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"catalyse" Definitions
  1. catalyse something to make a chemical reaction happen fasterTopics Physics and chemistryc2

369 Sentences With "catalyse"

How to use catalyse in a sentence? Find typical usage patterns (collocations)/phrases/context for "catalyse" and check conjugation/comparative form for "catalyse". Mastering all the usages of "catalyse" from sentence examples published by news publications.

But private-sector customers are themselves too fragmented to catalyse change.
One reason is to help catalyse Riyadh's development as a financial centre.
The furore will eventually subside, but justified public outrage should catalyse boardroom reform.
It's not going to beat poverty or catalyse some new form of romance.
That may be the point: a stern external force should help catalyse fiscal reforms.
Our five-year goal is to help catalyse large scale development in the Niger Delta.
"What the business growth fund will do is catalyse them," he added in an interview.
"This (ruling) might also catalyse the potential for the use of blockchain in diverse areas," Viswanathan added.
Nevertheless, advocates believe the instruments can help catalyse a broader shift to clean energy sources by financing projects.
PPA supporters believe the instruments can help catalyse a broader shift to clean energy sources by funding projects.
In other words, the problem with both Valentine's Day and ecstasy is that the lovey-dovey feelings they catalyse aren't exactly genuine.
Progress in America also helped catalyse the historic Paris climate agreement, which presents the best opportunity to save the planet for future generations.
But that should catalyse positive change, just as a spate of quality-control crises ought to force Japanese bosses to become more competitive.
"We want to catalyse the private sector, to be a partner with it — we want them to play the prime role," Hogail said.
His dark sonics and intimate vocal style went on to catalyse a string of well-received hits and collaborations with Massive Attack and Gorillaz.
Bank of England Deputy Governor for banking and markets Dave Ramsden said the change would "catalyse" transition to SONIA across a broad range of markets.
Dr Arnold, who studied mechanical and aerospace engineering as an undergraduate, won her half for making synthetic enzymes (proteins that catalyse chemical reactions) by "directed evolution".
Mr Luce is the founder of Texas 2036, a group that collects data to reveal Texas's relative position and catalyse a strategic plan for the state.
Life uses proteins called enzymes, which catalyse chemical reactions, to build all the other molecules it needs, with a different enzyme for each step of the construction.
" The strategists, writing in its 2018 global foreign exchange outlook released on Tuesday, said that comparatively the euro "remains cheap" and that "strong growth should catalyse appreciation.
A more radical possibility, at least in terms of chemistry, than remaking and improving natural compounds is to create enzymes to catalyse chemical reactions nature never carries out.
These, as in a natural metabolic pathway, consist of a series of enzymes (another type of specialised protein) that catalyse a sequence of chemical changes, gradually converting one molecule into another.
The locals are using a biotechnology that finds hydrocarbon at the molecular level and destroys its bioavailability, killing the oil, and leaving behind nutrients that catalyse the regrowth of the ecosystem.
These are aimed at the industry itself, but since our money is what makes the fashion world go round — it's us consumers that are going to have to catalyse this change.
Beyond that, it might provide scholarships to promising young politicians, nurture parliamentary links between like-minded MPs, deploy activists to favoured local campaigns or even, some reckon, catalyse a new political party.
But the interest in returning to the Moon that the prize sought to catalyse did not quickly materialise; faced with a dearth of likely winners, the XPRIZE Foundation was forced to push back its deadline again and again.
Another envisaged benefit for startups is "trust in the framework and recognition that promising, innovative digital businesses will be protected from foreclosure or exclusion" — which they argue "should catalyse investment in UK digital businesses, driving the sector's growth".
While nobody knows whether popular calls for action will catalyse the drastic lifestyle shifts that scientists say are needed to avert the worst loss of life, a growing number of people are taking whatever steps they can to create change.
While nobody can say whether the activists will catalyse the kind of transformational changes in energy, transport and farming that scientists say are needed to avert the worst loss of life from climate change, campaigners believe the moment is ripe to redefine the politically possible.
"Through this memorandum of intent (MOI), both parties aim to lower the access barriers for technology companies into the capital markets, catalyse more high-tech IPOs and increase Singapore's attractiveness as a venue for capital raising," SGX and the Infocomm Media Development Authority (IMDA) said in a joint statement on Wednesday.
Weeks after the Weinstein claims broke, I'm still writing news stories about men in music who are accused of abuse, assault, and cruelty, and the outpouring that has occurred since he was named is, certainly, what was needed to catalyse change in a culture that has never been properly confronted with its own pathology.
"Governments must ratify the Paris agreement swiftly and have a responsibility to implement policies that drive better disclosure of climate risk, curb fossil fuel subsidies and put in place strong pricing signals sufficient to catalyse the significant private sector investment in low carbon solutions," said Stephanie Pfeifer, chief executive at Institutional Investors Group on Climate Change.
These enzymes catalyse the interconversion of L- and D-proline in bacteria.
The alcohol dehydrogenases comprise a group of several isozymes that catalyse the oxidation of primary and secondary alcohols to aldehydes and ketones, respectively, and also can catalyse the reverse reaction. In mammals this is a redox (reduction/oxidation) reaction involving the coenzyme nicotinamide adenine dinucleotide (NAD+).
Deoxyribose is generated from ribose 5-phosphate by enzymes called ribonucleotide reductases. These enzymes catalyse the deoxygenation process.
The enolase superfamily is a superfamily of enzymes, members of which catalyse a range of reactions. The enolase superfamily includes enzymes that catalyse a wide variety of reactions and performing diverse roles in metabolism. However, the reactions catalysed share the common chemical step of abstraction of a proton from a carbon adjacent to a carboxylic acid and a requirement of a divalent metal ion. This diversity of functions is in contrast to many families of enzymes whose members catalyse similar chemical reactions on different substrates.
Technetium can catalyse the destruction of hydrazine by nitric acid, and this property is due to its multiplicity of valencies.
133-4 The case received much public and academic attention and probably helped catalyse further scientific developments in the field of forensics.
Various amines can be used to catalyse this process. It can be used as a sarin-simulant for the calibration of organophosphorus detectors.
As an example, one may consider proteases (enzymes that aid digestion by causing hydrolysis of peptide bonds in proteins). They catalyse the hydrolysis of interior peptide bonds in peptide chains, as opposed to exopeptidases (another class of enzymes, that catalyse the hydrolysis of terminal peptide bonds, liberating one free amino acid at a time). However, proteases do not catalyse the hydrolysis of all kinds of proteins. Their action is stereo-selective: Only proteins with a certain tertiary structure are targeted as some kind of orienting force is needed to place the amide group in the proper position for catalysis.
Organophosphines are important in catalysts where they complex (adhere) to various metal ions; complexes derived from a chiral phosphine can catalyse reactions to give chiral, enantioenriched products.
The family also contains L-lactate dehydrogenases that catalyse the conversion of L-lactate to pyruvate, the last step in anaerobic glycolysis. Malate dehydrogenases that catalyse the interconversion of malate to oxaloacetate and participate in the citric acid cycle, and L-2-hydroxyisocaproate dehydrogenases are also members of the family. The N-terminus is a Rossmann NAD-binding fold and the C-terminus is an unusual alpha+beta fold.
In recent years, several reagents such as Tris(2,2,2-trifluoroethyl)borate [B(OCH2CF3)3], pyrrolidine or titanium ethoxide [Ti(OEt)4] have been shown to catalyse imine formation.
To build an Intentional DiscipleMaking Church (IDMC) model so as to launch an IDMC movement to catalyse a multiplication of Intentional Disciplemaking Churches to fulfill the Great Commission Mandate.
Various amines can be used to catalyse this process. It reacts with hydrogen fluoride or sodium fluoride to produce methylphosphonyl difluoride, which is used in the production of sarin and soman nerve agents.
This tendency was found statistically significant. Theories point to a perceptual tool to catalyse contrast adaptation (slow, seconds) to contrast gain control (fast,≈100ms) at an early cortical or pre-cortical ‘neural locus’.
Methanogens, archaea, bacteria and some unicellular eukaryotes contain hydrogenase enzymes that catalyse metabolic reactions involving free hydrogen, whose active site is an iron atom with Fe–H bonds as well as other ligands.
For example, polyketide synthases are large enzymes that make antibiotics; they contain up to one hundred independent domains that each catalyse one step in the overall process, like a step in an assembly line.
This family includes glucosyltransferases or sucrose 6-glycosyl transferases (GTF-S) (CAZY GH_70) which catalyse the transfer of D-glucopyramnosyl units from sucrose onto acceptor molecules. Some members of this family contain a cell wall-binding repeat.
The glycosyl hydrolase 42 family CAZY GH_42 comprises beta- galactosidase enzymes (). These enzyme catalyse the hydrolysis of terminal, non-reducing terminal beta-D-galactoside residues. The middle domain of these three-domain enzymes is involved in trimerisation.
Glycoside hydrolase family 46 CAZY GH_46 comprises enzymes with only one known activity; chitosanase (). Chitosanase enzymes catalyse the endohydrolysis of beta-1,4-linkages between N-acetyl-D-glucosamine and D-glucosamine residues in a partly acetylated chitosan.
Khandker, Shahidur R., Fighting Poverty with Microcredit: Experience in Bangladesh, Bangladesh Edition, The University Press Ltd., Dhaka, 1999, pp. 17–18 Both Yunus and Abed also attempted to catalyse collective enterprises that were locally owned and controlled.
An attP site on the phage exchanges segments with an attB site on the bacterial DNA. Thus, these are site-specific, occurring only at the respective att sites. The integrase class of enzymes catalyse this particular reaction.
