required while variations at other three positions can be tolerated. Caspase substrate specificity has been widely used in caspase based inhibitor and drug design.
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When the degradation of BBP is taken into consideration, one should be aware of the fact that it contains two ester functional groups. This gives organisms a handle for biotransformations. The ester groups gives BBP hydrophilic properties and will therefore hydrolyze fairly easy. Following an examination performed in 1997, it was found that biotransformations play a very important role in the degeneration of BBP.
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Endothelial lipase (LIPG) is a form of lipase secreted by vascular endothelial cells in tissues with high metabolic rates and vascularization, such as the liver, lung, kidney, and thyroid gland. The LIPG enzyme is a vital component to many biological process. These processes include lipoprotein metabolism, cytokine expression, and lipid composition in cells. Unlike the lipases that hydrolyze Triglycerides, endothelial lipase primarily hydrolyzes phospholipids.
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A chemical depilatory is a cosmetic preparation used to remove hair from the skin. Common active ingredients are salts of thioglycolic acid and thiolactic acids. These compounds break the disulfide bonds in keratin and also hydrolyze the hair so that it is easily removed. Formerly, sulfides such as strontium sulfide were used, but due to their unpleasant odor, they have been replaced by thiols.
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The toxicity of chlorfenvinphos is primarily caused by its inhibition of cholinesterase activity. Chlorfenvinphos reacts with the acetylcholine binding sites of enzymes that hydrolyze acetylcholine, thereby preventing their catalysis of this reaction. The reaction itself is a phosphorylation, which is reversible. The phosphorylated enzymes can undergo conformational changes and additional reactions however, which prevent the dephosporylation. This “aging” results in irreversible inhibition of the cholinesterase.
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Dipeptidases are enzymes secreted by enterocytes into the small intestine. Dipeptidases hydrolyze bound pairs of amino acids, called dipeptides. Dipeptidases are secreted onto the brush border of the villi in the small intestine, where they cleave dipeptides into their two component amino acids prior to absorption. DIPEPTIDASES convert dipeptides into amino acids Dipeptidases are also found within the enterocytes themselves, performing cytosolic digestion of absorbed dipeptides.
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Growth on peptone-yeast extract-glucose broth cultures with 20% bile yields vast amounts of acetate and succinate but minor amounts of propionate and isovalerate. Lactate and threonine are not used by the type strain. B. caccae produces a trace amount of (0.1%) of hydrogen. They hydrolyze esculin, weakly digest gelatin, and are susceptible to chloramphenicol and clindamycin, but not susceptible to penicillin G and tetracycline.
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Depending on purity, samples can appear yellow-green to grey. The compound was discovered by G. Lemoine and first produced safely in commercial quantities in 1898 by Albright and Wilson. It dissolves in an equal weight of carbon disulfide (CS2), and in a 1:50 weight ratio of benzene. Unlike some other phosphorus sulfides, P4S3 is slow to hydrolyze and has a well-defined melting point.
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These compounds are stable while solids and may be used in powdered, granular, or tablet form. When added in small amounts to pool water or industrial water systems, the chlorine atoms hydrolyze from the rest of the molecule forming hypochlorous acid (HOCl) which acts as a general biocide killing germs, micro-organisms, algae, and so on. Halogenated hydantoin compounds are also used as biocides.
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Degradation is carried out primarily by a class of enzymes known as phosphodiesterases (PDEs). In mammalian cells, there are 11 known PDE families with varying isoforms of each protein expressed based on the cell's regulatory needs. Some phosphodiesterases are cNMP-specific, while others can hydrolyze non- specifically. However, the cAMP and cGMP degradation pathways are much more understood than those for either cCMP or cUMP.
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T. flagellatus was the third species of Tumebacillus to be discovered, but was the first found to be motile. T. flagellatus was found during a survey for bacteria that were able to hydrolyze pullulan or starch. The optimum growth temperature for T. flagellatus is 37 °C, and can grow in the 20-42 °C range. Its optimum pH is 5.5, and grows in pH range 4.5-8.5.
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As stated above, ethiofencarb is stable in acidic conditions, but hydrolyzes when in the presence of a base. It was found to rapidly hydrolyze at pH conditions of 9 and 12. When subjected to sunlight, the main products that resulted from photodegredation are 2-hydroxybenzaldehyde and 3-methylbenzo[e-1,3]oxazine-2-4-dione. The main reaction to occur is the precession of ethiofencarb to its sulfide.
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At least the Actinobacillus pleuropneumoniae N-glycosyltransferase can also hydrolyze sugar-nucleotides in the absence of a substrate, a pattern frequently observed in glycosyltransferases, and some N-glycosyltransferases can attach additional hexoses on oxygen atoms of the protein-linked hexose. N-glycosylation by Actinobacillus pleuropneumoniae HMW1C does not require metals, consistent with observations made on other GT41 family glycosyltransferases and a distinction from oligosaccharyltransferases.
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Tumebacillus lipolyticus is a species of Gram positive, aerobic, bacterium. The cells are rod-shaped, non-motile, and form spores. It was first isolated from surface water of Godavari River in Kapileswarapuram, India. The species was first described in 2015, and the name is derived from Greek lipos (fat) and lytikos (able to loosen, able to dissolve), referring to the species ability to hydrolyze lipids.
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Encyclopedia of Earth. eds. Sidney Draggan and C.J.Cleveland, National Council for Science and the Environment, Washington DC The genus is named after Theodor Escherich, the discoverer of Escherichia coli. Escherichia are facultative aerobes, with both aerobic and anaerobic growth, and an optimum temperature of 37 °C. Escherichia are usually motile by flagella, produce gas from fermentable carbohydrates, and do not decarboxylate lysine or hydrolyze arginine .
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Given that snake venom contains many biologically active ingredients, some may be useful to treat disease. For instance, phospholipases type A2 (PLA2s) from the Tunisian vipers Cerastes cerastes and Macrovipera lebetina have been found to have antitumor activity. Anticancer activity has been also reported for other compounds in snake venom. PLA2s hydrolyze phospholipids, thus could act on bacterial cell surfaces, providing novel antimicrobial (antibiotic) activities.
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Elastases form a subfamily of serine proteases that hydrolyze many proteins in addition to elastin. Humans have six elastase genes which encode the structurally similar proteins elastase 1, 2, 2A, 2B, 3A, and 3B. Like most of the human elastases, elastase 2B is secreted from the pancreas as a zymogen. In other species, elastase 2B has been shown to preferentially cleave proteins after leucine, methionine, and phenylalanine residues.
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Bacterial species that had the ability to degrade organophosphate pesticides have been isolated from soil samples from different parts of the world. The first bacterial strain identified to be able to hydrolyze organophosphates was Flavobacterium sp. ATCC 27551, found by Sethunathan and Yoshida in 1973 from a soil sample originally from the Philippines. Since then, other species were found to also have organophosphate-degrading enzymes similar to that found in Flavobacterium.
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Nuclear export first begins with the binding of Ran-GTP (a G-protein) to exportin. This causes a shape change in exportin, increasing its affinity for the export cargo. Once the cargo is bound, the Ran-exportin-cargo complex moves out of the nucleus through the nuclear pore. GTPase activating proteins (GAPs) then hydrolyze the Ran-GTP to Ran-GDP, and this causes a shape change and subsequent exportin release.
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Later, a second plant was opened in Louisiana. However, both plants were closed after World War I due to economic reasons. The first attempt at commercializing a process for ethanol from wood was done in Germany in 1898. It involved the use of dilute acid to hydrolyze the cellulose to glucose, and was able to produce 7.6 liters of ethanol per 100 kg of wood waste ( per ton).
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Insulin-like growth factors can activate mTORC1 through the receptor tyrosine kinase (RTK)-Akt/PKB signaling pathway. Ultimately, Akt phosphorylates TSC2 on serine residue 939, serine residue 981, and threonine residue 1462. These phosphorylated sites will recruit the cytosolic anchoring protein 14-3-3 to TSC2, disrupting the TSC1/TSC2 dimer. When TSC2 is not associated with TSC1, TSC2 loses its GAP activity and can no longer hydrolyze Rheb-GTP.
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Organophosphates like TEPP and sarin inhibit cholinesterases, enzymes that hydrolyze the neurotransmitter acetylcholine. The active centre of cholinesterases feature two important sites, namely the anionic site and the esteratic site. After the binding of acetylcholine to the anionic site of the cholinesterase, the acetyl group of acetylcholine can bind to the esteratic site. Important amino acid residues in the esteratic site are a glutamate, a histidine, and a serine.
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The human genome contains at least 21 genes involved in determining the intracellular levels of cAMP and cGMP by the expression of phosphodiesterase proteins or PDE's. These PDE's are grouped into at least 11 functional subfamilies, named PDE1-PDE11. PDEs are enzymes that hydrolyze cyclic adenosine 3,5-monophosphate (cAMP) and cyclic guanosine 3,5-monophospahate (cGMP), which are intracellular second messengers, into AMP and GMP. These second messengers control many physiological processes.
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Elastases form a subfamily of serine proteases that hydrolyze many proteins in addition to elastin. Humans have six elastase genes which encode the structurally similar proteins elastase 1, 2, 2A, 2B, 3A, and 3B. Like most of the human elastases, elastase 2A is secreted from the pancreas as a zymogen. In other species, elastase 2A has been shown to preferentially cleave proteins after leucine, methionine, and phenylalanine residues.
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The bacterium Pseudomonas diminuta will hydrolyze this compound but not its stereoisomer trans-2,3-Butylene carbonate, yielding cis-2,3-butanediol. This has been proposed as an efficient route to produce the latter from a racemic mixture of 2,3-butylene carbonates. Kazutsugu Matsumoto, Youichi Sato, Megumi Shimojo and Minoru Hatanaka (2000), Highly enantioselective preparation of C2-symmetrical diols: microbial hydrolysis of cyclic carbonates. Tetrahedron: Asymmetry, volume 11, issue 9, pages 1965-1973.
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It is also involved in silver recovery and peptide synthesis. One strain of R. oryzae was found to secrete alkaline serine protease which shows high pH stability within 3 to 6 and poor thermos- stability. Lipase that is extracted from R. oryzae have been consumed as digestive aids without adverse reactions. Lipases hydrolyze fats and oils with subsequent release of free fatty acids such as diacylglycerols, monoacylglycerols and glycerol.
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RuvA has a domain with acidic amino acid residues that interfere with the base pairs in the centre of the junction. This forces the base pairs apart so that they can re-anneal with base pairs on the homologous strands. In order for migration to occur, RuvA must be associated with RuvB and ATP. RuvB has the ability to hydrolyze ATP, driving the movement of the branch point.
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Phytic acid has six phosphate groups that may be released by phytases at different rates and in different order. Phytases hydrolyze phosphates from phytic acid in a stepwise manner, yielding products that again become substrates for further hydrolysis. Most phytases are able to cleave five of the six phosphate groups from phytic acid. Phytases have been grouped based on the first phosphate position of phytic acid that is hydrolyzed.
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There has been great potential shown in the use of endoglycosidase enzymes undergoing mutagenesis. This new mutated enzyme when exposed to the proper compounds will undergo oligosaccharide synthesis and will not hydrolyze the newly formed polymer chains. This is an extremely useful tool, as oligosaccharides have a great potential for use as therapeutics. For example, globo H hexasaccharide will indicate cancer related malignant cell transformation in the breast, prostate and ovaries.
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GTP hydrolysis activity of RHEB is intrinsically slow and the GTP-bound form is more common, thus RHEB is more likely active than not active within the cell. Its activity is strongly regulated within the cell by tumor-suppressant proteins that form the TSC complex. Specifically, the TSC2 subunit, tuberin of the complex interacts with and inhibits RHEB to regulate the protein. Tuberin stimulates RHEB to hydrolyze GTP, thus inactivating it.
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Cronobacter is a genus of Gram-negative, facultatively anaerobic, oxidase- negative, catalase-positive, rod-shaped bacteria of the family Enterobacteriaceae. They are generally motile, reduce nitrate, use citrate, hydrolyze esculin and arginine, and are positive for L-ornithine decarboxylation. Acid is produced from D-glucose, D-sucrose, D-raffinose, D-melibiose, D-cellobiose, D-mannitol, D-mannose, L-rhamnose, L-arabinose, D-trehalose, galacturonate and D-maltose. Cronobacter spp.
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They reason that when lignin is melted in the presence of water, because of its hydrophobic nature it will form micro- droplets that solidify at lower temperatures. The conditions used in the pretreatment also hydrolyze hemicellulose. Therefore, the creation of these lignin micro-droplets and the hydrolysis of hemicellulose neutralize the two components protecting cellulose. This method keeps feedstock in its native fibrous state, while enhancing the efficiency of enzymatic hydrolysis.
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Familial hypertriglyceridemia is considered to be inherited in an autosomal dominant manner. However, it is important to recognize that most cases have a polygenic inheritance distancing themselves from traditional Mendelian inheritance patterns. One of the most common mutations implicated in the development of familial hypertriglyceridemia is a heterozygous inactivating mutation of the LPL gene. Inactivation of this gene leads to an individual’s inability to hydrolyze the triglycerides within the VLDL core.
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BPPs could be used in aquatic animal feed because many of these animals like fishes and shrimps have a neutral or alkaline gastrointestinal tract. BPPs are also phytate specific unlike HAPs, which hydrolyze also other phosphate containing molecules like ADP, GTP and NADH. However, BPPs are catalytically more than 2–60 times slower than current the HAPs. HAPs have a specific catalytic activity of 100–3000 U mg−1.
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Alpha-amylase 1 is an enzyme that in humans is encoded by the AMY1A gene. This gene is found in many organisms. Amylases are secreted proteins that hydrolyze 1,4-alpha-glucoside bonds in oligosaccharides and polysaccharides, and thus catalyze the first step in digestion of dietary starch and glycogen. The human genome has a cluster of several amylase genes that are expressed at high levels in either salivary gland or pancreas.