Optimizing data models, size and processing path/time are ongoing work. As more data is captured at different data stages in not only EIS apps but also other enterprise apps, audio and video tagging can catalyse data discovery.
Formate dehydrogenases are a set of enzymes that catalyse the oxidation of formate to carbon dioxide, donating the electrons to a second substrate, such as NAD+ in formate:NAD+ oxidoreductase (EC 1.2.1.2) or to a cytochrome in formate:ferricytochrome-b1 oxidoreductase (EC 1.2.2.1).
Pseudomonas frederiksbergensis is a Gram-negative, phenanthrene-degrading bacterium from a coal gasification site in Frederiksberg, Copenhagen, Denmark. It is able to catalyse the asymmetric oxidation of sulfides to give exclusively the R enantiomer. The type strain is DSM 13022.
Fondation Botnar works with Unicef on the African Youth Digital Innovation Platform. The project aims to catalyse young people’s creativity and ideas on how to create economically viable business models and employment opportunities for young people across the African region.
7 Apr. 2010. Some cross coupling reaction are catalyzed by ferric fluoride-based compounds. Specifically the coupling of biaryl compounds are catalyzed by hydrated iron(II) fluoride complexes of N-heterocyclic carbene ligands. Other metal fluorides also catalyse similar reactions.
The domain is associated with the oxidoreductase family and acts on NADH or NADPH, using a heme protein as an electron acceptor. Requires FAD and FMN as cofactors to catalyse the reaction: NADPH + H+ + n oxidised hemoprotein = NADP+ + n reduced hemoprotein.
Resource developed by InterNICHE to catalyse change comprise the multi-language book From Guinea Pig to Computer Mouse (2003), several Alternative Loan Systems, the Humane Education Award, the information-rich website www.interniche.org, conferences, outreach visits and training around the world.
Nevertheless, it was able to catalyse only a polymerization of a chain having the size of about 14 nucleotides, even though it was 200 nucleotides long. The most up-to-date version of this polymerase was shown in 2013. While it has an ability to catalyse polymerization of longer sequences, even of its own length, it cannot replicate itself due to a lack of sequence generality and its inability to transverse secondary structures of long RNA templates. However, it was recently shown that those limitations could in principle be overcome by the assembly of active polymerase ribozymes from several short RNA strands.
Site-specific recombination makes use of phage integrases instead of restriction enzymes, eliminating the need for having restriction sites in the DNA fragments. Instead, integrases make use of unique attachment (att) sites, and catalyse DNA rearrangement between the target fragment and the destination vector. The Invitrogen Gateway cloning system was invented in the late 1990s and uses two proprietary enzyme mixtures, BP clonase and LR clonase. The BP clonase mix catalyses the recombination between attB and attP sites, generating hybrid attL and attR sites, while the LR clonase mix catalyse the recombination of attL and attR sites to give attB and attP sites.
Clearly, MPs are using MPLADS as political mileage to be gained during elections. Yearly expenditure, % utilisation of funds over sanctioned and % completed work over sanctioned increases during the last year of the Lok Sabha term. Non-lapsable funds also catalyse this behaviour.
Isobutyraldehyde is produced industrially by the hydroformylation of propene. Several million tons are produced annually.Boy Cornils, Richard W. Fischer, Christian Kohlpaintner "Butanals" in Ullmann's Encyclopedia of Industrial Chemistry, 2000, Wiley-VCH, Weinheim. Strong mineral acids catalyse the rearrangement of methallyl alcohol to isobutyraldehyde.
A sample of copper(I) oxide. Copper forms a rich variety of compounds, usually with oxidation states +1 and +2, which are often called cuprous and cupric, respectively. Copper compounds, whether organic complexes or organometallics, promote or catalyse numerous chemical and biological processes.
A second hypothesis involves the methylation of genes in vascular cells by folic acid and vitamin B12, which may also accelerate plaque growth. Finally, altered methylation may catalyse l-arginine to asymmetric dimethylarginine, which is known to increase the risk of vascular disease.
Catalyse consists of Bhumi’s civic projects that engage volunteers in causes like animal welfare, community welfare, disability, environment, health etc. The programmes consisting of one-off and regular volunteering activities engage over 5,000 volunteers each year in over 15 cities across India.
Glycosyl hydrolase family 63 (CAZY GH_63) is a family of eukaryotic enzymes. They catalyse the specific cleavage of the non-reducing terminal glucose residue from Glc(3)Man(9)GlcNAc(2). Mannosyl oligosaccharide glucosidase is the first enzyme in the N-linked oligosaccharide processing pathway.
Ribosomal L28e protein family is a family of evolutionarily related proteins. Members include 60S ribosomal protein L28. Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding.
C. Elschenbroich, Organometallics (2006) Wiley and Sons- VCH: Weinheim. Cis-dichlorobis(diethyl sulfide)platinum(II) and Karstedt’s catalyst (adduct of divinyltetramethyldisiloxane and chloroplatinic acid) also catalyse hydrosilylation. Many metallodendrimers have repeating units based on organoplatinum compounds. Idealized mechanism for metal-catalysed hydrosilylation of an alkene.
Aldehyde dehydrogenases () are a group of enzymes that catalyse the oxidation of aldehydes. They convert aldehydes (R-C(=O)) to carboxylic acids (R-C(=O)). The oxygen comes from a water molecule. To date, nineteen ALDH genes have been identified within the human genome.
Distinct from plasma kallikrein, tissue kallikreins (KLKs) are expressed throughout the human body and perform various physiological roles. As some kallikreins are able to catalyse the activation of other kallikreins, several cascades involving these proteases have been implicated in the regulation of homeostatic functions.
London: Centaur Publishing, 2005, Vol. 25, Issue 1, p. 18. is a French public artist, stimulating debate in public space to catalyse social change. Firrell uses language to engage directly with the public, provoking dialogue, usually about aspects of marginalisation, equality and equitable social organisation.
NTPDase1 is an ectonucleotidase that catalyse the hydrolysis of γ- and β-phosphate residues of triphospho- and diphosphonucleosides to the monophosphonucleoside derivative. NTPDase1 hydrolyzes P2 receptor ligands, namely ATP, ADP, UTP and UDP with similar efficacy. NTPDase1 can therefore effect P2 receptor activation and functions.
Chitin-related genes (deacetylases) are thought to play an important part in the expression/development of these morphological defenses in Daphnia. Chitin-modifying enzymes (chitin deacetylases) have been shown to catalyse the N-deacetylation of chitin to influence the protein-binding affinity of these chitin filaments.
Linalool dehydratase (, linalool hydro-lyase (myrcene-forming)) is an enzyme with systematic name (3S)-linalool hydro-lyase (myrcene-forming). This enzyme catalyses the following chemical reaction : (3S)-linalool \rightleftharpoons myrcene + H2O In absence of oxygen this enzyme can also catalyse the isomerization of (3S)-linalool to geraniol.
Many αKG-dependent dioxygenase also catalyse uncoupled turnover, in which oxidative decarboxylation of αKG into succinate and carbon dioxide proceeds in the absence of substrate. The catalytic activity of many αKG-dependent dioxygenases are dependent on reducing agents (especially ascorbate) although the exact roles are not understood.
For heterogeneous catalysts, the stereoregularity is determined by the surface structure around the active site on the catalyst particle, and can be influenced by additives such as succinates or phthalates, which tend to block specific sites, while leaving others (with different stereoreactivity) to catalyse the polymerization.
For example, many FLPs split hydrogen molecules. Thus, a mixture of tricyclohexylphosphine (PCy3) and tris(pentafluorophenyl)borane reacts with hydrogen to give the respective phosphonium and borate ions: :PCy3 + B(C6F5)3 + H2 -> [HPCy3]+ [HB(C6F5)3]- This reactivity has been exploited to produce FLPs which catalyse hydrogenation reactions.
The B Team is a global nonprofit initiative co-founded by Sir Richard Branson and Jochen Zeitz that brings together a group of global leaders from business, civil society and government to catalyse a better way of doing business, that prioritises the wellbeing of people and the planet.
Flavin adenine dinucleotide in its oxidized form, FAD is a cofactor of flavoprotein oxidoreductase enzymes. Flavoprotein pyridine nucleotide cytochrome reductases, including FAD catalyse the interchange of reducing equivalents (H+ or electrons). Initial electron donors and final electron acceptors comprise single electron carriers and two electron carrying nicotinamide dinucleotides respectively.
Most alkenes are prochiral, meaning in this context that their hydrocyanation generates chiral nitriles. Conventional hydrocyanation catalysts, e.g. Ni(P(OR)3)4, catalyse the formation of racemic mixtures, consisting of equal amounts of the two enantiomeric nitriles. When however the supporting ligands are chiral, the hydrocyanation can be highly enantioselective.
Pentalenolactone synthase (, Formerly , penM (gene), pntM (gene)) is an enzyme with systematic name pentalenolactone-F:oxidized-ferredoxin oxidoreductase (pentalenolactone forming). This enzyme catalyse the following chemical reaction : pentalenolactone F + oxidized ferredoxin \rightleftharpoons pentalenolactone + reduced ferredoxin This is heme-thiolate protein (P-450), which is isolated from the bacteria Streptomyces exfoliatus and Streptomyces arenae.
The Office also provides partnership advisory and outreach services in response to demand from the United Nations system, governments and non-State actors to catalyse public-private partnerships through high-impact events and advice to potential partners regarding opportunities and good practices to promote the Sustainable Development Goals as a framework for action.
She is also launching an app called "Phree" for the safety of women. The app is due to be launched in August 2016. Madhureeta has a column "The Big M" on India Today's website DailyO. She has launched with ActionAid India - "Two Way Street" an initiative to catalyse media for social change.
This protein is made up of two identical polypeptide chains, totaling 372 residues. The biological function of branched-chain amino acid aminotransferases is to catalyse the synthesis or degradation of the branched chain amino acids leucine, isoleucine, and valine. In humans, branched chain amino acids are essential and are degraded by BCATs.
Na+/H+ antiporter A (NhaA) family (TC# 2.A.33) contains a number of bacterial sodium-proton antiporter (SPAP) proteins. These are integral membrane proteins that catalyse the exchange of H+ for Na+ in a manner that is highly pH dependent. Homologues have been sequenced from a number of bacteria and archaea.
Malonyl CoA reductase (malonate semialdehyde-forming) (, NADP-dependent malonyl CoA reductase, malonyl CoA reductase (NADP)) is an enzyme with systematic name malonate semialdehyde:NADP+ oxidoreductase (malonate semialdehyde-forming). This enzyme catalyse the following chemical reaction : malonate semialdehyde + CoA + NADP+ \rightleftharpoons malonyl-CoA + NADPH + H+ Requires Mg2+. Catalyses the reduction of malonyl-CoA to malonate semialdehyde.
Cyclohexadienes, many derived from Birch reduction of aromatic compounds, form derivatives (diene)Fe(CO)3. The affinity of the Fe(CO)3 unit for conjugated dienes is manifested in the ability of iron carbonyls catalyse the isomerisations of 1,5-cyclooctadiene to 1,3-cyclooctadiene. Cyclohexadiene complexes undergo hydride abstraction to give cyclohexadienyl cations, which add nucleophiles.
Deamination is the removal of an amino group from a molecule. Enzymes that catalyse this reaction are called deaminases. In the human body, deamination takes place primarily in the liver, however it can also occur in the kidney. In situations of excess protein intake, deamination is used to break down amino acids for energy.
In molecular biology, the red chlorophyll catabolite reductase (RCC reductase) family of proteins consists of several red chlorophyll catabolite reductase (RCC reductase) proteins. Red chlorophyll catabolite (RCC) reductase (RCCR) and pheophorbide (Pheide) a oxygenase (PaO) catalyse the key reaction of chlorophyll catabolism, porphyrin macrocycle cleavage of Pheide a to a primary fluorescent catabolite (pFCC).
Proceedings of the National Academy of Sciences. 2007 Oct 23;104(43):17004-9. For example, enzymes can sometimes catalyse more than just one reaction, even though they usually are optimised for catalysing just one reaction. Such promiscuous protein functions, if they provide an advantage to the host organism, can then be amplified with additional copies of the gene.
The Speak! programme is hosted at Man Kiu College and is a program focusing on current-events, international relations as well as domestic affairs. Students participate in and contribute to multiple round table discussions. By having talking about and carefully evaluating social issues and current affairs, students will improve their speaking skills and catalyse their English abilities.
Once this initial sugar has been added, other glycosyltransferases can catalyse the addition of additional sugars. Two of the most common structures formed are Core 1 and Core 2. Core 1 is formed by the addition of a galactose sugar onto the initial GalNAc. Core 2 consists of a Core 1 structure with an additional N-acetylglucosamine (GlcNAc) sugar.
3,5,7-Trioxododecanoyl-CoA synthase (, TKS) is an enzyme with systematic name malonyl-CoA:hexanoyl-CoA malonyltransferase (3,5,7-trioxododecanoyl-CoA- forming). This enzyme catalyses the following chemical reaction : 3 malonyl- CoA + hexanoyl-CoA \rightleftharpoons 3 CoA + 3,5,7-trioxododecanoyl-CoA + 3 CO2 This polyketide synthase catalyse the first step in the cannabinoids biosynthetic pathway of the plant Cannabis sativa.
Synzymes are substances with catalytic capabilities. The name synzyme is derived from synthetic enzyme. Current synzymes consist mainly of organic molecules tailored in such a way that they catalyse certain kinds of reactions. Like enzymes, they bind a transition state of a substrate in an active site, and like enzymes they generally obey Michaelis-Menten kinetics.
Enzymes involved in metabolic pathways within the body such as cellular respiration fail to work effectively at higher temperatures, and further increases can lead them to denature, reducing their ability to catalyse essential chemical reactions. This loss of enzymatic control affects the functioning of major organs with high energy demands such as the heart and brain.
There are two different forms of the spliceosome, the major and minor forms. The ncRNA components of the major spliceosome are U1, U2, U4, U5, and U6. The ncRNA components of the minor spliceosome are U11, U12, U5, U4atac and U6atac. Another group of introns can catalyse their own removal from host transcripts; these are called self-splicing RNAs.
The VPg protein interacts with eukaryotic initiation factor 4E (eIF4E). This interaction appears to be essential to viral infectivity. Two proteinases, P1 and the helper component proteinase (HC) catalyse only autoproteolytic reactions at their respective C termini. The remaining cleavage reactions are catalysed by either trans-proteolytic or autoproteolytic mechanisms by the small nuclear inclusion protein (NIa-Pro).
Prof Schofield is currently working on the design and synthesis of enzyme inhibitors for the metallo β-lactamases – there are no clinically used inhibitor of these enzymes but they pose a significant threat as they catalyse the hydrolysis of almost all clinically used β-lactam antibiotics. A particular interest involves human metallo β-lactamases which share the same fold.
Acid secretion by the human stomach results in a median diurnal pH of 1.4. This very large (>106-fold) H+ gradient is generated by the gastric H+/K+ ATPase which is an ATP-driven proton pump. Hydrolysis of one ATP molecule is used to catalyse the electroneutral exchange of two luminal potassium ions for two cytoplasmic protons through the gastric membrane.
The Global Poverty Project is an international education and advocacy organisation working to catalyse the movement to end extreme poverty. The Project was founded by Hugh Evans and Simon Moss and aims to increase the number and effectiveness of people taking action to end extreme poverty.Australia to launch global anti-poverty campaign , West Australian, May 18, 2009.Obeng-Odoom, Franklin 2010.
Nitrilase enzymes (nitrile aminohydrolase; ) catalyse the hydrolysis of nitriles to carboxylic acids and ammonia, without the formation of "free" amide intermediates. Nitrilases are involved in natural product biosynthesis and post translational modifications in plants, animals, fungi and certain prokaryotes. Nitrilases can also be used as catalysts in preparative organic chemistry. Among others, nitrilases have been used for the resolution of racemic mixtures.
Michaelis–Menten equation describes how this slope varies with the concentration of substrate. Enzyme assays are laboratory procedures that measure the rate of enzyme reactions. Since enzymes are not consumed by the reactions they catalyse, enzyme assays usually follow changes in the concentration of either substrates or products to measure the rate of reaction. There are many methods of measurement.
Lewis acids are also used to catalyse many C-N bond-forming reactions. Pyridine compounds are common in biology and have many applications. Normally, pyridine is synthesized from acetaldehyde, formaldehyde and ammonia under high temperatures and pressures. Lanthanide triflates can be used to synthesize pyridine by catalysing either the condensation of aldehydes and amines, or the aza Diels-Alder reaction catalytic synthesis.
The centre is dedicated to provide infrastructural facilities and a coordinated multidisciplinary team to work at the frontiers of neuroscience research and network the existing groups and whenever required, create satellite units to catalyse the overall growth of this discipline in the country. Till date, these are the Director or Director-In charge Prof. Vijayalakshmi Ravindranath Prof. Prasun K Roy Prof.
Enzymes must bind their substrates before they can catalyse any chemical reaction. Enzymes are usually very specific as to what substrates they bind and then the chemical reaction catalysed. Specificity is achieved by binding pockets with complementary shape, charge and hydrophilic/hydrophobic characteristics to the substrates. Enzymes can therefore distinguish between very similar substrate molecules to be chemoselective, regioselective and stereospecific.
All classes of adenylyl cyclase catalyse the conversion of adenosine triphosphate (ATP) to 3',5'-cyclic AMP (cAMP) and pyrophosphate. Magnesium ions are generally required and appear to be closely involved in the enzymatic mechanism. The cAMP produced by AC then serves as a regulatory signal via specific cAMP-binding proteins, either transcription factors, enzymes (e.g., cAMP-dependent kinases), or ion transporters.
Ribonucleoprotein (RNP) particles called ribosomes are the 'factories' where translation takes place in the cell. The ribosome consists of more than 60% ribosomal RNA; these are made up of 3 ncRNAs in prokaryotes and 4 ncRNAs in eukaryotes. Ribosomal RNAs catalyse the translation of nucleotide sequences to protein. Another set of ncRNAs, Transfer RNAs, form an 'adaptor molecule' between mRNA and protein.
Lord Genghis Khan, in Ordos City. A cult of Genghis Khan had existed until the 1930s, centered on a shrine which preserved mystical relics of Genghis, that was located in the Ordos Loop of Inner Mongolia.Bawden, 2013. The Japanese, during the occupation of China, tried to take possession of the relics in order to catalyse a pro-Japanese Mongol nationalism, but they failed.
In biochemistry, isozymes (or isoenzymes) are isoforms (closely related variants) of enzymes. In many cases, they are coded for by homologous genes that have diverged over time. Although, strictly speaking, allozymes represent enzymes from different alleles of the same gene, and isozymes represent enzymes from different genes that process or catalyse the same reaction, the two words are usually used interchangeably.