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Comparison of three-electron bond to the conventional covalent bond The two resonance structures Chlorine dioxide is a neutral chlorine compound. It is very different from elemental chlorine, both in its chemical structure and in its behavior. One of the most important qualities of chlorine dioxide is its high water solubility, especially in cold water. Chlorine dioxide does not hydrolyze when it enters water; it remains a dissolved gas in solution.
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ParM is a prokaryotic actin homologue which provides the force to drive copies of the R1 plasmid to opposite ends of rod shaped bacteria before cytokinesis. ParM is a monomer that is encoded in the DNA of the R1 plasmid and manufactured by the host cell's ribosomes. In the cytoplasm it spontaneously polymerizes forming short strands that either bind to ParR or hydrolyze. ParR stabilizes ParM and prevents it from hydrolyzing.
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Nitrogen monofluoride is a metastable species that has been observed in laser studies. It is isoelectronic with O2 and, unusually, like BF, has a higher bond order than single-bonded fluorine. see-saw shape is predicted by VSEPR theory. The chalcogens (oxygen's periodic table column) are somewhat similar: The tetrafluorides are thermally unstable and hydrolyze, and are also ready to use their lone pair to form adducts to other (acidic) fluorides.
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Carnosinase in humans has two forms: 1\. Cellular, or tissue carnosinase: This form of the enzyme is found in every bodily tissue. It is a dimer, and hydrolyzes both carnosine and anserine, preferring dipeptides that have a histidine monomer in the C-terminus position. Tissue carnosinase is often considered a "nonspecific dipeptidase", based in part on its ability to hydrolyze a range of dipeptide substrates, including those belonging to prolinase. 2\.
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Monoamine oxidase (MAO) is an extensively studied flavoenzyme due to its biological importance with the catabolism of norepinephrine, serotonin and dopamine. MAO oxidizes primary, secondary and tertiary amines, which nonenzymatically hydrolyze from the imine to aldehyde or ketone. Even though this class of enzyme has been extensively studied, its mechanism of action is still being debated. Two mechanisms have been proposed: a radical mechanism and a nucleophilic mechanism.
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During inhibition, each acts as a ligand to an oxygen in 2-PMPA or phosphate. There is also one calcium ion coordinated in GCPII, far from the active site. It has been proposed that calcium holds together the protease and apical domains. In addition, human GCPII has ten sites of potential glycosylation, and many of these sites (including some far from the catalytic domain) affect the ability of GCPII to hydrolyze NAAG.
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HIV-1 PR serves a dual purpose. Precursor HIV-1 PR is responsible for catalyzing its own production into mature PR enzymes via PR auto-processing. Mature protease is able to hydrolyze peptide bonds on the Gag-Pol polyproteins at nine specific sites, processing the resulting subunits into mature, fully functional proteins. These cleaved proteins, including reverse transcriptase, integrase, and RNaseH, are encoded by the coding region components necessary for viral replication.
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The human AMY1C gene encodes the protein Amylase, alpha 1C (salivary). Amylases are secreted proteins that hydrolyze 1,4-alpha-glucoside bonds in oligosaccharides and polysaccharides, and thus catalyze the first step in digestion of dietary starch and glycogen. The human genome has a cluster of several amylase genes that are expressed at high levels in either the salivary gland or pancreas. This gene encodes an amylase isoenzyme produced by the salivary gland.
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Carboxylesterase 3 is a member of a large multigene family. The enzymes encoded by these genes are responsible for the hydrolysis of ester- and amide-bond-containing drugs such as cocaine and heroin. They also hydrolyze long-chain fatty acid esters and thioesters. The specific function of this enzyme has not yet been determined; however, it is speculated that carboxylesterases may play a role in lipid metabolism and/or the blood–brain barrier system.
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Gamma-glutamyltransferase 5 is an enzyme that in humans is encoded by the GGT5 gene. Gamma-glutamyltransferase-like activity 1 (GGTLA1) is a member of a gene family with at least 4 members (GGTLA1, GGTLA2, GGTLA3 and GGTLA4). The enzyme encoded by GGTLA1 is related to, but distinct from, gamma-glutamyl transpeptidase (GGT). The GGTLA1 enzyme consists of a heavy and a light chain and is able to hydrolyze the gamma-glutamyl moiety of glutathione.
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This gene encodes a member of family 1 glycosidases. Glycosidases are enzymes that hydrolyze glycosidic bonds and are classified into families based on primary amino acid sequence. Most members of family 1 have two conserved glutamic acid residues, which are required for enzymatic activity. The mouse ortholog of this protein has been characterized and has a domain structure of an N-terminal signal peptide, glycosidase domain, transmembrane domain, and a short cytoplasmic tail.
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Most mammals have limited ability to digest dietary fiber such as cellulose. Some ruminants like cows and sheep contain certain symbiotic anaerobic bacteria (such as Cellulomonas and Ruminococcus spp.) in the flora of the rumen, and these bacteria produce enzymes called cellulases that hydrolyze cellulose. The breakdown products are then used by the bacteria for proliferation. The bacterial mass is later digested by the ruminant in its digestive system (stomach and small intestine).
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Strain halo-2T does not contain the catalase, oxidase, urease, or nitrate reductase enzymes, but does contain enzymes to hydrolyze starch. It's cell wall peptidoglycan contains meso-diaminopimelic acid and MK-7, the predominant menaquinone. The polar lipid profile of strain halo-2T consists of diphosphatidylglycerol, phosphatidylethanolamine and phosphatidylglycerol. The strain produces a water-insoluble orange pigment, with a major peak at 459 nm, and has a genomic DNA G+C content of 48.2 mol%.
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The French chemist, Henri Braconnot, was the first to discover that cellulose could be hydrolyzed into sugars by treatment with sulfuric acid in 1819. The hydrolyzed sugar could then be processed to form ethanol through fermentation. The first commercialized ethanol production began in Germany in 1898, where acid was used to hydrolyze cellulose. In the United States, the Standard Alcohol Company opened the first cellulosic ethanol production plant in South Carolina in 1910.
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In order to have these types of qualities, positive resist utilize polymers with labile linkers in their back bone that can be cleaved upon irradiation or using a photo- generated acid to hydrolyze bonds in the polymer. A polymer that decomposes upon irradiation to a liquid, or more soluble product is referred to as a positive tone resist. Common functional groups that can be hydrolyzed by photo-generated acid catalyst include polycarbonates and polyesters.
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The hexavalent phytate anion. Phosphorus and inositol in phytate form are not, in general, bioavailable to non-ruminant animals because these animals lack the digestive enzyme phytase required to hydrolyze the inositol-phosphate linkages. Ruminants are readily able to digest phytate because of the phytase produced by rumen microorganisms. In most commercial agriculture, non-ruminant livestock, such as swine, fowl, and fish, are fed mainly grains, such as maize, legumes, and soybeans.
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Phospholipase A1 encoded by the PLA1A gene is a phospholipase enzyme which removes the 1-acyl. Phospholipase A1 is an enzyme that resides in a class of enzymes called phospholipase that hydrolyze phospholipids into fatty acids. There are 4 classes, which are separated by the type of reaction they catalyze. In particular, phospholipase A1 (PLA1) specifically catalyzes the cleavage at the SN-1 position of phospholipids, forming a fatty acid and a lysophospholipid.
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GTPase-activator protein for Ras-like GTPase is a family of evolutionarily related proteins. Ras proteins are membrane-associated molecular switches that bind GTP and GDP and slowly hydrolyze GTP to GDP. This intrinsic GTPase activity of ras is stimulated by a family of proteins collectively known as 'GAP' or GTPase-activating proteins. As it is the GTP bound form of ras which is active, these proteins are said to be down-regulators of ras.
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It was heavily stressed by Criegee that the reaction must be run in anhydrous solvents, as any water present would hydrolyze the lead tetraacetate; however, subsequent publications have reported that if the rate of oxidation is faster than the rate of hydrolysis, the cleavage can be run in wet solvents or even aqueous solutions. For example, glucose, glycerol, mannitol, and xylose can all undergo a Criegee oxidation in aqueous solutions, but sucrose cannot.
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ZrCl4 is an intermediate in the conversion of zirconium minerals to metallic zirconium by the Kroll process. In nature, zirconium minerals invariably exist as oxides (reflected also by the tendency of all zirconium chlorides to hydrolyze). For their conversion to bulk metal, these refractory oxides are first converted to the tetrachloride, which can be distilled at high temperatures. The purified ZrCl4 can be reduced with Zr metal to produce zirconium(III) chloride.
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This unique formation of cyclic and acyclic acetals leads to varying degradation time because the two acetal groups hydrolyze at different rates. Acetalated dextran's degradation time can vary from hours to a month or more at pH 7.2. Also, acetalated dextran is unique because it is acid sensitive. Therefore, at lower pH acetalated dextran degrades more rapidly, which results in a polymer that degrades approximately two logs faster at pH 5 compared to pH 7.
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GTPases are enzymes that bind to a molecule called guanosine triphosphate (GTP) which they then hydrolyze to create guanosine diphosphate (GDP) and release energy. Ran is in a different conformation depending on whether it is bound to GTP or GDP. In its GTP bound state, Ran is capable of binding karyopherins (importins and exportins). Importins release cargo upon binding to RanGTP, while exportins must bind RanGTP to form a ternary complex with their export cargo.
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The NFPA rating is NFPA 704. Ethylene oxide in presence of water can hydrolyze to ethylene glycol and form poly ethylene oxide which then eventually gets oxidized by air and leads to hotspots that can trigger explosive decomposition. Fires caused by ethylene oxide are extinguished by traditional media, including foam, carbon dioxide or water. Suppression of this activity can be done by blanketing with an inert gas until total pressure reaches non explosive range.
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Penicillinase-mediated resistance in N. gonorrhoeae is mediated by the plasmid borne TEM-1 type beta-lactamase which falls under the third general mechanism for beta-lactam resistance. There have been over 200 beta-lactamases described and some of them are antibiotic specific. TEM-1 is a penicillinase specific for penicillins. This enzyme will bind to the beta-lactam ring which is a structural characteristic for beta- lactams and hydrolyze the ring.
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Biodegradation is generally recognized as biggest contributor to degradation. Whereas plants, animals and fungi (Eukaryota) typically transform pesticides for detoxification through metabolism by broad- spectrum enzymes, bacteria (Prokaryota) more commonly metabolize them. This dichotomy is likely due to a wider range of sensitive targets in Eukaryota. For example, organophosphate esters that interfere with nerve signal transmission in insects do not affect microbial processes and offering nourishment for microorganisms whose enzymes can hydrolyze phosphotriesters.
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Amygdalin is a cyanogenic glycoside derived from the aromatic amino acid phenylalanine. Amygdalin and prunasin are common among plants of the family Rosaceae, particularly the genus Prunus, Poaceae (grasses), Fabaceae (legumes), and in other food plants, including flaxseed and manioc. Within these plants, amygdalin and the enzymes necessary to hydrolyze it are stored in separate locations so that they will mix in response to tissue damage. This provides a natural defense system.
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Dew retting of flax Bacteria such as Clostridium butyricum are used to separate fibres of jute, hemp and flax in the process of retting. The plants are immersed in water and when they swell, inoculated with bacteria which hydrolyze pectic substances of the cell walls and separate the fibres. Alternatively, the plants are spread out on the ground and ret naturally because dew provides moisture. These separated fibres are used to make ropes, sacks etc.
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Pancreatic alpha-amylase is an enzyme that in humans is encoded by the AMY2A gene. Amylases are secreted proteins that hydrolyze 1,4-alpha-glucoside bonds in oligosaccharides and polysaccharides, and thus catalyze the first step in digestion of dietary starch and glycogen. The human genome has a cluster of several amylase genes that are expressed at high levels in either salivary gland or pancreas. This gene encodes an amylase isoenzyme produced by the pancreas.
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Lysosomal acid phosphatase is an enzyme that in humans is encoded by the ACP2 gene. Lysosomal acid phosphatase is composed of two subunits, alpha and beta, and is chemically and genetically distinct from red cell acid phosphatase. Lysosomal acid phosphatase 2 is a member of a family of distinct isoenzymes which hydrolyze orthophosphoric monoesters to alcohol and phosphate. Acid phosphatase deficiency is caused by mutations in the ACP2 (beta subunit) and ACP3 (alpha subunit) genes.
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ESBLs are beta-lactamases that hydrolyze extended-spectrum cephalosporins with an oxyimino side chain. These cephalosporins include cefotaxime, ceftriaxone, and ceftazidime, as well as the oxyimino-monobactam aztreonam. Thus ESBLs confer multi-resistance to these antibiotics and related oxyimino-beta lactams. In typical circumstances, they derive from genes for TEM-1, TEM-2, or SHV-1 by mutations that alter the amino acid configuration around the active site of these β-lactamases.
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The chloride from the hydrochloric acid in sodium chloride does not hydrolyze, though, so sodium chloride is not basic. The difference between a basic salt and an alkali is that an alkali is the soluble hydroxide compound of an alkali metal or an alkaline earth metal. A basic salt is any salt that hydrolyzes to form a basic solution. Another definition of a basic salt would be a salt that contains amounts of both hydroxide and other anions.
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Sucrose intolerance (also known as congenital sucrase-isomaltase deficiency (CSID), genetic sucrase-isomaltase deficiency (GSID), or sucrase-isomaltase deficiency) occurs when sucrase is not being secreted in the small intestine. With sucrose intolerance, the result of consuming sucrose is excess gas production and often diarrhea and malabsorption. Lactose intolerance is a related disorder that reflects an individual's inability to hydrolyze the disaccharide lactose. Sucrase is secreted by the tips of the villi of the epithelium in the small intestine.
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Cathepsin zymography is a technique for quantifying enzymatic activity of the cathepsin family of cysteine proteases. It is based on SDS-PAGE whereby samples tested for cathepsin activity are loaded into a polyacrylamide gel and then separated by molecular weight. Gelatin is embedded in the gel itself, providing a substrate for the enzymes to hydrolyze. While the proform of cathepsins are generally stable, once activated, proteases such as cathepsin K are vulnerable to inactivation in neutral pH environments.