Since all steps in the catalytic cycle are considered reversible, it is possible for some of these other pathways to intersect with RCM depending on the reaction conditions and substrates. In 1971, Chauvin proposed the formation of a metallacyclobutane intermediate through a [2+2] cycloadditionHerisson, J-L.; Chauvin, Y. (1971). “Catalyse de transformation des olefines par les complexes du tungsten”.
Rhodococcus rhodochrous is a bacterium used as a soil inoculant in agriculture and horticulture. It is gram positive, in the shape of rods/cocci, oxidase negative, and catalase positive. It is industrially produced to catalyse acrylonitrile conversion to acrylamide. A 2015 study showed that Rhodococcus rhodochrous could inhibit the growth of Pseudogymnoascus destructans, the fungal species responsible for white nose syndrome in bats.
The Catalytic Fund of the Cities Alliance is a fund for small grants ($50,000 to $200,000), intended to "catalyse urban transformation processes that promote inclusive cities" and advance collective knowledge "through learning distilled from project experiences" and are issued along selected themes. The themes in question vary, but in years past, they have included "Know Your City" and "Youth and the City".
RhlA was subsequently shown to be involved in the production of the precursor to RHLs, HAAs. RhlB adds a rhamnose group to the HAA precursor to form mono-rhamnolipid. Therefore, the products of the rhlAB operon; RhlA and RhlB, catalyse the formation of HAAs and mono-rhamnolipids respectively. RhlA is an α, β hydrolase (analysis by Fugue structural prediction programme).
Ketosamine-3-kinases (KT3K) catalyse the phosphorylation of the ketosamine moiety of glycated proteins. The instability of a phosphorylated ketosamine leads to its degradation, and KT3K is thus thought to be involved in protein repair. The function of the prokaryotic members of this group has not been established. However, several lines of evidence indicate that they may function as fructosamine-3-kinases (FN3K).
This enables side-on addition of an ethylene unit and a polymer chain can grow by migratory insertion. Chromium compounds also catalyse the trimerization of ethylene to produce the monomer 1-hexene.John T. Dixon, Mike J. Green, Fiona M. Hess, David H. Morgan “Advances in selective ethylene trimerisation – a critical overview” Journal of Organometallic Chemistry 2004, Volume 689, Pages 3641-3668.
It is unclear how phenacetin induces injury to the kidney. Bach and Hardy have proposed that phenacetin's metabolites lead to lipid peroxidation that damages cells of the kidney. Paracetamol is the major metabolite of phenacetin and may contribute to kidney injury through a specific mechanism. In cells of the kidney, cyclooxygenases catalyse the conversion of paracetamol into N-acetyl- p-benzoquinoneimine (NAPQI).
The first step in immunoperoxidase staining is the binding of the specific (primary) antibody to the cell or tissue sample. The detection of the primary antibody can be then accomplished directly (example 1) or indirectly (examples 2 & 3). :Example 1. The primary antibody can be directly tagged with the enzyme peroxidase which is then used to catalyse a chemical reaction to generate a coloured product.
In molecular biology, XhoI is a type II restriction enzyme EC that recognise the double-stranded DNA sequence CTCGAG and cleaves after C-1. Type II restriction endonucleases (EC) are components of prokaryotic DNA restriction- modification mechanisms that protect the organism against invading foreign DNA. These site-specific deoxyribonucleases catalyse the endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Diphenylborinic acid was discovered in 1894 by Michaelis who produced it by hydrolysing the chloride. Letsinger determined its properties in 1955. Diphenylborinic acid has an extra high affinity for catechols compared with carbohydrates Diphenylborinic acid can catalyse the condensation of pyruvic acids with aldehydes to yield substituted isotetronic acid. Diphenylborinic acid is an inhibitor of several enzymes such as α-chymotrypsin, subtilisin BPN' and trypsin.
TRNA (guanine10-N2)-methyltransferase (, (m2G10) methyltransferase, Trm11-Trm112 complex) is an enzyme with systematic name S-adenosyl-L- methionine:tRNA (guanine10-N2)-methyltransferase. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + guanine10 in tRNA \rightleftharpoons S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA tRNA (guanine10-N2)-methyltransferase from yeast does not catalyse the methylation from N2-methylguanine10 to N2-dimethylguanine10 in tRNA.
Gold has been shown to be effective in low-temperature CO oxidation and acetylene hydrochlorination to vinyl chlorides. The exact nature of the catalytic site in this type of process is debated. The notion that gold can catalyse a reaction does not imply it is the only way. However, other metals can do the same job inexpensively, notably in recent years iron (see organoiron chemistry).
Proteins are polymers of amino acids, and they do all sorts of incredible things. They give structure to living things, carry messages and molecules around our bodies, support the immune system and catalyse chemical reactions, and they are used widely in industry and medicine too. In this issue, we explore proteins and discover how they are involved in all kinds of processes in humans and other organisms.
This is also known as kinetic perfection or catalytic perfection. Since the rate of catalysis of such enzymes is set by the diffusion-controlled reaction, it therefore represents an intrinsic, physical constraint on evolution (a maximum peak height in the fitness landscape). Diffusion limited perfect enzymes are very rare. Most enzymes catalyse their reactions to a rate that is 1,000-10,000 times slower than this limit.
In molecular biology, the protein domain SATase is short for Serine acetyltransferase and refers to an enzyme that catalyses the conversion of L-serine to L-cysteine in E. coli. More specifically, its role is to catalyse the activation of L-serine by acetyl-CoA.This entry refers to the N-terminus of the protein which has a sequence that is conserved in plants and bacteria.
Each of these proteins is a zinc-dependent enzyme, binding 3 zinc ions per molecule. The enzymes catalyse the conversion of phosphatidylcholine and water to 1,2-diacylglycerol and choline phosphate. In Bacillus cereus, there are nine residues known to be involved in binding the zinc ions: 5 His, 2 Asp, 1 Glu and 1 Trp. These residues are all conserved in the Clostridium alpha-toxin.
The Shibasaki group produced the first chiral lanthanide- binaphtholate complex in 1992, which was used to catalyse nitroaldol reactions. The complex was not characterised but was the first to perform the reaction enantioselectively. This success led to further research which resulted in the development of heterometallic complexes with the formula [Ln(binol)3(M)3], the structure of which was elucidated by X-ray crystallography.
Enzymes in a variety of biological systems may also catalyse the decomposition of hydrogen peroxide. Luminol reacts with the hydroxide ion, forming a dianion. The oxygen produced from the hydrogen peroxide then reacts with the luminol dianion. The product of this reaction, an organic peroxide, is very unstable and immediately decomposes with the loss of nitrogen to produce 5-aminophthalic acid with electrons in an excited state.
PEPPSI: Instructions for Use, Sigma- Aldrich Suzuki coupling (a) and Buchwald-Hartwig reaction (b) can be activated by PEPPSI complexes. An efficient, cationic palladium catalyst of iPEPPSI (internal PEPPSI) type was demonstrated to efficiently catalyse the copper- free Sonogashira reaction in water as the only solvent, under aerobic conditions, in the absence of copper, amines, phosphines and other additives. Sonogashira coupling under green reaction conditions using iPEPPSI.
A small steady stream of sulfuric acid is added to catalyse the cleavage reaction. In this reaction the CHP splits open and rearranges itself into two molecules; one each of phenol and acetone. Since the reaction is very unstable the Cleavage Reactor operated under strict temperature and acidity control with a high level of acetone reflux. The reactor was also equipped with emergency firewater injection.
Since many distinct tissue types express the IGF-1 receptor, IGF-1's effects are diverse. It acts as a neurotrophic factor, inducing the survival of neurons. It may catalyse skeletal muscle hypertrophy, by inducing protein synthesis, and by blocking muscle atrophy. It is protective for cartilage cells, and is associated with activation of osteocytes, and thus may be an anabolic factor for bone.
Not all cells carry out cell cycle withdrawal. In some cells, such as germ cells, stem cells and white blood cells, the withdrawal process do not occur. This is to ensure that these cells continue dividing for body growth or reproduction. Such phenomena is brought about by the presence of telomerase, which would catalyse the reaction of adding nucleotide sequences to the ends of telomeres.
In enzymology, a cadmium-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O \rightleftharpoons ADP + phosphate Thus, the two substrates of this enzyme are ATP and H2O, whereas its two products are ADP and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (heavy-metal-exporting).
The Stone Family Foundation (or the Stone Foundation) is one of the largest international grant makers in the United Kingdom. It aims to supports innovative, entrepreneurial and sustainable approaches to major social problems. The foundation's main focus has been on water, sanitation and hygiene (WASH). Its goal is to help catalyse lasting and effective solutions to the lack of adequate sanitation, safe water and good hygiene across the world.
When in the GA- GID1-DELLA complex, it is thought that DELLA proteins undergo changes in structure that enable their binding to F-box proteins (SLY1 in Arabidopsis or GID2 in rice). F-box proteins catalyse the addition of ubiquitin to their targets. The addition of ubiquitin to DELLA proteins promotes their degradation via the 26S-proteosome. The degradation of DELLA proteins releases cells from their repressive effects.
In biochemistry, the process of breaking down large molecules by splitting their internal bonds is catabolism. Enzymes which catalyse bond cleavage are known as lyases, unless they operate by hydrolysis or oxidoreduction, in which case they are known as hydrolases and oxidoreductases respectively. In proteomics, cleaving agents are used in proteome analysis where proteins are cleaved into smaller peptide fragments. Examples of cleaving agents used are cyanogen bromide, pepsin, and trypsin.
In enzymology, a protein-secreting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O \rightleftharpoons ADP + phosphate Thus, the two substrates of this enzyme are ATP and H2O, whereas its two products are ADP and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (protein-secreting).