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Elastases form a subfamily of serine proteases that hydrolyze many proteins in addition to elastin. Humans have six elastase genes which encode the structurally similar proteins elastase 1, 2, 2A, 2B, 3A, and 3B. Unlike other elastases, elastase 3A has little elastolytic activity. Like most of the human elastases, elastase 3A is secreted from the pancreas as a zymogen and, like other serine proteases such as trypsin, chymotrypsin and kallikrein, it has a digestive function in the intestine.
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Elastases form a subfamily of serine proteases that hydrolyze many proteins in addition to elastin. Humans have six elastase genes which encode the structurally similar proteins elastase 1, 2, 2A, 2B, 3A, and 3B. Unlike other elastases, elastase 3B has little elastolytic activity. Like most of the human elastases, elastase 3B is secreted from the pancreas as a zymogen and, like other serine proteases such as trypsin, chymotrypsin and kallikrein, it has a digestive function in the intestine.
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With no GAPs to curb the G protein's activity, this results in constitutively active G proteins, unregulated cell growth, and the cancerous state. In the case of the latter, a loss of the G protein's ability to respond to GAP, the G proteins have lost their ability to hydrolyze GTP. With a nonfunctional G protein enzyme, GAPs cannot activate the GTPase activity, and the G protein is constitutively on. This also results in unregulated cell growth and cancer.
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To revert TNP-ATP back to its constituent parts, or in other words to hydrolyze TNP-ATP to give equilmolar amounts of picric acid (TNP) and ATP, TNP-ATP should be treated with 1 M HCl at 100 degrees Celsius for 1.5 hours. This is because if TNP-ATP is acidified under mild conditions, it results in the opening of the dioxolane ring attached to the 2’-oxygen, leaving a 3’O-TNP derivative as the only product.
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Dark fermentation is the fermentative conversion of organic substrate to biohydrogen. It is a complex process manifested by diverse groups of bacteria, involving a series of biochemical reactions using three steps similar to anaerobic conversion. Dark fermentation differs from photofermentation in that it proceeds without the presence of light. Fermentative/hydrolytic microorganisms hydrolyze complex organic polymers to monomers which are further converted to a mixture of lower-molecular-weight organic acids and alcohols by obligatory producing acidogenic bacteria.
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A novel feature of this compound is its unreactivity towards water and the fact that it reacts with mineral acids at a significant rate only at elevated temperatures, whereas the corresponding organocadmium and organozinc compounds hydrolyze rapidly. The difference reflects the low affinity of Hg(II) for oxygen ligands. The compound reacts with mercuric chloride to give the mixed chloro-methyl compound: : (CH3)2Hg + HgCl2 → 2 CH3HgCl Whereas dimethylmercury is a volatile liquid, methylmercury chloride is a crystalline solid.
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Alpha- glucosidase inhibitors are saccharides that act as competitive inhibitors of enzymes needed to digest carbohydrates: specifically alpha-glucosidase enzymes in the brush border of the small intestines. The membrane-bound intestinal alpha-glucosidases hydrolyze oligosaccharides, trisaccharides, and disaccharides to glucose and other monosaccharides in the small intestine. Acarbose also blocks pancreatic alpha-amylase in addition to inhibiting membrane-bound alpha-glucosidases. Pancreatic alpha-amylase hydrolyzes complex starches to oligosaccharides in the lumen of the small intestine.
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Lysozyme exhibits two conformations: an open active state and a closed inactive state. The catalytic relevance was examined with single walled carbon nanotubes (SWCN) field effect transistors (FETs), where a singular lysozyme was bound to the SWCN FET. Electronically monitoring the lysozyme showed two conformations, an open active site and a closed inactive site. In its active state lysozyme is able to processively hydrolyze its substrate, breaking on average 100 bonds at a rate of 15 per second.
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Here, arylsulfatase A hydrolyzes the sulfate group. However, in order for this reaction to be carried out, a sphingolipid activator protein such as saposin B must be present. Saposin B extracts sulfatide from the membrane, which makes it accessible to arylsulfatase A. Arylsulfatase A can then hydrolyze the sulfate group. Accumulation of sulfatide can cause metachromatic leukodystrophy, a lysosomal storage disease and may be caused because of a defect in arylsulfatase A, leading to an inability to degrade sulfatide.
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Pancreatin contains the pancreatic enzymes trypsin, amylase and lipase. A similar mixture of enzymes is sold as pancrelipase, which contains more active lipase enzyme than does pancreatin. The trypsin found in pancreatin works to hydrolyze proteins into oligopeptides; amylase hydrolyzes starches into oligosaccharides and the disaccharide maltose; and lipase hydrolyzes triglycerides into fatty acids and glycerols. Pancreatin is an effective enzyme supplement for replacing missing pancreatic enzymes, and aids in the digestion of foods in cases of pancreatic insufficiency.
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In vitro exposure of tomatine to 1 M HCl for 3 hours at did not hydrolyze tomatine, so probably the tomatine is also not hydrolyzed by acid in the digestive tract of humans. The hydroxylation of tomatine likely leads to the formation of tomatidine, which is the aglycon of tomatine. Tomatidine is a metabolite which may not be completely nontoxic; it could have effects on the human body. Fungal tomatinase enzymes can transform tomatine to deactivate it.
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Hepatic lipase falls under a class of enzymes known as hydrolases. Its function is to hydrolyze triacylglycerol to diacylglycerol and carboxylate (free fatty acids) with the addition of water. The substrate, triacylglycerol, comes from IDL (Intermediate-density lipoprotein) and the release of free fatty acids converts IDL into LDL (Low-density lipoprotein). These remaining remnants of LDL can be sent back to the liver, where it can be stored for later use or broken down to harness its energy.
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Outside of the stomach, gastric lipase can hydrolyze triacylglycerol in the duodenum with the help of other lipases and bile secretion. It is an essential enzyme for hydrolyzing milk fat globule membranes. For a newborn with an underdeveloped pancreas, LIPF plays a more important role in lipid digestion compared to an adult with a fully functioning pancreas. There is typically an increase in production of LIPF when the pancreas is unable to operate at its optimal potential.
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Like many other peptides, aspartame may hydrolyze (break down) into its constituent amino acids under conditions of elevated temperature or high pH. This makes aspartame undesirable as a baking sweetener, and prone to degradation in products hosting a high pH, as required for a long shelf life. The stability of aspartame under heating can be improved to some extent by encasing it in fats or in maltodextrin. The stability when dissolved in water depends markedly on pH.
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MenH (SHCHC synthase) was previously thought to be a thioesterase involved in hydrolyzing DHNA-CoA in a later step of menaquinone synthesis. In 2008, it was determined that MenH has poor catalytic activity toward palmitoyl-CoA, casting doubt on its role as a thioesterase. Direct analysis confirmed that MenH is unable to hydrolyze DHNA-CoA. In 2009, it was proposed that a dedicated hotdog fold thioesterase would be needed to catalyze the hydrolysis of DHNA-CoA.
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Dr. Joseph Cecil Patrick (August 28, 1892 – April 12, 1965) invented Thiokol, America's first synthetic rubber in the early 1920s. While seeking a formulation for automotive antifreeze, he attempted to hydrolyze ethylene dichloride with sodium polysulfide. In doing so, he produced a brown, insoluble gum that later became known as Thiokol. He solved commercial production problems by inventing the suspension polymerization process, and solved compounding problems by degrading high molecular weight polymer to a low molecular weight liquid polymer.
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Curcumin Demethoxycurcumin Bisdemethoxycurcumin A curcuminoid is a linear diarylheptanoid, with molecules such as curcumin or derivatives of curcumin with different chemical groups that have been formed to increase solubility of curcumins and make them suitable for drug formulation. These compounds are natural phenols and produce a pronounced yellow color. Many curcumin characters are unsuitable for use as drugs by themselves. They have poor solubility in water at acidic and physiological pH, and also hydrolyze rapidly in alkaline solutions.
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As ureases they hydrolyze urea to produce ammonia and carbonic acid. As the bacteria are localized to the stomach ammonia produced is readily taken up by the circulatory system from the gastric lumen. This results in elevated ammonia levels in the blood and is coined as hyperammonemia, eradication of Heliobacter pylori show marked decreases in ammonia levels. Urease in peptic ulcers Helicobacter pylori is also the cause of peptic ulcers with its manifestation in 55–68% reported cases.
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The actual substrate of BPPs is calcium phytate and in order to hydrolyze it, BPPs must have Ca2+ ions bound to themselves. BPPs are the most widely found phytase superfamily in the environment and they are thought to have a major role in phytate-phosphorus cycling in soil and water. As their alternative name alkaline phytase suggests, BPPs work best in basic (or neutral) environment. Their pH optima is 6–9, which is unique among the phytases.
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Due to proline’s cyclic structure, only few peptidases could cleave the bond between proline and other amino acids. Along with prolinase, prolidase are the only known enzymes that can break down dipeptides to yield free proline. Prolidase serve to hydrolyze both dietary and endogenous Xaa-Pro dipeptides. More specifically, it is essential in catalyzing the last step of the degradation of procollagen, collagen, and other proline-containing peptides into free amino acids to be used for cellular growth.
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Glucosylceramides (GluCer) are the most widely distributed glycosphingolipids in cells serving as precursors for the formation of over 200 known glycosphingolipids. GluCer is formed by the glycosylation of ceramide in an organelle called Golgi via enzymes called glucosylceramide synthase (GCS) or by the breakdown of complex glycosphingolipids (GSLs) through the action of specific hydrolase enzymes. In turn, certain β-glucosidases hydrolyze these lipids to regenerate ceramide. GluCer appears to be synthesized in the inner leaflet of the Golgi.
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CYTH-like superfamily enzymes, which include polyphosphate polymerases, hydrolyze triphosphate-containing substrates and require metal cations as cofactors. They have a unique active site located at the center of an eight-stranded antiparallel beta barrel tunnel (the triphosphate tunnel). The name CYTH originated from the gene designation for bacterial class IV adenylyl cyclases (CyaB), and from thiamine triphosphatase (THTPA). Class IV adenylate cyclases catalyze the conversion of ATP to 3',5'-cyclic AMP (cAMP) and PPi.
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This toxin activates Rho GTPases, which bind and hydrolyze GTP, and are important in actin stress fiber formation. Formation of stress fibers may aid in the endocytosis of P. multocida. The host cell cycle is also modulated by the toxin, which can act as an intracellular mitogen.Lacerda HM, Lax AJ, Rozenqurt E. Pasteurella multocida toxin, a potent intracellularly acting mitogen, induces p125FAK and paxillin tyrosine phosphorylation, actin stress fiber formation, and focal contact assembly in Swiss 3T3 cells.
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The inhibitor protein (IP) is situated in the mitochondrial matrix and protects the cell against rapid ATP hydrolysis during momentary ischaemia. In oxygen absence, the pH of the matrix drops. This causes IP to become protonated and change its conformation to one that can bind to the F1Fo synthetase and stops it thereby preventing it from moving in a backwards direction and hydrolyze ATP instead of make it. When oxygen is finally incorporated into the system, the pH rises and IP is deprotonated.
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The aspartic acid side chain has a pKa of approximately 4. In an acidic environment, this residue will readily give up its proton, but will also take a proton away from water if the side chain is deprotonized, thus catalyzing the hydroxyl attack on the phosphate group. Soon after the deprotonation of the histidine residue and the protonation of the aspartic acid residue, the histidine residue will deprotonate the aspartic acid residue, preparing the enzyme to hydrolyze an LPA again.
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PgpB is competitively inhibited by phosphatidylethanolamine (PE), a phospholipid formed from DAG. This is therefore an example of negative feedback regulation. The enzyme active site contains a catalytic triad Asp-211, His-207, and His-163 that establishes a charge relay system. However, this catalytic triad is essential for the dephosphorylation of lysophosphatidic acid, phosphatidic acid, and sphingosine-1-phosphate, but is not essential in its entirety for the enzyme's native substrate, phosphatidylglycerol phosphate; His-207 alone is sufficient to hydrolyze PGP.
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Phosducin- transducin beta-gamma complex. Beta and gamma subunits of G-protein are shown by blue and red, respectively. Guanosine diphosphate Guanosine triphosphate G proteins, also known as guanine nucleotide-binding proteins, are a family of proteins that act as molecular switches inside cells, and are involved in transmitting signals from a variety of stimuli outside a cell to its interior. Their activity is regulated by factors that control their ability to bind to and hydrolyze guanosine triphosphate (GTP) to guanosine diphosphate (GDP).
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The Gα subunit will eventually hydrolyze the attached GTP to GDP by its inherent enzymatic activity, allowing it to re-associate with Gβγ and starting a new cycle. A group of proteins called Regulator of G protein signalling (RGSs), act as GTPase-activating proteins (GAPs), are specific for Gα subunits. These proteins accelerate the hydrolysis of GTP to GDP, thus terminating the transduced signal. In some cases, the effector itself may possess intrinsic GAP activity, which then can help deactivate the pathway.
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Mammalian milk all contain oligosaccharides showing natural selection . Human milk oligosaccharides are not digested by enzymes and remain whole through the digestive tract before being broken down in the colon by microbiota. Bifidobacterium species genomes of B. longum, B. bifidum, B. breve contain genes that can hydrolyze some of the human milk oligosaccharides and these are found in higher numbers in infants that are breast-fed. Glycans that are produced by the humans are converted into food and energy for the B. bifidum.
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This protein is a membrane glycoprotein localized at the cell plasma membrane. It has been shown to actively hydrolyze extracellular lysophosphatidic acid (LPA) and short-chain phosphatidic acid. [5] As an LPA inhibitor, PPAP2B is known to suppress LPA receptor mediated cellular signaling, which is associated with activation of vascular and blood cells and epithelial cell migration and proliferation. In response to dynamic atherorelevant-flows, PPAP2B can promote anti-inflammatory phenotype via inhibition of LPA signaling and maintain vascular integrity of endothelial monolayer.
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Bisoxazolidines are chemical compounds that contain two oxazolidine rings, they are used as performance modifiers in polyurethane coatings and paints. The rings hydrolyze in the presence of moisture to give amine and hydroxyl groups, these can then react with diisocyanates, polyisocyanates and polyurethane prepolymers to form a coating.Emission control chembytes e-zine 2001. The use of a bisoxazolidine in a polyurethane systems can prevent the unwanted reaction between isocyanate and moisture resulting in coating defects, as a result of carbon dioxide release.
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In eukaryotes, post-translational translocation depends on BiP and other complexes, including the SEC62/SEC63 integral membrane protein complex. In this mode of translocation, Sec63 helps BiP hydrolyze ATP, which then binds to the peptide and "pulls" it out. This process is repeated for other BiP molecules until the entire peptide has been pulled through. In bacteria, the same process is done by a "pushing" ATPase known as SecA, sometimes assisted by the SecDF complex on the other side responsible for pulling.
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Clostridium indolis is a Gram-positive, motile, anaerobic, rod-shaped bacteria that produces terminal spores. Clostridium indolis was originally named for its ability to hydrolyze tryptophan to indole, pyruvate, and ammonia in the classic indole test which is used to distinguish bacterial species. It is commonly found in soil and can be found in human and bird feces. Colonies of Clostridium indolis are found to be non-hemolytic and have an optimal growth temperature of 37 °C, classifying them as mesophiles.
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Ester linkages arise between oxidized sugars, the uronic acids, and the phenols and phenylpropanols functionalities of the lignin. To extract the fermentable sugars, one must first disconnect the celluloses from the lignin, and then use acid or enzymatic methods to hydrolyze the newly freed celluloses to break them down into simple monosaccharides. Another challenge to biomass fermentation is the high percentage of pentoses in the hemicellulose, such as xylose, or wood sugar. Unlike hexoses such as glucose, pentoses are difficult to ferment.
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In contrast to calcein-AM, calcein has low permeability and therefore gets trapped in the cell and accumulates. As calcein-AM is an excellent substrate of the MDR1 and MRP1 efflux transporters, cells expressing MDR1 and/or MRP1 transporters pump the calcein-AM out of the cell before esterases can hydrolyze it. This results in a lower cellular accumulation rate of calcein. The higher the MDR activity is in the cell membrane, the less Calcein is accumulated in the cytoplasm.
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Morphine and its major metabolites, morphine-3-glucuronide and morphine-6-glucuronide, can be detected in blood, plasma, hair, and urine using an immunoassay. Chromatography can be used to test for each of these substances individually. Some testing procedures hydrolyze metabolic products into morphine before the immunoassay, which must be considered when comparing morphine levels in separately published results. Morphine can also be isolated from whole blood samples by solid phase extraction (SPE) and detected using liquid chromatography-mass spectrometry (LC-MS).
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Due to the fact that CRAT binds CoA, rather than acetyl-CoA, it appears that CRAT possesses the ability to hydrolyze acetyl-CoA, before interacting with the lone CoA fragment at the binding site. CoA is bound in a linear conformation with its pantothenic arm binding at the active site. Here, the pantothenic arm’s terminal thiol group and the ε2 nitrogen on the catalytic His343 side chain form a hydrogen bond. The 3’-phosphate on CoA forms interactions with residues Lys419 and Lys423.
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Adenosine 5′-(γ-thiotriphosphate) is an extremely common ATP analog in which one of the gamma-phosphate oxygens is replaced by a sulfur atom; this anion is hydrolyzed at a dramatically slower rate than ATP itself and functions as an inhibitor of ATP-dependent processes. In crystallographic studies, hydrolysis transition states are modeled by the bound vanadate ion. Caution is warranted in interpreting the results of experiments using ATP analogs, since some enzymes can hydrolyze them at appreciable rates at high concentration.
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RNase R, or Ribonuclease R, is a 3'-->5' exoribonuclease, which belongs to the RNase II superfamily ,a group of enzymes that hydrolyze RNA in the 3' - 5' direction. RNase R has been shown to be involved in selective mRNA degradation, particularly of non stop mRNAs in bacteria. RNase R has homologues in many other organisms. When a part of another larger protein has a domain that is very similar to RNase R, this is called an RNase R domain.
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Experiments involving the mating types suggest that the (+) mating type has higher virulence and causes more cases of infection. However, both strains demonstrate a positive result for their ability to hydrolyze the urea molecule, indicating the presence of the urease enzyme. A conducted study showed that a majority of tested isolates (>50%) of M. fulvum tested positive for urea hydrolysis within 0–7 days, and almost all isolates tested positive within 10–12 days, suggesting rapid growth of the organism.
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The degradation of proteins occurs within the cells, as the amino acids have to pass through certain membranes before being able to be used for different processes. This first step to protein catabolism is breaking the protein down into amino acids by cleaving their peptide bonds, also known as proteolysis. The peptide bonds are broken up by the proteasome, which is able to hydrolyze the peptide bonds by using ATP energy. This process is further helped by the use of enzymes called proteases.
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With time, these Arp1 filaments appeared to anneal to form longer assemblies but never attained the length of conventional actin filaments. As for conventional actin, Arp1 can bind and hydrolyze ATP, and Arp1 assembly is accompanied by nucleotide hydrolysis. It has been reported that Arp1 interacts with other dynactin components including DCTN1/p150Glued,DCTN4/p62 and Actr10/Arp11. Arp1 has been shown as the domain for dynactin binding to membrane vesicles (such as Golgi or late endosome) through its association with β-spectrin.
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ATP synthase consists of a F1 and F0 subunit. The F1 subunit contains alpha and beta subunits of its own which can assist in the formation of ATP, or hydrolyze it to serve as a proton pump. Though most catalytic actions happen on the beta subunits, the alpha subunits each contain an arginine finger. The role of the arginine finger in ATP synthase is akin to the function of the arginine finger residues of G proteins; to help split ATP.
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"Targeting renal dipeptidase (dehydropeptidase I) for inactivation by mechanism-based inactivators." Journal of Medicinal Chemistry 34.6 (1991): 1914-916. Web. The addition of cobalt or manganese ions cause the enzyme to take on different conformations, which suggests that the enzyme may be able to hydrolyze different dipeptides depending on which metal ions are present—aka the metal-content of one’s micronutrient intake could affect their renal dipeptidase’s ability to metabolize various dipeptides.Hayman, Selma, Joselina S. Gatmaitan, and Elizabeth K. Patterson.
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The ATP hydrolyzing activity is indispensable for the p97/CDC48 functions. The two ATPase domains of p97 (D1 and D2) are not equivalent because the D2 domain displays higher ATPase activity than the D1 domain in wild-type protein. Nevertheless, their activities are dependent of each other. For example, nucleotide binding to the D1 domain is required for ATP binding to the D2 domain and nucleotide binding and hydrolysis in D2 is required for the D1 domain to hydrolyze ATP.
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Elastases form a subfamily of serine proteases that hydrolyze many proteins in addition to elastin. Humans have six elastase genes that encode the structurally similar proteins elastase 1, 2, 2A, 2B, 3A, and 3B. Neutrophil elastase hydrolyzes proteins within specialized neutrophil lysosomes, called azurophil granules, as well as proteins of the extracellular matrix following the protein's release from activated neutrophils. Neutrophil elastase may play a role in degenerative and inflammatory diseases by its proteolysis of collagen-IV and elastin of the extracellular matrix.
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Once in the periplasm they are cleaved by the pre-pilin peptidase GspO and converted into mature pseudopilins. The mature pseudopilins can then insert themselves into the inner membrane where they will exist until pseudopilus assembly occurs. #The secretion ATPase GspE will then bind and hydrolyze ATP and the energy produced is used to power the formation of the pseudopilus. GspE is located in the cytoplasm but remains associated with the inner membrane complex via interactions with both GspL and GspF.
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ARF binds to two forms of the guanosine nucleotide, guanosine triphosphate (GTP) and guanosine diphosphate (GDP). The shape of the ARF molecule is dependent upon the form to which it is bound, allowing it to serve in a regulatory capacity. ARF requires assistance from other proteins in order to switch between binding to GTP and GDP. GTPase activating proteins (GAPs) force ARF to hydrolyze bound GTP to GDP, and Guanine nucleotide exchange factors force ARF to adopt a new GTP molecule in place of a bound GDP.
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Cerastocytin, like most other serine proteases,Nelson, D. and Cox, M. Lehninger Principles of Biochemistry (4th Ed.), W.H. Freeman and Company, New York (2005). thrombin specifically, has three distinguishing features: the hydrophobic pocket, the positive surface and the catalytic triad. Additionally, the tertiary structure of cerastocytin is maintained by disulfide bridges similar to those formed in other serine proteases. This structural similarity results of cerastocytin's ability to clot platelets and hydrolyze fibrinogen at the concentration of 5 nM, closely mimics the activity of thrombin at 1nM.
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The chemistry of acid halides and anhydrides is similar. While anhydrides cannot be converted to acid halides, they can be converted to the remaining acyl derivatives. Anhydrides also participate in Schotten–Baumann-type reactions to furnish esters and amides from alcohols and amines, and water can hydrolyze anhydrides to their corresponding acids. As with acid halides, anhydrides can also react with carbon nucleophiles to furnish ketones and/or tertiary alcohols, and can participate in both the Friedel–Crafts acylation and the Weinreb ketone synthesis.
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The subunit Rpn12 incorporated into 19S regulatory particle when 19S lid and base bind together. Among these lid subunits, protein Rpn11 presents the metalloproteases activity to hydrolyze the ubiquitin molecules from the poly-ubiquitin chain before protein substrates are unfolded and degraded. During substrate degradation, the 19S regulatory particles undergo a conformation switch that is characterized by a rearranged ATPase ring with uniform subunit interfaces. Notably, Rpn11 migrates from an occluded position to directly above the central pore, thus facilitating substrate deubiquitination concomitant with translocation.
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At first, RAPTA was anticipated to hydrolyze and interact with DNA to target primary tumors, which is similar to the platinum analogue cisplatin. Studies showed that adducts form between RAPTA compounds and proteins (especially cathepsin B and thioredoxin reductase(TrxR)). Moreover, the reactivity of RAPTA in the presence of protein was totally different than that of cisplatin. In vitro studies showed that cytotoxicity of RAPTA derivatives was much less as compared to cisplatin, and some RAPTA compounds are not even cytotoxic to healthy cells.
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The enzymes that hydrolyze the peptidoglycan cross-links continue to function, even while those that form such cross-links do not. This weakens the cell wall of the bacterium, and osmotic pressure becomes increasingly uncompensated—eventually causing cell death (cytolysis). In addition, the build-up of peptidoglycan precursors triggers the activation of bacterial cell wall hydrolases and autolysins, which further digest the cell wall's peptidoglycans. The small size of the penicillins increases their potency, by allowing them to penetrate the entire depth of the cell wall.
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However, monogastric animals do not carry bacteria that produce phytase, thus, these animals cannot use phytic acid as a major source of phosphorus and it is excreted in the feces. However, human—especially vegetarians and vegans due to increased gut microbiome adaptation—can have microbes in their gut that can produce phytase that break down phytic acid. Phytic acid and its metabolites have several other important roles in Eukaryotic physiological processes. As such, phytases, which hydrolyze phytic acid and its metabolites, also have important roles.
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Smoked cigarette butts and cigarette tobacco are toxic to water organisms such as the marine topsmelt (Atherinops affinis) and the freshwater fathead minnow (Pimephales promelas). Atmospheric moisture, gastric acid, light, and enzymes hydrolyze cellulose acetate to acetic acid and cellulose. Cellulose may be further hydrolyzed to cellobiose or glucose in an acidic medium, and eventually form valuable humus. Humans cannot digest cellulose and excrete the fibers in feces, because, unlike ruminant animals, rabbits, rodents, termites, and some bacteria and fungi, they lack cellulolytic enzymes such as cellulase.
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S. salivarius group organisms are positive for acetoin production and are esculin positive but are negative for arginine hydrolysis and fermentation of mannitol and sorbitol. S. mutans group Members of the S. mutans group are primarily isolated from the human oral cavity and includes several species that are phenotypically similar. S. mutans and S. sobrinus are the species within this group most commonly isolated from human infection. They do not hydrolyze arginine but are positive for acetoin production, esculin hydrolysis, and mannitol and sorbitol fermentation.
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The amino acid sequences on the surface of the two domains facing each other are conserved in bacterial and firefly luciferase, thereby strongly suggesting that the active site is located in the cleft between the domains. During a reaction, luciferase has a conformational change and goes into a “closed” form with the two domains coming together to enclose the substrate. This ensures that water is excluded from the reaction and does not hydrolyze ATP or the electronically excited product. Diagram of the secondary structure of firefly luciferase.
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The function of PNKD proteins are unknown but the long and medium isoforms of PNKD contain a conserved β-lactamase domain which suggest it may function as an enzyme. The closest mammalian homolog to PNKD is HAGH, an enzyme involves in a two-step reaction to hydrolyze SLG and produce D-lactic acid and reduced GSH. However, the hydrolytic activity of PNKD is minimal. The long form of PNKD is neuronal specific and encodes a synaptic protein that localizes dominantly to the pre- synaptic membrane.
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The abgT gene is preceded by two genes, abgA and abgB, which code for homologous amino acyl amino hydrolases and hydrolyze p-aminobenzoyl glutamate to p-aminobenzoate and glutamate. Because of the structural similarity of p-aminobenzoyl-glutatmate to peptides, and the enzymatic activities of the abgA and abgB gene products, it has been suggested that AbgT is also a peptide transporter. Demonstration of an energy requirement suggested an H+-dependent mechanism. Expression of these genes is regulated by AbgR and an unknown effector.
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As a result, a mosquito replete with blood can continue to absorb sugar, even as the blood meal is slowly digested over a period of several days. Once blood is in the stomach, the midgut of the female synthesizes proteolytic enzymes that hydrolyze the blood proteins into free amino acids. These are used as building blocks for the synthesis of vitellogenin, which are the precursors for egg yolk protein. In the mosquito Anopheles stephensi, trypsin activity is restricted entirely to the posterior midgut lumen.