For PDI to catalyse the formation of disulfide bonds in unfolded proteins, it must be reoxidized. This is carried out by an ER membrane-associated protein, Ero1p, which is no homolog of DsbB. This Ero1p protein forms a mixed disulfide with PDI, which is resolved by a nucleophilic attack of the second cystein residue in one of the active sites of PDI. As result, oxidized PDI is obtained.
The biosynthesis of disaccharides, oligosaccharides and polysaccharides involves the action of hundreds of different glycosyltransferases. These enzymes catalyse the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. A classification of glycosyltransferases using nucleotide diphospho-sugar, nucleotide monophospho-sugar and sugar phosphates () and related proteins into distinct sequence based families has been described. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site.
This converts the serpin from a stressed state, to a lower-energy relaxed state (S to R transition). Serine and cysteine proteases catalyse peptide bond cleavage by a two-step process. Initially, the catalytic residue of the active site triad performs a nucleophilic attack on the peptide bond of the substrate. This releases the new N-terminus and forms a covalent ester- bond between the enzyme and the substrate.
Homologues are sometimes known to display promiscuity towards each other's main reactions. This crosswise promiscuity has been most studied with members of the alkaline phosphatase superfamily, which catalyse hydrolytic reaction on the sulfate, phosphonate, monophosphate, diphosphate or triphosphate ester bond of several compounds. Despite the divergence the homologues have a varying degree of reciprocal promiscuity: the differences in promiscuity are due to mechanisms involved, particularly the intermediate required.
Alpha-ketoglutarate-dependent hydroxylases are non-heme, iron-containing enzymes that consume oxygen and alpha-ketoglutarate (αKG, also known as 2-oxoglutarate, or 2OG) as co-substrates. They catalyse a wide range of oxygenation reactions. These include hydroxylation reactions, demethylations, ring expansions, ring closures and desaturations. Functionally, the αKG- dependent hydroxylases are comparable to cytochrome P450 enzymes, which use oxygen and reducing equivalents to oxygenate substrates concomitant with formation of water.
In molecular biology, tRNA-dihydrouridine synthase is a family of enzymes which catalyse the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA.
This enzyme participates in porphyrin and chlorophyll metabolism. Cytochrome c haem-lyase (CCHL) and cytochrome Cc1 haem-lyase (CC1HL) are mitochondrial enzymes that catalyse the covalent attachment of a haem group on two cysteine residues of cytochrome c and c1. These two enzymes are functionally and evolutionary related. There are two conserved regions, the first is located in the central section and the second in the C-terminal section.
Ribosomes are the organelles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accordance with the genetic information. Incoming amino acid monomers enter the ribosomal A site in the form of aminoacyl-tRNAs complexed with elongation factor Tu (EF- Tu) and GTP.
In enzymology, an Ag+-exporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + Ag+in \rightleftharpoons ADP + phosphate + Ag+out The 3 substrates of this enzyme are ATP, H2O, and Ag+, whereas its 3 products are ADP, phosphate, and Ag+. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (Ag+-exporting).
In enzymology, a Cd2+-exporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + Cd2+in \rightleftharpoons ADP + phosphate + Cd2+out The 3 substrates of this enzyme are ATP, H2O, and Cd2+, whereas its 3 products are ADP, phosphate, and Cd2+. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (Cd2+-exporting).
To date, periplasmic, cytoplasmic, and cytoplasmic membrane-bound hydrogenases have been found. The [NiFe] hydrogenases, when isolated, are found to catalyse both H2 evolution and uptake, with low-potential multihaem cytochromes such as cytochrome c3 acting as either electron donors or acceptors, depending on their oxidation state. Generally speaking, however, [NiFe] hydrogenases are more active in oxidizing H2. A wide spectrum of H2 affinities have also been observed in H2-oxidizing hydrogenases.
In enzymology, a Na+-exporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + Na+ \rightleftharpoons ADP + phosphate + Na+ The 3 substrates of this enzyme are ATP, H2O, and Na+, whereas its 3 products are ADP, phosphate, and Na+. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (Na+-exporting).
In enzymology, a Na+-transporting two-sector ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O \rightleftharpoons ADP + phosphate Thus, the two substrates of this enzyme are ATP and H2O, whereas its two products are ADP and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (Na+-transporting).
In enzymology, a nickel-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + Ni2+out \rightleftharpoons ADP + phosphate + Ni2+in The 3 substrates of this enzyme are ATP, H2O, and Ni2+, whereas its 3 products are ADP, phosphate, and Ni2+. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (nickel-importing).
In enzymology, a lipopolysaccharide-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + lipopolysaccharidein \rightleftharpoons ADP + phosphate + lipopolysaccharideout The 3 substrates of this enzyme are ATP, H2O, and lipopolysaccharide, whereas its 3 products are ADP, phosphate, and lipopolysaccharide. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (lipopolysaccharide-exporting).
In enzymology, a nitrate-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + nitrateout \rightleftharpoons ADP + phosphate + nitratein The 3 substrates of this enzyme are ATP, H2O, and nitrate, whereas its 3 products are ADP, phosphate, and nitrate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (nitrate-importing).
In enzymology, a channel-conductance-controlling ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O \rightleftharpoons ADP + phosphate Thus, the two substrates of this enzyme are ATP and H2O, whereas its two products are ADP and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (channel-conductance-controlling).
In enzymology, a chloroplast protein-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O \rightleftharpoons ADP + phosphate Thus, the two substrates of this enzyme are ATP and H2O, whereas its two products are ADP and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (chloroplast protein-importing).
In enzymology, a guanine-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + guanineout \rightleftharpoons ADP + phosphate + guaninein The 3 substrates of this enzyme are ATP, H2O, and guanine, whereas its 3 products are ADP, phosphate, and guanine. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (guanine-importing).
In enzymology, an oligosaccharide-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + oligosaccharideout \rightleftharpoons ADP + phosphate + oligosaccharidein The 3 substrates of this enzyme are ATP, H2O, and oligosaccharide, whereas its 3 products are ADP, phosphate, and oligosaccharide. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (disaccharide-importing).
In enzymology, a taurine-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + taurineout \rightleftharpoons ADP + phosphate + taurinein The 3 substrates of this enzyme are ATP, H2O, and taurine, whereas its 3 products are ADP, phosphate, and taurine. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (taurine-importing).
In enzymology, a peptide-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + peptidein \rightleftharpoons ADP + phosphate + peptideout The 3 substrates of this enzyme are ATP, H2O, and peptide, whereas its 3 products are ADP, phosphate, and peptide. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (peptide-exporting).
In enzymology, a phosphonate-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + phosphonateout \rightleftharpoons ADP + phosphate + phosphonatein The 3 substrates of this enzyme are ATP, H2O, and phosphonate, whereas its 3 products are ADP, phosphate, and phosphonate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (phosphonate- transporting).
Aminoacyl-tRNA synthetases can catalyse editing reactions to correct errors produced during amino acid activation and tRNA esterification, in order to prevent the attachment of incorrect amino acids to tRNA. The B3/B4 domain of the beta subunit contains an editing site, which lies close to the active site on the alpha subunit. Disruption of this site abolished tRNA editing, a process that is essential for faithful translation of the genetic code.
The first reported example of asymmetric cation-binding catalysis originates from Cram and Sogah who in 1981 used a chiral crown ether in combination with a potassium base in an enantioselective Michael addition.Chiral crown complexes catalyse Michael addition reactions to give adducts in high optical yields Donald J. Cram and G. D. Y. Sogah J. Chem. Soc., Chem. Commun., 1981, 625-628 The development of chiral anionic catalysists is a more recent research field.
On 3 August 2008, the Highlands and Islands Council announced plans to modernise and catalyse industry in Helmsdale and its surrounding areas. This included a £3.5 million revamp of the harbour and the development of two battery processing factories. Work on the harbour was set to begin in spring 2009, while the battery plants were expected to open before May 2009. It was hoped up to 50 new jobs would be created.
At 120 °C, hydroxylammonium sulfate begins to decompose to sulfur trioxide, nitrous oxide, water, and ammonia: :2(NH3OH)2SO4 → 2SO3 \+ N2O + 2NH3 \+ 5H2O The reaction is exothermic above 138 °C, and is most exothermic at 177 °C.BASF hydroxylammonium sulfate product page Metals (especially copper, its alloys and its salts) catalyse the decomposition of hydroxylammonium sulfate. The instability of this compound is mainly due to the hydroxylammonium ion's weak nitrogen to oxygen single bond.
These enzymes catalyse sialyltransfer reactions during glycosylation, and are type II membrane proteins. There are about twenty different sialyltransferases which can be distinguished on the basis of the acceptor structure on which they act and on the type of sugar linkage they form. For example, a group of sialyltransferases adds sialic acid with an alpha-2,3 linkage to galactose, while other sialyltransferases add sialic acid with an alpha-2,6 linkage to galactose or N-acetylgalactosamine.
Sustain our Africa is an African based public advocacy organisation and forum focused on increasing awareness, facilitating and promoting sustainable development intuitives in Africa. The organisation's fundamental mission is to serve as a forum for the debate, discussion and dissemination of issues relating to sustainable development in an African context. Sustain our Africa hosts an annual sustainability summit in October and runs a media platform to facilitate dialogue, spread information, and catalyse change.
He is also the Founder of ‘Mission Samriddhi’, a social impact enterprise dedicated to holistic human development in India, through the design and development of projects that are sustainable and capable of scale to positively impact the larger population. Projects are currently supported in seven clusters including: Leadership Capacity Building, Farm-to-Fabric, Farm-to-Table, Scientific Agricultural Training, Education, Community Health and Grassroots Relief. The objectives of Mission Samriddhi are: Celebrate, Connect, Catalyse.