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Enzymes called peptidylarginine deiminases (PADs) hydrolyze the imine group of arginines and attach a keto group, so that there is one less positive charge on the amino acid residue. This process has been involved in the activation of gene expression by making the modified histones less tightly bound to DNA and thus making the chromatin more accessible. PADs can also produce the opposite effect by removing or inhibiting mono-methylation of arginine residues on histones and thus antagonizing the positive effect arginine methylation has on transcriptional activity.
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Muscimol was synthesized in 1965 by Gagneux, who utilized a bromo-isoxazole starting material in a two step reaction. 3-bromo-5-aminomethyl-isoxazole (1) was refluxed in a mixture of Methanol and Potassium Hydroxide for 30 hours, resulting in 3-methoxy-5-aminomethyl-isoxazole (2) with a yield of 60%. 450px (2) was then refluxed in concentrated hydrochloric acid to hydrolyze the methoxy group, and the zwitterion crystallized from a solution of methanol and tetrahydrofuran after the addition of triethylamine, resulting in a 50% yield. 450px Chemists report having struggled to reproduce these results.
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Grignard reagents do not typically react with organic halides, in contrast with their high reactivity with other main group halides. In the presence of metal catalysts, however, Grignard reagents participate in C-C coupling reactions. For example, nonylmagnesium bromide reacts with methyl p-chlorobenzoate to give p-nonylbenzoic acid, in the presence of Tris(acetylacetonato)iron(III) (Fe(acac)3), after workup with NaOH to hydrolyze the ester, shown as follows. Without the Fe(acac)3, the Grignard reagent would attack the ester group over the aryl halide.
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UCH-L1 is a member of a gene family whose products hydrolyze small C-terminal adducts of ubiquitin to generate the ubiquitin monomer. Expression of UCH-L1 is highly specific to neurons and to cells of the diffuse neuroendocrine system and their tumors. It is abundantly present in all neurons (accounts for 1-2% of total brain protein), expressed specifically in neurons and testis/ovary. The catalytic triad of UCH-L1 contains a cysteine at position 90, an aspartate at position 176, and a histidine at position 161 that are responsible for its hydrolase activity.
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Lead(II) compounds are characteristic of the inorganic chemistry of lead. Even strong oxidizing agents like fluorine and chlorine react with lead to give only PbF2 and PbCl2. Lead(II) ions are usually colorless in solution, and partially hydrolyze to form Pb(OH)+ and finally [Pb4(OH)4]4+ (in which the hydroxyl ions act as bridging ligands), but are not reducing agents as tin(II) ions are. Techniques for identifying the presence of the Pb2+ ion in water generally rely on the precipitation of lead(II) chloride using dilute hydrochloric acid.
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An example of the use of sodium carbonate as an alkali is when washing soda (another name for sodium carbonate) acts on insoluble esters, such as triglycerides, commonly known as fats, to hydrolyze them and make them soluble. Bauxite, a basic hydroxide of aluminium, is the principal ore from which the metal is manufactured. Similarly, goethite (α-FeO(OH)) and lepidocrocite (γ-FeO(OH)), basic hydroxides of iron, are among the principal ores used for the manufacture of metallic iron. Numerous other uses can be found in the articles on individual hydroxides.
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The 6-week old infant was unable to hydrolyze dietary protein due to a singular deficiency of pancreatic trypsinogen. This inborn error of metabolism, resulting in failure to thrive, became known as trypsinogen deficiency disease. In 1972, he identified a rare inherited syndrome in a father and four of his six children, characterized by the triad of imperforate anus, dysplastic ears, and thumb malformations, subsequently known as Townes-Brocks syndrome. Townes-Brocks syndrome was later found to be caused by a mutation in the DACT1 gene on chromosome 14q23.
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Acyl-CoA thioesterase 2, also known as ACOT2, is an enzyme which in humans is encoded by the ACOT2 gene. Acyl-CoA thioesterases, such as ACOT2, are a group of enzymes that hydrolyze Coenzyme A (CoA) esters, such as acyl-CoAs, bile CoAs, and CoA esters of prostaglandins, to the corresponding free acid and CoA. ACOT2 shows high acyl-CoA thioesterase activity on medium- and long-chain acyl-CoAs, with an optimal pH of 8.5. It is most active on myristoyl-CoA but also shows high activity on palmitoyl-CoA, stearoyl-CoA, and arachidoyl-CoA.
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L. cherrii is rod-shaped and considered an oxidase-negative bacterium since it lacks cytochrome c oxidase and does not use oxygen in its electron transport chain. L. cherrii also has the ability to autofluoresce a bluish-white color which was tested by placing the specimen under a Woods lamp-a mechanism that uses backlight to highlight bacteria-and measured under 366 nm wavelengths. L. cherrii lacks the ability to reduce nitrate, does not contain a urease, and does not convert D-glucose to acid. However, L. cherrii can hydrolyze gelatin.
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Leukotriene A4 hydrolase (LTA4H) acts primarily, if not exclusively, to hydrolyze leukotriene A4 (LTA4, i.e. 5S,6S-oxido-7E,9E,11Z,14Z-eicosatetetraenoic acid; IUPAC name 4-{(2S,3S)-3-[(1E,3E,5Z,8Z)-1,3,5,8-Tetradecatetraen-1-yl]-2-oxiranyl}butanoic acid) to its diol metabolite, leukotriene B4 (LTB4, i.e. 5S,12R-dihydroxy-6Z,8E,10E,14Z-icosatetraenoic acid; IUPA name 5S,6Z,8E,10E,12R,14Z)-5,12-Dihydroxy-6,8,10,14-icosatetraenoic acid). LTB4 is an important recruiter and activator of leukocytes involved in mediation in inflammatory responses and diseases.
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These enzymes cleave the β-lactam ring, an essential component of β-lactam antibiotics that are recognized by and bound to PBPs. Carbapenemases are divided into different classes, depending on the structure of the enzyme and the mechanism by which they hydrolyze the β-lactam ring. The two broad categories of carbapenemases are serine-carbopenemases, which contain serine at the active site, and metallocarbapenemases, which contain zinc at the active site. Class A carbapenemases are serine carbapenemases and are encoded on either the chromosome of the bacteria or a plasmid.
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Intact beta-lactam antibiotics act by binding to penicillin binding proteins (PBPs) involved in peptidoglycan synthesis. Beta-lactamases hydrolyze the amide bond between the carbonyl carbon and the nitrogen in the beta-lactam ring of susceptible beta- lactams and members of beta-lactam subclasses (including certain cephalosporins). After hydrolysis of the amide bond, the antibiotic lacks the ability to bind bacterial PBPs and is rendered useless. Visual detection of this process is essentially impossible with most cephalosporins because the shift of ultraviolet absorption from the intact versus hydrolyzed product occurs outside of the visible spectrum.
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GBS is also able to hydrolyze hippurate and this test can also be used to identify presumptively GBS. Hemolytic GBS strains produce an orange-brick-red non-isoprenoid polyene pigment (granadaene) when cultivated on granada medium that allows its straightforward identification. GBS can also be identified using MALDI-TOF (Matrix Assisted Laser Desorption/Ionization- Time of Flight) instruments. GBS colonies can additionally be identified tentatively after their appearance in chromogenic agar media, nevertheless GBS-like colonies that develop in chromogenic media should be confirmed as GBS using additional reliable tests (e.g.
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In the second step the now deprotonated acidic carboxylate acts as a base and assists a nucleophilic water to hydrolyze the glycosyl enzyme intermediate, giving the hydrolyzed product. The mechanism is illustrated below for hen egg white lysozyme. center An alternative mechanism for hydrolysis with retention of stereochemistry can occur that proceeds through a nucleophilic residue that is bound to the substrate, rather than being attached to the enzyme. Such mechanisms are common for certain N-acetylhexosaminidases, which have an acetamido group capable of neighboring group participation to form an intermediate oxazoline or oxazolinium ion.
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The enantioselective synthesis was accomplished by J. K. Whitesell by adding Pseudomonas fluorescens lipase to racemic trans-2-phenylcyclohexyl chloroacetate. This enzyme is able to hydrolyze the ester bond of the (−)-enantiomer but not the (+)-enantiomer. The (−)-cyclohexanol and the (+)-ester are separated by fractional crystallization and the isolated (+)-ester hydrolyzed to the (+)-cyclohexanol in a separate step. The enantiomers have also been prepared by the Sharpless asymmetric dihydroxylation of 1-phenylcyclohexene to the diol followed by the selective reduction of the 1-hydroxyl group by Raney nickel.
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Quisqualic acid The mGluRs in group I, including mGluR1 and mGluR5, are stimulated most strongly by the excitatory amino acid analog L-quisqualic acid. Stimulating the receptors causes the associated enzyme phospholipase C to hydrolyze phosphoinositide phospholipids in the cell's plasma membrane. This leads to the formation of inositol 1,4,5-trisphosphate (IP3) and diacyl glycerol. Due to its hydrophilic character, IP3 can travel to the endoplasmic reticulum, where it induces, via fixation on its receptor, the opening of calcium channels increasing in this way the cytosolic calcium concentrations.
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In addition to the important role it plays in biofuel production, xylanase is utilized in a number of other industrial and biotechnology applications due to its ability to hydrolyze cellulose and hemicellulose. These applications include the breakdown of agricultural and forestry wastes, working as a feed additive to facilitate greater nutrient uptake by livestock, and as an ingredient in bread making to improve the rise and texture of the bread. Generic Biodiesel Reaction. Lipases can serve as a biocatalyst in this reaction Lipases are one of the most used exoenzymes in biotechnology and industrial applications.
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Acarbose inhibits enzymes (glycoside hydrolases) needed to digest carbohydrates, specifically, alpha- glucosidase enzymes in the brush border of the small intestines, and pancreatic alpha-amylase. Pancreatic alpha-amylase hydrolyzes complex starches to oligosaccharides in the lumen of the small intestine, whereas the membrane- bound intestinal alpha-glucosidases hydrolyze oligosaccharides, trisaccharides, and disaccharides to glucose and other monosaccharides in the small intestine. Inhibition of these enzyme systems reduces the rate of digestion of complex carbohydrates. Less glucose is absorbed because the carbohydrates are not broken down into glucose molecules.
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The cell membrane of nearly all organisms is primarily made up of a phospholipid bilayer, a micelle of hydrophobic fatty acid esters with polar, hydrophilic phosphate "head" groups. Membranes contain additional components, some of which can participate in acid-base reactions. In humans and many other animals, hydrochloric acid is a part of the gastric acid secreted within the stomach to help hydrolyze proteins and polysaccharides, as well as converting the inactive pro-enzyme, pepsinogen into the enzyme, pepsin. Some organisms produce acids for defense; for example, ants produce formic acid.
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In addition, B. longum can uniquely ferment galactomannan-rich natural gum using glucosaminidases and alpha-mannosidases that participate in the fermentation of glucosamine and mannose, respectively. The high number of genes associated with oligosaccharide metabolism is a result of gene duplication and horizontal gene transfer, indicating that B. longum is under selective pressure to increase its capability to compete for various substrates in the gastrointestinal tract. Furthermore, B. longum possesses hydrolases, deaminases, and dehydratases to ferment amino acids. B. longum also has bile salt hydrolases to hydrolyze bile salts into amino acids and bile acids.
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The standard way to hydrolyze a protein or peptide into its constituent amino acids for analysis is to heat it to 105 °C for around 24 hours in 6M hydrochloric acid. However, some proteins are resistant to acid hydrolysis. One well-known example is ribonuclease A, which can be purified by treating crude extracts with hot sulfuric acid so that other proteins become degraded while ribonuclease A is left intact. Certain chemicals cause proteolysis only after specific residues, and these can be used to selectively break down a protein into smaller polypeptides for laboratory analysis.
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Many cellular proteins cleave (hydrolyze) nucleoside triphosphates-adenosine triphosphate (ATP) or guanosine triphosphate (GTP)-to their diphosphate forms (ADP and GDP) as a source of energy and to drive conformational changes. These changes in turn affect the structural, enzymatic, or signalling properties of the protein. Nucleotide exchange factors actively assist in the exchange of depleted nucleoside diphosphates for fresh nucleoside triphosphates. NEFs are specific for the nucleotides they exchange (ADP or GDP, but not both) and are often specific to a single protein or class of proteins with which they interact.
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Whether to add organic solvent into aqueous solvent, or vice versa, becomes important on the industrial scale. Depending on your solvents, emulsions can form, and the time for your layers to separate can be extended if the mixing between solvents is not optimal. When adding organic solvent to aqueous, stoichiometry must be considered again as the excess of water could hydrolyze organic compounds in only mildly acid base conditions. In an even wider scope, the location of your chemical plant can play a role in the ambient temperature of your reaction vessel.
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Recombinant phytases are added commonly in agriculture to animal feed of monogastric animals to enhance the feed's nutrient bioavailability. These nutrients include phosphorus which is bound to phytates in the form of their phosphate groups. In contrast to ruminants like cattle, gut bacteria of monogastric animals like pigs and chickens can't properly hydrolyze these groups free so that the digestive system of the animal can use the phosphorus. Unabsorbed phosphorus is thus wasted and may end up into the environment in animal manure via agricultural runoff and cause eutrophication.
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As part of phase II metabolism, the resulting carboxylates are then often conjugated by other enzymes to increase solubility and eventually excreted. This enzyme is known to hydrolyze aromatic and aliphatic esters and can manage cellular cholesterol esterification levels. It may also play a role in detoxification in the lung and/or protection of the central nervous system from ester or amide compounds. The protein contains an amino acid sequence at its N-terminus that sends it into the endoplasmic reticulum where a C-terminal sequence can bind to a KDEL receptor.
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This causes increased charge density on the beta phosphate of GTP and planarization of the gamma phosphate, which creates an opening and reduces steric hindrance for water to hydrolyze the phosphoanhydride beta-gamma bond. This is because the gamma phosphate's bond to the beta phosphate bends, exposing its connection and allowing the subsequent nucleophilic substitution reaction initiated by water. The complex formed with RGS4 assists in this process by creating strain on the bond between the gamma and beta phosphates and assisting in distributing more charge onto the beta phosphate.