Grx2 is structurally similar to glutathione-S-transferases (GST), but there is no obvious sequence similarity. The inter-domain contacts are mainly hydrophobic, suggesting that the two domains are unlikely to be stable on their own. Both domains are needed for correct folding and activity of Grx2. It is thought that the primary function of Grx2 is to catalyse reversible glutathionylation of proteins with GSH in cellular redox regulation including the response to oxidative stress.
The best-known role of proteins in the cell is as enzymes, which catalyse chemical reactions. Enzymes are usually highly specific and accelerate only one or a few chemical reactions. Enzymes carry out most of the reactions involved in metabolism, as well as manipulating DNA in processes such as DNA replication, DNA repair, and transcription. Some enzymes act on other proteins to add or remove chemical groups in a process known as posttranslational modification.
The stabilisation of the diiron-oxo element required to catalyse the reaction has been of particular interest. Crystallographic studies suggest that the iron groups are held in place by the desaturase using aspartate and glutamate. A structure of aspartate-X-X-histidine was found to be a common motif in several plant species. This desaturase family can be further divided by the consensus motif used to hold the iron clusters in place.
Lipotropic compounds are those that help catalyse the breakdown of fat during metabolism in the body. Choline is the major lipotrope in mammals and other known lipotropes are important only insofar as they contribute to the synthesis of choline.(Barak, 1973) A lipotropic nutrient promotes or encourages the export of fat from the liver. Lipotropics are necessary for maintenance of a healthy liver, and for burning the exported fat for additional energy.
Catalases are enzymes that catalyse the conversion of hydrogen peroxide to water and oxygen, using either an iron or manganese cofactor. This protein is localized to peroxisomes in most eukaryotic cells. Catalase is an unusual enzyme since, although hydrogen peroxide is its only substrate, it follows a ping-pong mechanism. Here, its cofactor is oxidised by one molecule of hydrogen peroxide and then regenerated by transferring the bound oxygen to a second molecule of substrate.
It is used to catalyse the reduction of carbon monoxide to acetyl-CoA. Nickel superoxide dismutase (or Ni-SOD) from Streptomyces contains six nickel atoms. The nickel holding is done by a "nickel binding hook" which as the amino acid pattern H2N-His-Cys-X- X-Pro-Cys-Gly-X-Tyr-rest of protein, where the bold bits are ligands for the nickel atom. Nickel transporter proteins exist to move nickel atoms in the cell.
Multivesicular bodies are endosomal compartments that sort ubiquitinated membrane proteins by incorporating them into vesicles. This process involves the sequential action of three multiprotein complexes, ESCRT I to III (ESCRT standing for 'endosomal sorting complexes required for transport'). Vps4p is a AAA-type ATPase involved in this MVB sorting pathway. It had originally been identified as a ”class E” vps (vacuolar protein sorting) mutant and was subsequently shown to catalyse the dissociation of ESCRT complexes.
The catalytic domain of DUBs is what classifies them into particular groups; USPs, OTUs, MJDs, UCHs and MPN+/JAMMs. The first 4 groups are cysteine proteases, whereas the latter is a zinc metalloprotease. The cysteine protease DUBs are papain-like and thus have a similar mechanism of action. They use either catalytic diads or triads (either two or three amino acids) to catalyse the hydrolysis of the amide bonds between ubiquitin and the substrate.
The most prominent examples of non-coding RNAs are transfer RNA (tRNA) and ribosomal RNA (rRNA), both of which are involved in the process of translation. There are also non-coding RNAs involved in gene regulation, RNA processing and other roles. Certain RNAs are able to catalyse chemical reactions such as cutting and ligating other RNA molecules, and the catalysis of peptide bond formation in the ribosome; these are known as ribozymes.
By harnessing creative teamwork within a suitable co-design framework, some metadesigners have sought to catalyse changes at a behavioural level.Wood, J., (2007), "Win- Win-Win-Win-Win-Win: synergy tools for metadesigners", a chapter in "Designing for the 21st Century, Interdisciplinary Questions and Insights" book, (ed. Thomas Inns) Gower Publishing, , December 2007. However, as Albert Einstein said, "We can't solve problems by using the same kind of thinking we used when we created them".
Technetium exhibits nine oxidation states from −1 to +7, with +4, +5, and +7 being the most common. Technetium dissolves in aqua regia, nitric acid, and concentrated sulfuric acid, but it is not soluble in hydrochloric acid of any concentration. Metallic technetium slowly tarnishes in moist air and, in powder form, burns in oxygen. Technetium can catalyse the destruction of hydrazine by nitric acid, and this property is due to its multiplicity of valencies.
In molecular biology, the ELFV dehydrogenase family of enzymes include glutamate, leucine, phenylalanine and valine dehydrogenases. These enzymes are structurally and functionally related. They contain a Gly-rich region containing a conserved Lys residue, which has been implicated in the catalytic activity, in each case a reversible oxidative deamination reaction. Glutamate dehydrogenases , and (GluDH) are enzymes that catalyse the NAD- and/or NADP- dependent reversible deamination of L-glutamate into alpha-ketoglutarate.
Reaction mechanism of the flavin cofactor to catalyse the Baeyer-Villiger reaction in Baeyer-Villiger monooxygenase enzymes. In nature, enzymes called Baeyer- Villiger monooxygenases (BVMOs) perform the oxidation analogously to the chemical reaction. To facilitate this chemistry, BVMOs contain a flavin adenine dinucleotide (FAD) cofactor. In the catalytic cycle (see figure on the right), the cellular redox equivalent NADPH first reduces the cofactor, which allows it subsequently to react with molecular oxygen.
Most clinically used antibiotics are based upon natural products. The most important family of antibiotics contains a β-lactam ring, and includes the penicillin, cephalosporin, clavam, and carbapenem antibiotics. The group's biosynthetic work has focused on the clavams and carbapenems, with a particular focus being on the mechanism and structures of enzymes that catalyse chemically 'interesting' steps. The biggest threat to the continued use of β-lactam antibiotics is that of bacterial resistance.
The pathogenesis of MEB is related to an abnormal level of α‐dystroglycan glycosylation. Genetic mutations of the POMGnT1 gene reduced the O-mannosyl glycosylation of α-dystroglycan. The POMGnT1 gene encodes the enzyme POMGnT1, a type II transmembrane protein residing in the Golgi Apparatus. The role of the enzyme POMGnT1 is to catalyse glycosylation specific for alpha-linked terminal mannose, the process where N-acetylglucosamine is added to O-linked mannose of α-dystroglycan.
In enzymology, an alpha-factor-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + alpha-factorin \rightleftharpoons ADP + phosphate + alpha-factorout The 3 substrates of this enzyme are ATP, H2O, and alpha-factor, whereas its 3 products are ADP, phosphate, and alpha- factor. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (alpha- factor-transporting).
In enzymology, an arsenite-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + arsenitein \rightleftharpoons ADP + phosphate + arseniteout The 3 substrates of this enzyme are ATP, H2O, and arsenite, whereas its 3 products are ADP, phosphate, and arsenite. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (arsenite-exporting).
In enzymology, a beta-glucan-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + beta-glucanin \rightleftharpoons ADP + phosphate + beta-glucanout The 3 substrates of this enzyme are ATP, H2O, and beta-glucan, whereas its 3 products are ADP, phosphate, and beta-glucan. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (beta-glucan- exporting).
In enzymology, a capsular-polysaccharide-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + capsular polysaccharidein \rightleftharpoons ADP + phosphate + capsular polysaccharideout The 3 substrates of this enzyme are ATP, H2O, and capsular polysaccharide, whereas its 3 products are ADP, phosphate, and capsular polysaccharide. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (capsular-polysaccharide- exporting).
For example, proteases such as chymotrypsin contain an oxyanion hole to stabilise the tetrahedral intermediate anion formed during proteolysis and protects substrate's negatively charged oxygen from water molecules. Additionally, it may allow for insertion or positioning of a substrate, which would suffer from steric hindrance if it could not occupy the hole (such as BPG in hemoglobin). Enzymes that catalyse multi-step reactions can have multiple oxyanion holes that stabilise different transition states in the reaction.
Addition of fucose sugars to serine and threonine residues is an unusual form of O-glycosylation that occurs in the endoplasmic reticulum and is catalysed by two fucosyltransferases. These were discovered in Plasmodium falciparum and Toxoplasma gondii. Several different enzymes catalyse the elongation of the core fucose, meaning that different sugars can be added to the initial fucose on the protein. Along with O-glucosylation, O-fucosylation is mainly found on epidermal growth factor (EGF) domains found in proteins.
The biosynthesis of disaccharides, oligosaccharides, and polysaccharides involves the action of hundreds of different glycosyltransferases. These enzymes catalyse the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The family consists of various 1,3-beta-glucan synthase components including Gls1, Gls2, and Gls3 from yeast. 1,3-Beta-glucan synthase () also known as callose synthase catalyses the formation of a beta-1,3-glucan polymer that is a major component of the fungal cell wall.
Western blotting allows the detection of specific proteins from extracts made from cells or tissues, before or after any purification steps. Proteins are generally separated by size using gel electrophoresis before being transferred to a synthetic membrane via dry, semi-dry, or wet blotting methods. The membrane can then be probed using antibodies using methods similar to immunohistochemistry, but without a need for fixation. Detection is typically performed using peroxidase linked antibodies to catalyse a chemiluminescent reaction.
The general mechanism for the Suzuki reaction Pincer complexes have been shown to catalyse Suzuki-Miyaura coupling reactions, a versatile carbon-carbon bond forming reaction. Typical Suzuki coupling employ Pd(0) catalysts with monodentate tertiary phosphine ligands (e.g. Pd(PPh3)4). It is a very selective method to couple aryl substituents together, but requires elevated temperatures. Using PCP pincer-palladium catalysts, aryl-aryl couplings can be achieved with turnover numbers (TONs) upwards of 900,000 and high yields.
Aminoacyl-tRNA synthetases, class II is a family of proteins. These proteins catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction. These proteins differ widely in size and oligomeric state, and have a limited sequence homology. The 20 aminoacyl- tRNA synthetases are divided into two classes, I and II. Class I aminoacyl- tRNA synthetases contain a characteristic Rossman fold catalytic domain and are mostly monomeric.
Science Foundation Ireland, through the SFI Discover Programme promotes awareness and engagement of the Irish public with science, technology, engineering and maths (STEM). The SFI Discover Programme was set up to catalyse, inspire and guide STEM education and public engagement. To achieve this the programme Call funds the development of STEM education and public engagement sector in Ireland, investing in developing and extending activity and ability in this area, and exploring and encouraging novel means of engaging the public.
Amine-borane FLPs catalyse the borylation of electron-rich aromatic heterocycles (Scheme 1). The reaction is driven by release of hydrogen via C-H activation by the FLP. Aromatic borylations are often used in pharmaceutical development, particularly due to the abundance, low cost and low toxicity of boron compounds compared to noble metals., Scheme 1: Mechanism for borylation catalysed by FLPThe substrate for the reaction has two main requirements, strongly linked to the mechanism of borylation.
Many proteins are enzymes that catalyse biochemical reactions and are vital to metabolism. Proteins also have structural or mechanical functions, such as actin and myosin in muscle and the proteins in the cytoskeleton, which form a system of scaffolding that maintains cell shape. Other proteins are important in cell signaling, immune responses, cell adhesion, and the cell cycle. In animals, proteins are needed in the diet to provide the essential amino acids that cannot be synthesized.
The image shows a cytosine single ring base and a methyl group added on to the 5 carbon. In mammals, DNA methylation occurs almost exclusively at a cytosine that is followed by a guanine. Demethylation by TET enzymes (see second Figure), can alter the regulation of transcription. The TET enzymes catalyze the hydroxylation of DNA 5-methylcytosine (5mC) to 5-hydroxymethylcytosine (5hmC), and can further catalyse oxidation of 5hmC to 5-formylcytosine (5fC) and then to 5-carboxycytosine (5caC).
The tungsten oxidoreductases may also catalyse oxidations. The first tungsten-requiring enzyme to be discovered also requires selenium, and in this case the tungsten- selenium pair may function analogously to the molybdenum-sulfur pairing of some molybdopterin-requiring enzymes. One of the enzymes in the oxidoreductase family which sometimes employ tungsten (bacterial formate dehydrogenase H) is known to use a selenium-molybdenum version of molybdopterin. Acetylene hydratase is an unusual metalloenzyme in that it catalyzes a hydration reaction.
When CO2 is released in the bundle sheath cells, pyruvate is regenerated, and the cycle continues. Though the reaction catalysed by PPDK is reversible, PEP is favoured as the product in biological conditions. This is due to the basic pH in the stroma, where the reaction occurs, as well as high concentrations of adenylate kinase and pyrophosphatase. Because these two enzymes catalyse exergonic reactions involving AMP, and disphosphate, respectively, they drive the PPDK-catalysed reaction forward.
Some E3 enzymes also activate the E2 enzymes. E3 enzymes possess one of two domains: the homologous to the E6-AP carboxyl terminus (HECT) domain and the really interesting new gene (RING) domain (or the closely related U-box domain). HECT domain E3s transiently bind ubiquitin in this process (an obligate thioester intermediate is formed with the active-site cysteine of the E3), whereas RING domain E3s catalyse the direct transfer from the E2 enzyme to the substrate.
Earlier work by Agnes Pockels influenced the development of the trough. ;Zeolite Y :Zeolite Y, a molecular sieve used to catalyse fractional distillation in petroleum refining, was invented by Edith M. Flanigen while working for Union Carbide. Flanigen also co-invented a synthetic emerald and was the first female recipient of the Perkin Medal in 1992. ;Synthetic radiochemistry :Irene Joliot-Curie was awarded the 1935 Nobel Prize in Chemistry for synthesis of new radioactive elements for application in medicine.
The aliens consider the Alphans inconsequential life-forms and have no qualms about killing them. As they possess little kinetic energy, they must deceive the Alphans via illusion into performing the act themselves. Koenig accesses cameras at the nuclear-waste domes and finds the Eagle there. Atomic fuel will be needed to catalyse the reaction; he switches cameras to the atomic fuel storage facility and finds Carter and Erhlich already there to procure the deadly container.
The catalytic region can be subdivided into three domains: an N-domain (N-terminal), a large L-domain, and a small S-domain (inserted within the L-domain). The L-domain binds the substrate, while the S-domain binds NADP. Class II HMG-CoA reductases catalyse the reverse reaction of class I enzymes, namely the NAD-dependent synthesis of HMG-CoA from mevalonate and CoA. Some bacteria, such as Pseudomonas mevalonii, can use mevalonate as the sole carbon source.
Since DcuA is encoded in an operon with the gene for aspartase, and DcuB is encoded in an operon with the gene for fumarase, their physiological functions may be to catalyse aspartate:fumarate and fumarate:malate exchange during the anaerobic utilization of aspartate and fumarate, respectively. The two transporters can apparently substitute for each other under certain physiological conditions. The generalized transport reaction catalyzed by the proteins of the Dcu family is: > Dicarboxylate1 (out) + Dicarboxylate2 (in) ⇌ Dicarboxylate1 (in) + > Dicarboxylate2 (out).
The PKA enzyme also contains two catalytic PKS-Cα subunits, and a regulator PKA-R subunit dimer. The PKA holoenzyme is inactive under normal conditions, however, when cAMP molecules that are produced earlier in the signal transduction mechanism combine with the enzyme, PKA undergoes a conformational change. This activates it, giving it the ability to catalyse substrate phosphorylation. CREB (cAMP response element binding protein) belongs to a family of transcription factors and is positioned in the nucleus of the neuron.
Class II comprises three catalytic isoforms (C2α, C2β, and C2γ), but, unlike Classes I and III, no regulatory proteins. Class II catalyse the production of PI(3)P from PI and PI(3,4)P2 from PI(4)P; however, little is known about their role in immune cells. PI(3,4)P2 has, however, been shown to play a role in the invagination phase of clathrin-mediated endocytosis. C2α and C2β are expressed through the body, but expression of C2γ is limited to hepatocytes.
In enzymology, a molybdate-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + molybdateout \rightleftharpoons ADP + phosphate + molybdatein The 3 substrates of this enzyme are ATP, H2O, and molybdate, whereas its 3 products are ADP, phosphate, and molybdate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (molybdate-importing). This enzyme participates in abc transporters - general.
In enzymology, a monosaccharide-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + monosaccharideout \rightleftharpoons ADP + phosphate + monosaccharidein The 3 substrates of this enzyme are ATP, H2O, and monosaccharide, whereas its 3 products are ADP, phosphate, and monosaccharide. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (monosaccharide-importing). This enzyme participates in abc transporters - general.
In enzymology, a maltose-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + maltoseout \rightleftharpoons ADP + phosphate + maltosein The 3 substrates of this enzyme are ATP, H2O, and maltose, whereas its 3 products are ADP, phosphate, and maltose. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (maltose-importing). This enzyme is a member of the ABC Transporter family.
In enzymology, a Fe3+-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + Fe3+out \rightleftharpoons ADP + phosphate + Fe3+in The 3 substrates of this enzyme are ATP, H2O, and Fe3+, whereas its 3 products are ADP, phosphate, and Fe3+. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (ferric-ion-transporting). This enzyme participates in abc transporters - general.
In enzymology, a heme-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + hemein \rightleftharpoons ADP + phosphate + hemeout The 3 substrates of this enzyme are ATP, H2O, and heme, whereas its 3 products are ADP, phosphate, and heme. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (heme-exporting). This enzyme participates in abc transporters - general.
In enzymology, an oligopeptide-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + oligopeptide(out) \rightleftharpoons ADP + phosphate + oligopeptide(in) The 3 substrates of this enzyme are ATP, H2O, and oligopeptide, whereas its 3 products are ADP, phosphate, and oligopeptide. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (oligopeptide-importing). This enzyme is also called oligopeptide permease.
In enzymology, a sulfate-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + sulfateout \rightleftharpoons ADP + phosphate + sulfatein The 3 substrates of this enzyme are ATP, H2O, and sulfate, whereas its 3 products are ADP, phosphate, and sulfate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (sulfate-importing). This enzyme participates in abc transporters - general.
In enzymology, a phosphate-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + phosphate(out) \rightleftharpoons ADP + phosphate + phosphate(in) The 3 substrates of this enzyme are ATP, H2O, and phosphate, whereas its two products are ADP and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (phosphate-importing). This enzyme is also called ABC phosphate transporter.
In enzymology, a polyamine-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + polyamineout \rightleftharpoons ADP + phosphate + polyaminein The 3 substrates of this enzyme are ATP, H2O, and polyamine, whereas its 3 products are ADP, phosphate, and polyamine. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (polyamine-importing). This enzyme participates in abc transporters - general.