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DLC1 is involved in the phosphoinositide and insulin signaling cascades. As mentioned, the C-terminal START domain of DLC1 is involved in phosphoinositide signaling: it is able to interact with phospholipase C-δ1 (PLC- δ1), thereby stimulating it to hydrolyze phosphatidylinositol 4,5-bisphosphate (PIP2) into the second messengers inositol 1,4,5-triphosphate (IP3) and diacylglycerol (DAG). IP3 causes calcium to be released from vesicles into the cytoplasm, which in turn regulates proteins which are sensitive to high calcium concentrations. DAG activates protein kinase C (PKC) and triggers a cascade of intracellular signals.
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Arginine fingers often work with other features in their assistance of catalysis. For example, in some trimeric dUTPases, such as those of M. tuberculosis, arginine fingers at the 64th and 140th residue can work with magnesium to cleave dUTP into dUMP and a pyrophosphate. The underlying mechanism of action for this is a nucleophilic attack; the positively charged magnesium ion () pulls on an oxygen of the beta and gamma phosphates to allow water to hydrolyze the bond between the beta and alpha phosphates. The arginine fingers help stabilize the transition state.
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NOx is either reduced by catalytic reduction with ammonia in a catalytic converter (selective catalytic reduction, SCR) or by a high-temperature reaction with ammonia in the furnace (selective non-catalytic reduction, SNCR). Urea may be substituted for ammonia as the reducing reagent but must be supplied earlier in the process so that it can hydrolyze into ammonia. Substitution of urea can reduce costs and potential hazards associated with storage of anhydrous ammonia. Heavy metals are often adsorbed on injected active carbon powder, which is collected by particle filtration.
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To meet or exceed the OECD Guideline 301B criteria for "readily biodegradable", a sample must produce 60% of the theoretical amount of carbon dioxide (TCO2) within a 10-day window of reaching 10% TCO2. The LEFA used in the study had a final average cumulative percent biodegradation of 92.0% and the test solution had a pH of 7.1 at the end of the 28-day test. Therefore, the test material met the criteria to be considered readily biodegradable. In the presence of water, lactylates will break down (hydrolyze) into fatty acid and lactic acid.
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Chlorine dioxide is a chemical compound with the formula ClO2 that exists as yellowish-green gas above 11 °C, a reddish-brown liquid between −59 °C and 11 °C, and as bright orange crystals when colder. It is an oxidizing agent, able to transfer oxygen to a variety of substrates, while gaining one or more electrons via oxidation-reduction (redox). It does not hydrolyze when it enters water, and is usually handled as a dissolved gas in solution in water. Potential hazards with chlorine dioxide include health concerns, explosiveness and fire ignition.
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Some iron(III) salts, like the chloride , sulfate , and nitrate are soluble in water. However, other salts like oxide (hematite) and iron(III) oxide- hydroxide are extremely insoluble, at least at neutral pH, due to their polymeric structure. Therefore, those soluble iron(III) salts tend to hydrolyze when dissolved in pure water, producing iron(III) hydroxide that immediately converts to polymeric oxide-hydroxide via the process called olation and precipitates out of the solution. That reaction liberates hydrogen ions to the solution, lowering the pH, until an equilibrium is reached.
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As it requires time to hydrolyze sucrose into glucose and fructose (in low pH conditions), there is a long delay between manufacture and spoilage of products contaminated with this yeast when sucrose is used as the primary carbohydrate ingredient. This is usually preceded by a lag of 2 – 4 weeks and apparent deterioration of product quality is only shown 2 – 3 months after manufacturing Silliker, J.H., 1980. Fats and oils. In: Silliker, J.H., Elliott, R.P., Baird-Darner, A.C., Bryan, F.L., Christian, J.H.B., Clark, D.S., Olson, J.C., Roberts, T.A. (Eds), Microbial ecology of foods, vol. 1.
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Yeast Sir2 and some, but not all, sirtuins are protein deacetylases. Unlike other known protein deacetylases, which simply hydrolyze acetyl-lysine residues, the sirtuin-mediated deacetylation reaction couples lysine deacetylation to NAD+ hydrolysis. This hydrolysis yields O-acetyl-ADP-ribose, the deacetylated substrate and nicotinamide, which is an inhibitor of sirtuin activity itself. The dependence of sirtuins on NAD+ links their enzymatic activity directly to the energy status of the cell via the cellular NAD+:NADH ratio, the absolute levels of NAD+, NADH or nicotinamide or a combination of these variables.
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For over the past 100 years, ginger protease has traditionally been used to curdle milk to create ginger milk curd, a gel-like Cantonese dish made from hot milk and ginger juice. The milk clotting ability and specificity of ginger protease to proteolysis of κ-casein make the enzyme a potential vegetable rennet substitute for cheese production. Milk coagulation is traditionally accomplished by coagulating enzymes extracted from sources such as rennet. In rennet, three chymosin isozymes hydrolyze κ-casein, a major protein fraction within milk, between Phe105 and Met106.
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OXA beta-lactamases were long recognized as a less common but also plasmid-mediated beta-lactamase variety that could hydrolyze oxacillin and related anti-staphylococcal penicillins. These beta- lactamases differ from the TEM and SHV enzymes in that they belong to molecular class D and functional group 2d . The OXA-type beta-lactamases confer resistance to ampicillin and cephalothin and are characterized by their high hydrolytic activity against oxacillin and cloxacillin and the fact that they are poorly inhibited by clavulanic acid. Amino acid substitutions in OXA enzymes can also give the ESBL phenotype.
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Nitrilases have critical roles in plant- microbe interactions for defense, detoxification, nitrogen utilization, and plant hormone synthesis. In plants, there are two distinguishable groups in regard to substrate specificity: those with high hydrolytic activity towards arylacetonitriles and those with high activity towards β-cyano-L-alanine. NIT1, 2, and 3 of the A. thaliana species are examples of the first group of plant nitrilases (arylacetonitrilases) which hydrolyze the nitriles produced during the synthesis or degradation of cyanogenic glycosides and glucosinolates. The arylcetonitrile substrates for these particular enzymes consist of phenylpropionitrile and other products that result from glucosinolate metabolism.
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The basic reaction of urea and formaldehyde to create a urea- formaldehyde resin, followed by the condensation Urea-formaldehyde resins (UF) are a class of impregnation resins for wood modification made by reacting urea with formaldehyde. This resin can be polymerized after impregnation into the wood substrate by oven-curing. UF resins are beginning to be used less in the wood modification industry due to the fact that they are less durable than other impregnation resins and do not stand up well to harsh weather conditions. When exposed to water, UF resins can hydrolyze to release formaldehyde out of the wood substrate.
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The history of oligopeptidases originates in the late 1960s, when the rabbit brain was searched for enzymes that cause inactivation of the nonapeptide bradykinin. In the early and mid 1970s two thiol-activated endopeptidases, responsible for more than 90% of bradykinin inactivation, were isolated from cytosol of rabbit brain, and characterized. They correspond to EOPA (endooligopeptidase A, EC 3.4.22.19), and Prolyl endopeptidase or Prolyl oligopeptidase (POP) (EC 3.4.21.26). Since their activities are restricted to oligopeptides (usually from 8-13 amino acid residues), and do not hydrolyze proteins or large peptides (>30 amino acid residues), they were designated oligopeptidases.
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The ability of importins and exportins to transport their cargo is regulated by GTPases, enzymes that hydrolyze the molecule guanosine triphosphate (GTP) to release energy. The key GTPase in nuclear transport is Ran, which can bind either GTP or GDP (guanosine diphosphate), depending on whether it is located in the nucleus or the cytoplasm. Whereas importins depend on RanGTP to dissociate from their cargo, exportins require RanGTP in order to bind to their cargo. Nuclear import depends on the importin binding its cargo in the cytoplasm and carrying it through the nuclear pore into the nucleus.
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Normally, G proteins are regulated by GAP, which results in controlled cell division. Often, this oncogenic behavior is due to a loss of function of GAPs associated with those G proteins or a loss of the G protein's ability to respond to its GAP. With the former, G proteins are unable to hydrolyze GTP quickly, resulting in sustained expression of the active form of G proteins. Although the G proteins have weak hydrolytic activity, in the presence of functional GEFs, the inactivated G proteins are constantly replaced with activated ones because the GEFs exchange GDP for GTP in these proteins.
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That is to say that enzymes do not necessarily perform all the reactions in the body that may be possible in the laboratory. For example, while fatty acid amide hydrolase (FAAH) can hydrolyze the endocannabinoids 2-arachidonoylglycerol (2-AG) and anandamide at comparable rates in vitro, genetic or pharmacological disruption of FAAH elevates anandamide but not 2-AG, suggesting that 2-AG is not an endogenous, in vivo substrate for FAAH. In another example, the N-acyl taurines (NATs) are observed to increase dramatically in FAAH-disrupted animals, but are actually poor in vitro FAAH substrates.
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Traditional Cuban-style coffee is made using the darker roasts, typically either Italian or Spanish roasts, with the brands Cafe Bustelo Cafe La Llave and Cafe Pilón being popular. It can be made using an electric espresso machine, but is commonly made with a moka pot. Either some or all of the espresso is vigorously mixed with a spoon into a creamy foam called espuma or espumita. The heat from the coffee-making process will hydrolyze some of the sucrose, thereby creating a sweeter and slightly more viscous result than a normal pull or adding sugar at the table.
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Parasutterella species are Gram- negative, coccobacilli (circular and rod-shaped), strictly (or obligate) anaerobic, non-motile bacteria. When cultured, colonies from both P. excrementihominis and P. secunda appeared translucent to beige in color, convex and circular in shape, and extremely small in size. Both species do not metabolize glucose, lactate, or succinate or produce indole or short-chain fatty acids. Additionally, these bacteria do not reduce nitrate and are catalase-negative (inability to breakdown hydrogen peroxide into oxygen and water), urease-negative (inability to hydrolyze urea to ammonia and carbon dioxide), and oxidase-negative (inability to use oxygen).
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The main function of the SEC23A protein is to hydrolyze or break down a guanosine triphosphate (GTP) molecule bound to the SAR1A protein at the start of the COPII pathway. The energy released from the breaking of the GTP bond provides energy necessary to undergo another reaction. This triggers uncoating of the vesicle (a membrane bound carrying compartment for molecules) containing a secretory protein destined for packaging in the Golgi apparatus of the cell. Uncoating the vesicle exposes SNARE proteins which are needed for the vesicle to bind to the membrane site on the endoplasmic reticulum.
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Lingual lipase is a member of a family of digestive enzymes called triacylglycerol lipases, EC 3.1.1.3, that use the catalytic triad of aspartate, histidine, and serine to hydrolyze medium and long-chain triglycerides into partial glycerides and free fatty acids. The enzyme, released into the mouth along with the saliva, catalyzes the first reaction in the digestion of dietary lipid, with diglycerides being the primary reaction product. However, due to the unique characteristics of lingual lipase, including a pH optimum 4.5–5.4 and its ability to catalyze reactions without bile salts, the lipolytic activity continues through to the stomach.
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During pathogenesis, the fungus undergoes protease elaboration to hydrolyze structural proteins (such as the keratin found in hair), and isolates show peak values between days 18–22 during the sporulation phase. There are potentially 23 genes that may have mechanistic roles of this skin infection, and 21 show significant differences in infection rates, especially among children. The genes are typically involved in leukocyte activation and migration, and formation and integrity of the extracellular matrix. In molecular studies of its virulence, common target genes include CarbM14, CER, and Sub2, which encode the proteases carboxypeptidase, ceraminidase, and subtilisin, respectively.
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This protein complex is functionally similar to the TOM/TIM Complex located on the outer and inner membranes of the mitochondria, in the sense that it too transports proteins across multiple membranes and into the lumen of an organelle. Both complexes (TOC/TIC) are GTPases, that is, they must both hydrolyze GTP in order to power the translocation. The chloroplast also harnesses the power of an electrochemical gradient using protons. The gradient is only used to power transport across the thylakoid membrane, however, while the gradient in the mitochondria is used to power transport across its inner membrane.
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Sudan dyes have high affinity to fats, therefore they are used to demonstrate triglycerides, lipids, and lipoproteins. Alcoholic solutions of Sudan dyes are usually used, however pyridine solutions can be used in some situations as well. Sudan stain test is often used to determine the level of fecal fat to diagnose steatorrhea. A small sample is dissolved in water or saline, glacial acetic acid is added to hydrolyze the insoluble salts of fatty acids, a few drops of alcoholic solution of Sudan III are added, the sample is spread on a microscopic slide, and heated twice to boil.
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Ni2+ is taken up into prokaryotic cells by one of two types of high-affinity transport systems. The first method involves ABC-type transporters (discussed in this article) and the second mechanism makes use of transition-metal permeases (such as HoxN of Ralstonia eutropha). The ABC-type transporter system consists of five proteins, NikA–E, that carry out the ATP-dependent transport of Ni2+. NikA is a soluble, periplasmic, Ni- binding protein; NikB and NikC form a transmembrane pore for passage of Ni; and NikD and NikE hydrolyze ATP and couple this energy to Ni2+-transport.
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An abzyme (from antibody and enzyme), also called catmab (from catalytic monoclonal antibody), and most often called catalytic antibody, is a monoclonal antibody with catalytic activity. Abzymes are usually raised in lab animals immunized against synthetic haptens, but some natural abzymes can be found in normal humans (anti-vasoactive intestinal peptide autoantibodies) and in patients with autoimmune diseases such as systemic lupus erythematosus, where they can bind to and hydrolyze DNA. To date abzymes display only weak, modest catalytic activity and have not proved to be of any practical use. They are, however, subjects of considerable academic interest.
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A 1961 in vitro study conducted by Hodge showed that lipase will hydrolyze lactylates into stearic acid and lactic acid. A 1981 study expanded this research by treating various tissue and biological fluid preparations with 14C-labeled CSL, incubated at 37 °C (98.6 °F), and examined for lactylate hydrolysis. Assays used thin layer chromatography (TLC) with radioactivity detection to determine the levels of intact CSL and lactate (lactic acid). 14C-labeled CSL was found to undergo rapid hydrolysis in homogenized rat, mouse, and guinea-pig liver and intestinal mucosa, whereas CSL hydrolyzed much slower in rat and mice whole blood.
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Standard conditions for using NBS in allylic and/or benzylic bromination involves refluxing a solution of NBS in anhydrous CCl4 with a radical initiator—usually azobisisobutyronitrile (AIBN) or benzoyl peroxide, irradiation, or both to effect radical initiation. The allylic and benzylic radical intermediates formed during this reaction are more stable than other carbon radicals and the major products are allylic and benzylic bromides. This is also called the Wohl–Ziegler reaction. :Allylic bromination of 2-heptene The carbon tetrachloride must be maintained anhydrous throughout the reaction, as the presence of water may likely hydrolyze the desired product.
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APE2 has much weaker AP endonuclease activity than APE1, but its 3'-5' exonuclease activity is strong compared with APE1 and it has a fairly strong 3'-phosphodiesterase activity. The APE2 3' –5' exonuclease activity has the ability to hydrolyze blunt-ended duplex DNA, partial DNA duplexes with a recessed 3' -terminus or a single nucleotide gap containing heteroduplex DNA. The APE2 3'-phosphodiesterase activity can remove modified 3'-termini, such as 3'-phosphoglycolate as well as mismatched nucleotides from the 3' primer end of DNA. APE2 is required for ATR-Chk1 DNA damage response following oxidative stress.
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The scanning of an mRNA continues until the first AUG codon on the mRNA is reached, this is known as the "First AUG Rule". While exceptions to the "First AUG Rule" exist, most exceptions take place at a second AUG codon that is located 3 to 5 nucleotides downstream from the first AUG, or within 10 nucleotides from the 5′ end of the mRNA. At the AUG codon a Methionine tRNA anticodon is recognized by mRNA codon. Upon base pairing to the start codon the eIF5 in the PIC helps to hydrolyze a guanosine triphosphate (GTP) bound to the eIF2.
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RasGEF domain is domain found in the CDC25 family of guanine nucleotide exchange factors for Ras-like small GTPases. Ras proteins are membrane- associated molecular switches that bind GTP and GDP and slowly hydrolyze GTP to GDP. The balance between the GTP bound (active) and GDP bound (inactive) states is regulated by the opposite action of proteins activating the GTPase activity and that of proteins which promote the loss of bound GDP and the uptake of fresh GTP. The latter proteins are known as guanine-nucleotide dissociation stimulators (GDSs) (or also as guanine-nucleotide releasing (or exchange) factors (GRFs)).
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ESBL enzymes can hydrolyze all beta-lactam antibiotics, including cephalosporins, except for the carpabepenems. The first clinically observed ESBL enzymes were mutated versions of the narrow spectrum beta-lactamases, like TEM and SHV. Other ESBL enzymes originate outside of family Enterobacteriaceae, but have been spreading as well. In addition, since the plasmids that carry ESBL genes also commonly encode resistance determinants for many other antibiotics, ESBL strains are often resistant to many non-beta- lactam antibiotics as well,Broad spectrum antibiotics and resistance in non- target bacteria: an example from tetracycline, Journal of Pure and Applied Microbiology, (2014); 8(4): 2667-2671.
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Additionally, they were able to plasmolyze the bacteriophages so that they went into osmotic shock, which effectively created a solution containing most of the 32P and a heavier solution containing structures called "ghosts" that contained the 35S and the protein coat of the virus. It was found that these "ghosts" could adsorb to bacteria that were susceptible to T2, although they contained no DNA and were simply the remains of the original bacterial capsule. They concluded that the protein protected the DNA from DNAse, but that once the two were separated and the phage was inactivated, the DNAse could hydrolyze the phage DNA.
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When the cell receives the signal to differentiate to a specific type of cell, H3K27me3 will be removed from the genes needed for differentiation, while H3K27me3 maintains repression of developmental control genes that are unnecessary for the chosen lineage. The developmentally regulated process of resolving bivalent chromatin is aided by the activity of ATP-chromatin remodelers such as SWI/SNF, which hydrolyze ATP to evict Polycomb-group proteins from bivalent chromatin. Only a specific subset of regulators will be activated by H3K4me3 to give a certain cell lineage. This mark activates developmental regulators upon differentiation, and makes the genes needed for differentiation more efficient.
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There are three paralogs of non-muscle myosin II (NM II), NM IIA, IIB, and IIC, with each having the heavy chain encoded on a different chromosome. All three paralogs appear to bind the same or very similar light chains and share basic properties as to structure and activation, but all three play distinct roles during vertebrate development and adulthood (for general reviews on NM IIs, see ). All NM IIs have two important features: they are MgATPase enzymes that can hydrolyze ATP thereby converting chemical energy into mechanical movement. In addition, they can form bipolar filaments which can interact with and exert tension on actin filaments.
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In shade conditions, the genes coding for XTH9, XTH15/XTR7, XTH16, XTH17, and XTH19 are up-regulated and these proteins act to hydrolyze and weaken the cell wall, allowing for expansion of the petiole cells. Like in seedlings, PIF7 is involved in the regulation of petiole and leaf growth due to low R:FR, by up-regulating auxin-related and brassinosteroid-response genes which promote growth. Auxin signalling is also essential to hyponasty, though its role is not yet fully understood. Leaf curling is primarily a response to phytochrome B converting to PR in shade conditions, which promotes unequal proliferation and growth of cells on the upper and lower leaf sides.
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Enzymatic activity of intact and PEGylated lysozyme can be evaluated using glycol chitosan by reacting 1 mL of 0.05% (w/v) glycol chitosan in 100 mM of pH 5.5 acetate buffer and 100 μL of the intact or PEGylated protein at 40 °C for 30 min and subsequently adding 2 mL of 0.5 M sodium carbonate with 1 μg of potassium ferricyanide. The mixture is immediately heated, boiled for 15 minutes, and cooled for spectral analysis at 420 nm. As the enzymatic activity to hydrolyze β-1,4- N-acetylglucosamine linkage was retained after PEGylation, there was no decay in the enzymatic activity by increasing the degree of PEGylation.
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The dissociated SNARE proteins have a higher energy state than the more stable cis-SNARE complex. It is believed that the energy that drives fusion is derived from the transition to a lower energy cis-SNARE complex. The ATP hydrolysis-coupled dissociation of SNARE complexes is an energy investment that can be compared to "cocking the gun" so that, once vesicle fusion is triggered, the process takes place spontaneously and at optimum velocity. A comparable process takes place in muscles, in which the myosin heads must first hydrolyze ATP in order to adapt the necessary conformation for interaction with actin and the subsequent power stroke to occur.
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Like other enzymes, the activity of F1FO ATP synthase is reversible. Large- enough quantities of ATP cause it to create a transmembrane proton gradient, this is used by fermenting bacteria that do not have an electron transport chain, but rather hydrolyze ATP to make a proton gradient, which they use to drive flagella and the transport of nutrients into the cell. In respiring bacteria under physiological conditions, ATP synthase, in general, runs in the opposite direction, creating ATP while using the proton motive force created by the electron transport chain as a source of energy. The overall process of creating energy in this fashion is termed oxidative phosphorylation.
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Efflux transporter- expressing cells actively pump substrates out of the cell, which results in a lower rate of substrate accumulation, lower intracellular concentration at steady state, or a faster rate of substrate elimination from cells loaded with the substrate. Transported radioactive substrates or labeled fluorescent dyes can be directly measured, or in an indirect set up, the modulation of the accumulation of a probe substrate (e.g. fluorescent dyes like rhodamine 123, or calcein) can be determined in the presence of a test drug. Calcein-AM, A highly permeable derivative of calcein readily penetrates into intact cells, where the endogenous esterases rapidly hydrolyze it to the fluorescent calcein.
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As per its classification, Ras has an intrinsic GTPase activity, which means that the protein on its own will hydrolyze a bound GTP molecule into GDP. However this process is too slow for efficient function, and hence the GAP for Ras, RasGAP, may bind to and stabilize the catalytic machinery of Ras, supplying additional catalytic residues ("arginine finger") such that a water molecule is optimally positioned for nucleophilic attack on the gamma- phosphate of GTP. An inorganic phosphate is released and the Ras molecule is now bound to a GDP. Since the GDP-bound form is "off" or "inactive" for signaling, GTPase Activating Protein inactivates Ras by activating its GTPase activity.
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Rho-dependent transcription terminators require a large protein called a Rho factor which exhibits RNA helicase activity to disrupt the mRNA- DNA-RNA polymerase transcriptional complex. Rho-dependent terminators are found in bacteria and phages. The Rho-dependent terminator occurs downstream of translational stop codons and consists of an unstructured, cytosine-rich sequence on the mRNA known as a Rho utilization site (rut) for which a consensus sequence has not been identified, and a downstream transcription stop point (tsp). The rut serves as a mRNA loading site and as an activator for Rho; activation enables Rho to efficiently hydrolyze ATP and translocate down the mRNA while it maintains contact with the rut site.
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Studies have shown that YbaK functions as a Cys-tRNAPro deacylase in vivo, deacetylation additionally involves turning genes off, hence, it can be assumed that it is preventing the addition of an amino acid to a tRNA molecule, thus preventing translation. In vitro studies with the full set of 20 E. coli aminoacyl-tRNAs revealed that the Haemophilus influenzae and E. coli YbaK proteins are moderately general aminoacyl-tRNA deacylases that preferentially hydrolyze Cys-tRNAPro and Cys-tRNACy. Furthermore, YbaK- mediated hydrolysis of aminoacyl-tRNA has been indicated to influence cell growth. It has been further indicated that YbaK domain is important in the editing function if the wrong amino acid has been joined to the wrong tRNA.
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Chemical pretreatment of the feedstock is required to hydrolyze (separate) hemicellulose, so it can be more effectively converted into sugars. The dilute acid pretreatment is developed based on the early work on acid hydrolysis of wood at the USFS's Forest Products Laboratory. Recently, the Forest Products Laboratory together with the University of Wisconsin–Madison developed a sulfite pretreatment to overcome the recalcitrance of lignocellulose for robust enzymatic hydrolysis of wood cellulose. US President George W. Bush, in his State of the Union address delivered January 31, 2006, proposed to expand the use of cellulosic ethanol. In his State of the Union Address on January 23, 2007, President Bush announced a proposed mandate for of ethanol by 2017.
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The main function of hormone-sensitive lipase is to mobilize the stored fats. HSL functions to hydrolyze either a fatty acid from a triacylglycerol molecule, freeing a fatty acid and diglyceride, or a fatty acid from a diacylglycerol molecule, freeing a fatty acid and monoglyceride. Another enzyme found in adipose tissue, Adipose Triglyceride Lipase (ATGL), has a higher affinity for triglycerides than HSL, and ATGL predominantly acts as the enzyme for triglyceride hydrolysis in the adipocyte. HSL is also known as triglyceride lipase, while the enzyme that cleaves the second fatty acid in the triglyceride is known as diglyceride lipase, and the third enzyme that cleaves the final fatty acid is called monoglyceride lipase.
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Pancreatic elastase is a form of elastase that is produced in the acinar cells of the pancreas, initially produced as an inactive zymogen and later activated in the duodenum by trypsin. Elastases form a subfamily of serine proteases, characterized by a distinctive structure consisting of two beta barrel domains converging at the active site that hydrolyze amides and esters amongst many proteins in addition to elastin, a type of connective tissue that holds organs together. Pancreatic elastase 1 is a serine endopeptidase, a specific type of protease that has the amino acid serine at its active site. Although the recommended name is pancreatic elastase, it can also be referred to as elastase-1, pancreatopeptidase, PE, or serine elastase.
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Ecdysteroid-phosphate Phosphatase is the first structure of a steroid phosphate phosphotase containing alpha beta folds common to members of the two histidine (2H)-Phosphatase superfamily with strong homology to the Suppressor of T-cell receptor signaling-1 (Sts-1 PGM) protein. The putative EPPase PGM active site contains signature residues shared by 2H-phosphatase enzymes, including a conserved histidine (His80) that acts as a nucleophile during catalysis. The physiological substrate ecdysone 22-phosphate was modeled in a hydrophobic cavity close to the phosphate-binding site. EPPase PGM shows limited substrate specificity with an ability to hydrolyze steroid phosphates, the phospho-tyrosine (pTyr) substrate analogue para-nitrophenylphosphate ( pNPP) and pTyr-containing peptides and proteins.
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Expansins characteristically cause wall stress relaxation and irreversible wall extension (wall creep). This process is essential for cell enlargement. Expansins are also expressed in ripening fruit where they function in fruit softening, and in grass pollen, where they loosen stigmatic cell walls and aid pollen tube penetration of the stigmain germinating seeds for cell wall disassembly, in floral organs for their patterning, in developing nitrogen- fixing nodules in legumes, in abscissing leaves, in parasitic plants, and in ‘resurrection’ plants during their rehydration. No enzymatic activity has been found for expansin and in particular, no glucanase activity: they don't hydrolyze the matrix polysaccharides; the only definitive assay for expansin activity is thus to measure wall stress relaxation or wall extension.
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Ceramide (Cer) can be generated by the breakdown of sphingomyelin (SM) by sphingomyelinases (SMases), which are enzymes that hydrolyze the phosphocholine group from the sphingosine backbone. Alternatively, this sphingosine-derived lipid (sphingolipid) can be synthesized from scratch (de novo) by the enzymes serine palmitoyl transferase (SPT) and ceramide synthase in organelles such as the endoplasmic reticulum (ER) and possibly, in the mitochondria-associated membranes (MAMs) and the perinuclear membranes. Being located in the metabolic hub, ceramide leads to the formation of other sphingolipids, with the C1 hydroxyl (-OH) group as the major site of modification. A sugar can be attached to ceramide (glycosylation) through the action of the enzymes, glucosyl or galactosyl ceramide synthases.
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Because some of the meat the Inuit eat is raw and fresh, or freshly frozen, they can obtain more carbohydrates from their meat, as dietary glycogen, than Westerners can. The Inuit practice of preserving a whole seal or bird carcass under an intact whole skin with a thick layer of blubber also permits some proteins to ferment, or hydrolyze, into carbohydrates. Furthermore, the blubber, organs, muscle and skin of the marine mammals that Inuit eat have significant glycogen stores, which assist those animals when oxygen is depleted on prolonged dives. For instance, when blubber is analyzed by direct carbohydrate measurements, it has been shown to contain as much as 8—30% carbohydrates.
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The reaction is exothermic, and the mixture can reach the boiling point, if external cooling is not applied. The resulting product, diethyl 3,5-dimethylpyrrole-2,4-dicarboxylate, has been called Knorr's Pyrrole ever since. In the Scheme above, R2 = COOEt, and R1 = R3 = Me represent this original reaction. Knorr's pyrrole can be derivatized in a number of useful manners. One equivalent of sodium hydroxide will saponify the 2-ester selectively. Dissolving Knorr's pyrrole in concentrated sulfuric acid, and then pouring the resulting solution into water will hydrolyze the 4-ester group selectively. The 5-methyl group can be variously oxidized to chloromethyl, aldehyde, or carboxylic acid functionality by the use of stoichiometric sulfuryl chloride in glacial acetic acid. Alternatively, the nitrogen atom can be alkylated.
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Examples of low temperature ERH include heat-enhanced bioremediation, heating the subsurface to temperatures above the solubility of dissolved gasses to induce VOC stripping (most notably carbon dioxide ebullition), heat enhanced in situ chemical oxidation (especially for persulfate activation), and heat-enhanced reduction (such as with iron-catalyzed reactions). ERH low-temperature heating can also be used to hydrolyze chlorinated alkanes in-situ at sub-boiling temperatures where hydrochloric acid released during hydrolysis further reacts with subsurface carbonates and bicarbonates to produce carbon dioxide for subsurface stripping of VOCs. Using low temperature heating coupled with bioremediation, chemical oxidation, or dechlorination will result in increased reaction rates. This can significantly reduce the time required for these remediation processes as compared to a remediation at ambient temperature.
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PETN is practically insoluble in water (0.01 g/100 ml at 50 °C), weakly soluble in common nonpolar solvents such as aliphatic hydrocarbons (like gasoline) or tetrachloromethane, but soluble in some other organic solvents, particularly in acetone (about 15 g/100 g of the solution at 20 °C, 55 g/100 g at 60 °C) and dimethylformamide (40 g/100 g of the solution at 40 °C, 70 g/100 g at 70 °C). PETN forms eutectic mixtures with some liquid or molten aromatic nitro compounds, e.g. trinitrotoluene (TNT) or tetryl. Due to steric hindrance of the adjacent neopentyl-like moiety, PETN is resistant to attack by many chemical reagents; it does not hydrolyze in water at room temperature or in weaker alkaline aqueous solutions.
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Pinocytosis In cellular biology, pinocytosis, otherwise known as fluid endocytosis and bulk-phase pinocytosis, is a mode of endocytosis in which small particles suspended in extracellular fluid are brought into the cell through an invagination of the cell membrane, resulting in a suspension of the particles within a small vesicle inside the cell. These pinocytotic vesicles then typically fuse with early endosomes to hydrolyze (break down) the particles. Pinocytosis is further segregated into the pathways macropinocytosis, clathrin-mediated endocytosis, caveolin-mediated endocytosis, or clathrin- and caveolin-independent endocytosis, all of which differ by the mechanism of vesicle formation as well as the resulting size of these vesicles. Pinocytosis is variably subdivided into categories depending on molecular mechanism and the fate of the internalized molecules.
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The concentration of the inhaled gas and duration of exposure and water contents of the tissues exposed are the key determinants of toxicity; moist tissues like the eyes, throat, and lungs are the most susceptible to damage.CDC Basic Facts Page last reviewed April 10, 2013. Page last updated April 10, 2013 Once inhaled, chlorine gas diffuses into the epithelial lining fluid (ELF) of the respiratory epithelium and may directly interact with small molecules, proteins and lipids there and damage them, or may hydrolyze to hypochlorous acid and hydrochloric acid which in turn generate chloride ions and reactive oxygen species; the dominant theory is that most damage is via the acids.Squadrito GL, Postlethwait EM, Matalon S. Elucidating mechanisms of chlorine toxicity: reaction kinetics, thermodynamics, and physiological implications.
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The START domain (amino acids 878-1081) contains a β-sheet which forms a hydrophobic tunnel held in place by α-helices. This region interacts with phospholipase C-δ1 (PLCδ1) and activates its ability to hydrolyze the membrane lipid phosphatidylinositol 4,5-bisphosphate (PIP2) into diacylglycerol (DAG) and inositol 1,4,5-triphosphate (IP3), which in turn activates protein kinase C (PKC) and increases intracellular calcium ion concentration, which regulates the actin cytoskeleton. In addition, hydrolysis of PIP2 releases actin regulatory proteins assembled at PIP2 molecules on the membrane and allows them to promote the disassembly of actin filaments. The C-terminus of DLC1 is also known to interact with caveolin-1, although the biological significance of this interaction has not yet been discovered.
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Based on the alignment for sequences of different bacteria correlated to ribonuclease E of Escherichia coli, it appears that about 70% of the sequences are highly conserved at the beginning of sequences and poorly conserved toward the end of sequences. When comparing the five other organisms’ sequences to the sequence of the ribonuclease E, it looks like most of the sequences share the same residues at the N-terminal since the member from ribonuclease E/G family has the same hydrolyze function. In other words, the large catalytic domain of the ribonuclease E/G family member is almost the same. In contrast, the small structural domain, which is located at the C-terminus, is varied for different organisms since the small domain contains a structural sequence that serves as scaffolding for other enzymes.
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The ABC module (approximately two hundred amino acid residues) is known to bind and hydrolyze ATP, thereby coupling transport to ATP hydrolysis in a large number of biological processes. The cassette is duplicated in several subfamilies. Its primary sequence is highly conserved, displaying a typical phosphate-binding loop: Walker A, and a magnesium binding site: Walker B. Besides these two regions, three other conserved motifs are present in the ABC cassette: the switch region which contains a histidine loop, postulated to polarize the attacking water molecule for hydrolysis, the signature conserved motif (LSGGQ) specific to the ABC transporter, and the Q-motif (between Walker A and the signature), which interacts with the gamma phosphate through a water bond. The Walker A, Walker B, Q-loop and switch region form the nucleotide binding site.
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The first clinical trial of mivacurium (BW1090U), in 1984, was conducted in a cohort of 63 US patients undergoing surgical anesthesia. at the Harvard Medical School at Massachusetts General Hospital, Boston, MA. Preliminary data from the study confirmed a promise for this agent to elicit considerably lesser severity of histamine release than that observed with its immediate predecessor clinically tested agents, BW785U77 and BWA444U, which were discontinued from further clinical development. Mivacurium did not exhibit the ultra-short duration of action seen with BW785U; whereas, BW A444U produced an intermediate duration of action. Mivacurium is a biodegradable neuromuscular blocking agent owing to its degradation by plasma cholinesterases - the esterases rapidly hydrolyze one ester moiety initially resulting in a two mono-quaternary metabolites of which one still has an intact ester moiety.
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In the less common type, such as the Bacillus subtilis sporulation factor Spo0B or the Caulobacter crescentus protein ChpT, the bundle is assembled as a protein dimer, with similarity to the structure of histidine kinases. Monomeric HPt domains possess only one phosphorylatable histidine residue and interact with one response regulator, whereas dimers have two phosphorylation sites and can interact with two response regulators at the same time. Monomeric HPt domains have no enzymatic activity of their own and act purely as phosphate shuttles, while the dimeric Spo0B is catalytic; its phosphotransfer rate to the recipient response regulator is dramatically accelerated compared to histidine phosphate. Despite possessing a second domain with some similarity to ATPase domains, dimeric HPt proteins have not been shown to bind or hydrolyze ATP and lack key residues present in other ATPases.
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Acid halides hydrolyze in the presence of water to produce carboxylic acids, but this type of reaction is rarely useful, since carboxylic acids are typically used to synthesize acid halides. Most reactions with acid halides are carried out in the presence of a non-nucleophilic base, such as pyridine, to neutralize the hydrohalic acid that is formed as a byproduct. Acid halides will react with carbon nucleophiles, such as Grignards and enolates, though mixtures of products can result. While a carbon nucleophile will react with the acid halide first to produce a ketone, the ketone is also susceptible to nucleophilic attack, and can be converted to a tertiary alcohol. For example, when benzoyl chloride (1) is treated with two equivalents of a Grignard reagent, such as methyl magnesium bromide (MeMgBr), 2-phenyl-2-propanol (3) is obtained in excellent yield.
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Another attempt was made by Wiechert, who treated HF with dichromate, yielding impure liquid CrO2F2 at −40 °C. Engelbrecht and von Grosse's synthesis of CrO2F2, and most successive syntheses, involve treating chromium trioxide with a fluorinating agent: :CrO3 \+ 2 HF → CrO2F2 \+ H2O The reaction is reversible, as water will readily hydrolyze CrO2F2 back to CrO3. The approach published by Georg Brauer in the Handbook of Preparative Inorganic Chemistry drew on von Wartenberg's approach of direct fluoridation: :CrO2Cl2 \+ F2 → CrO2F2 \+ Cl2 Other methods include treatment with chlorine fluoride, carbonyl fluoride, or some metal hexafluorides: :CrO3 \+ 2 ClF → CrO2F2 \+ Cl2 \+ O2 :CrO3 \+ COF2 → CrO2F2 \+ CO2 :CrO3 \+ MF6 → CrO2F2 \+ MOF4 (M = Mo, W) The last method involving the fluorides of tungsten and molybdenum are reported by Green and Gard to be very simple and effective routes to large quantities of pure CrO2F2.
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Many general purpose vectors such as pUC19 usually include a system for detecting the presence of a cloned DNA fragment, based on the loss of an easily scored phenotype. The most widely used is the gene coding for E. coli β-galactosidase, whose activity can easily be detected by the ability of the enzyme it encodes to hydrolyze the soluble, colourless substrate X-gal (5-bromo-4-chloro-3-indolyl-beta-d-galactoside) into an insoluble, blue product (5,5'-dibromo-4,4'-dichloro indigo). Cloning a fragment of DNA within the vector-based lacZα sequence of the β-galactosidase prevents the production of an active enzyme. If X-gal is included in the selective agar plates, transformant colonies are generally blue in the case of a vector with no inserted DNA and white in the case of a vector containing a fragment of cloned DNA.
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Carbapenemases can be broadly divided into two different categories based on the mechanism they use to hydrolyze the lactam ring in their substrates: Metallo-β-lactamases contain bound zinc ions in their active sites and are therefore inhibited by chelating agents like EDTA, while serine carbapenemases feature an active site serine that participates in the hydrolysis of the substrate. Serine carbapenemase- catalyzed hydrolysis employs a three-step mechanism featuring acylation and deacylation steps analogous to the mechanism of protease-catalyzed peptide hydrolysis, proceeding through a tetrahedral transition state. Given their mechanism of action, the possibility of off-target effects brought about through inhibition of endogenous serine hydrolases is an obvious possible concern in the development of boronic acid β-lactamase inhibitors, and in fact boronic acids like bortezomib have previously been investigated or developed as inhibitors of various human proteases. Vaborbactam, however, is a highly specific β-lactamase inhibitor, with an IC50 >> 1 mM against all human serine hydrolases against which it has been tested.
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The problems with the acidic (aluminum sulfate-mediated) mass sizing of paper with alkaline-digested colophony resins introduced since the early 19th century led besides the use of alkaline flocculants (such as chalk or calcium carbonate as the alkali reserve) to the search for alternative materials for sizing in a neutral or alkaline environment. In addition to the significantly more reactive alkenylsuccinic anhydrides (which do also hydrolyze rapidly in the presence of water) alkylated ketene dimers have begun to be preferred surface and mass sizes in the paper industry from the 1960s onwards, beginning in the 1950s. Strukturformel von C18-Alkenylbernsteinsäureanhydrid (ASA) Industrially applied AKDs are derived from fatty acids with chain lengths between C14 (myristic acid) to C22 (behenic acid); palmityl (C16) diketene and stearyl (C18) ketene and mixtures thereof are preferably used, as well as fatty acid mixtures from the hydrolysis of animal and vegetable fats. Because of the chain length of the original fatty acids, AKD are waxy solids with melting points between 42 and about 70 °C.
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Iron(III) oxyhydroxide precipitates from solutions of iron(III) salts at pH between 6.5 and 8.Tim Grundl and Jim Delwiche (1993): "Kinetics of ferric oxyhydroxide precipitation". Journal of Contaminant Hydrology, volume 14, issue 1, pages 71-87. . Thus the oxyhydroxide can be obtained in the lab by reacting an iron(III) salt, such as ferric chloride or ferric nitrate, with sodium hydroxide:K. H. Gayer and Leo Woontner (1956): "The Solubility of Ferrous Hydroxide and Ferric Hydroxide in Acidic and Basic Media at 25°". Journal of Physical Chemistry, volume 60, issue 11, pages 1569–1571. : + 3 NaOH → + 3 NaCl : + 3 NaOH → + 3 In fact, when dissolved in water, pure will hydrolyze to some extent, yielding the oxyhydroxide and making the solution acidic: : + 2 ↔ + 3 Therefore, the compound can also be obtained by the decomposition of acidic solutions of iron(III) chloride held near the boiling point for days or weeks:Egon Matijević and Paul Scheiner (1978): "Ferric hydrous oxide sols: III. Preparation of uniform particles by hydrolysis of Fe(III)-chloride, -nitrate, and -perchlorate solutions". Journal of Colloid and Interface Science, volume 63, issue 3, pages 509-524.
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