For several years, she worked alongside Maria Balshaw on the £15 million transformation of the Whitworth. In 2016-17 she was a Fellow on the Clore Leadership Programme, exploring social and civic purpose, leadership and the future of museums. Her placement was with the Heritage Lottery Fund, exploring how to catalyse and support community heritage and activism. Her career has been driven by learning and social purpose with a longstanding commitment to make museums more inclusive and relevant to a wider audience.
Conjugates and their metabolites can be excreted from cells in phase III of their metabolism, with the anionic groups acting as affinity tags for a variety of membrane transporters of the multidrug resistance protein (MRP) family. These proteins are members of the family of ATP-binding cassette transporters and can catalyse the ATP-dependent transport of a huge variety of hydrophobic anions, and thus act to remove phase II products to the extracellular medium, where they may be further metabolized or excreted.
Ascorbate-dependent peroxidase activity was first reported in 1979,, more than 150 years after the first observation of peroxidase activity in horseradish plantsPlanche, LA. (1810) Bull. Pharm., 2, 578 and almost 40 years after the discovery of the closely related cytochrome c peroxidase enzyme. Peroxidases have been classified into three types (class I, class II and class III): ascorbate peroxidases is a class I peroxidase enzyme. APXs catalyse the H2O2-dependent oxidation of ascorbate in plants, algae and certain cyanobacteria.
A regulatory enzyme is an enzyme in a biochemical pathway which, through its responses to the presence of certain other biomolecules, regulates the pathway activity. This is usually done for pathways whose products may be needed in different amounts at different times, such as hormone production. Regulatory enzymes exist at high concentrations (low Vmax) so their activity can be increased or decreased with changes in substrate concentrations. The enzymes which catalyse chemical reactions again and again are called regulatory enzymes.
The first evidence for the requirement of flavin as an enzyme cofactor came in 1935. Hugo Theorell and coworkers showed that a bright-yellow-coloured yeast protein, identified previously as essential for cellular respiration, could be separated into apoprotein and a bright-yellow pigment. Neither apoprotein nor pigment alone could catalyse the oxidation of NADH, but mixing of the two restored the enzyme activity. However, replacing the isolated pigment with riboflavin did not restore enzyme activity, despite their being indistinguishable under spectroscopy.
OurCity is one of Fondation Botnar’s key initiatives, aiming to support selected cities around the world to implement coordinated programs that leverage digital technologies and artificial intelligence (AI), and transform them into places where young people’s wellbeing and opportunity is secured. We see OurCity as a process that will catalyse stakeholders and drive policy change through inclusive engagement and advocacy. The initiative collaborates with young people, civil society, policymakers, innovators, and other city champions to nurture wellbeing and opportunity for all.
As the prog country "Cosmic Cowboy" trend lost momentum, the store staff embraced the growing punk rock trend with zeal. Importers became the store's most important suppliers, with shipments arriving at least once or twice a week with singles, LPs and magazines from the United Kingdom punk scene. Buyer Neil Ruttenberg made punk rock the store's specialty and helped catalyse punk's local popularity. DIY bands began rapidly appearing throughout Austin, which already enjoyed a reputation as a haven for live music.
The N-terminal domain of the protein Serine acetyltransferase helps catalyse acetyl transfer. This particular enzyme catalyses serine into cysteine which is eventually converted to the essential amino acid methionine. Of particular interest to scientists, is the ability to harness the natural ability of the enzyme, Serine acetyltransferase, to create nutritionally essential amino acids and to exploit this ability through transgenic plants. These transgenic plants would contain more essential sulphur amino acids meaning a healthier diet for humans and animals.
The Sustainable Development Policy Institute (SDPI) provides the global sustainable development community with representation from Pakistan as well as South Asia as a whole. The Institute's mission is: "To catalyse the transition towards sustainable development, defined as the enhancement of peace, social justice and well-being, within and across generations". The think tank is based in Islamabad, Pakistan. The Lauder Institute of University of Pennsylvania ranks it at number 15 among research institutes in Southeast Asia and the Pacific region.
This has the effect of increasing the concentration of the reactants at the catalyst surface and also weakening of the bonds in the reacting molecules (the activation energy is lowered). Also because the transition metal ions can change their oxidation states, they become more effective as catalysts. An interesting type of catalysis occurs when the products of a reaction catalyse the reaction producing more catalyst (autocatalysis). One example is the reaction of oxalic acid with acidified potassium permanganate (or manganate (VII)).
This enzyme participates in limonene and pinene degradation. Epoxide hydrolases catalyse the hydrolysis of epoxides to corresponding diols, which is important in detoxification, synthesis of signal molecules, or metabolism. Limonene-1,2- epoxide hydrolase (LEH) differs from many other epoxide hydrolases in its structure and its novel one-step catalytic mechanism. Its main fold consists of a six-stranded mixed beta-sheet, with three N-terminal alpha helices packed to one side to create a pocket that extends into the protein core.
Glycine and lysine linked by an isopeptide bond. The isopeptide bond is highlighted yellow. # Ligation: E3 ubiquitin ligases catalyse the final step of the ubiquitination cascade. Most commonly, they create an isopeptide bond between a lysine of the target protein and the C-terminal glycine of ubiquitin. In general, this step requires the activity of one of the hundreds of E3s. E3 enzymes function as the substrate recognition modules of the system and are capable of interaction with both E2 and substrate.
In general, these systems use one or more proteins and act on unique asymmetric DNA sequences. The products of the recombination event depend on the relative orientation of these asymmetric sequences. Many other proteins apart from the recombinase are involved in regulating the reaction. During site-specific DNA recombination, which brings about genetic rearrangement in processes such as viral integration and excision and chromosomal segregation, these recombinase enzymes recognize specific DNA sequences and catalyse the reciprocal exchange of DNA strands between these sites.
Cre recombinase is a tyrosine recombinase enzyme derived from the P1 bacteriophage. The enzyme uses a topoisomerase I-like mechanism to carry out site specific recombination events. The enzyme (38kDa) is a member of the integrase family of site specific recombinase and it is known to catalyse the site specific recombination event between two DNA recognition sites (LoxP sites). This 34 base pair (bp) loxP recognition site consists of two 13 bp palindromic sequences which flank an 8bp spacer region.
Chromium(III) chloride is used as the precursor to many organochromium compounds, for example bis(benzene)chromium, an analogue of ferrocene: :400px Phosphine complexes derived from CrCl3 catalyse the trimerization of ethylene to 1-hexene.John T. Dixon, Mike J. Green, Fiona M. Hess, David H. Morgan “Advances in selective ethylene trimerisation – a critical overview” Journal of Organometallic Chemistry 2004, Volume 689, pp 3641-3668. Feng Zheng, Akella Sivaramakrishna, John R. Moss “Thermal studies on metallacycloalkanes” Coordination Chemistry Reviews 2007, Volume 251, 2056-2071.
In enzymology, a mitochondrial protein-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O \rightleftharpoons ADP + phosphate Thus, the two substrates of this enzyme are ATP and H2O, whereas its two products are ADP and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (mitochondrial protein-importing). During the interactions of the proteins Hsp70 and sunbit Tim44, ATPase domain is essential.
In enzymology, an iron-chelate-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + iron chelateout \rightleftharpoons ADP + phosphate + iron chelatein The 3 substrates of this enzyme are ATP, H2O, and iron chelate, whereas its 3 products are ADP, phosphate, and iron chelate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (iron-chelate-importing). This enzyme participates in abc transporters - general.
In enzymology, a manganese-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + Mn2+out \rightleftharpoons ADP + phosphate + Mn2+in The 3 substrates of this enzyme are ATP, H2O, and Mn2+, whereas its 3 products are ADP, phosphate, and Mn2+. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is called ATP phosphohydrolase (manganese-importing). This enzyme is also known as ABC-type manganese permease complex.
In enzymology, a nonpolar-amino-acid-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + nonpolar amino acidout \rightleftharpoons ADP + phosphate + nonpolar amino acidin The 3 substrates of this enzyme are ATP, H2O, and nonpolar amino acid, whereas its 3 products are ADP, phosphate, and nonpolar amino acid. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (nonpolar-amino-acid-transporting).
In enzymology, a fatty-acyl-CoA-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + fatty acyl CoAcis \rightleftharpoons ADP + phosphate + fatty acyl CoAtrans The 3 substrates of this enzyme are ATP, H2O, and fatty acyl CoAcis, whereas its 3 products are ADP, phosphate, and fatty acyl CoAtrans. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (fatty-acyl-CoA-transporting).
In enzymology, a teichoic-acid-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + teichoic acidin \rightleftharpoons ADP + phosphate + teichoic acidout The 3 substrates of this enzyme are ATP, H2O, and teichoic acid, whereas its 3 products are ADP, phosphate, and teichoic acid. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (teichoic-acid-exporting). This enzyme participates in abc transporters - general.
In enzymology, a vitamin B12-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + vitamin B12out \rightleftharpoons ADP + phosphate + vitamin B12in The 3 substrates of this enzyme are ATP, H2O, and vitamin B12, whereas its 3 products are ADP, phosphate, and vitamin B12. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (vitamin B12-importing). This enzyme participates in abc transporters - general.
In enzymology, a quaternary-amine-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + quaternary amineout \rightleftharpoons ADP + phosphate + quaternary aminein The 3 substrates of this enzyme are ATP, H2O, and quaternary amine, whereas its 3 products are ADP, phosphate, and quaternary amine. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (quaternary-amine-importing). This enzyme participates in abc transporters - general.
Rewilding Europe Capital (REC) is the first ‘rewilding enterprise’ funding facility that provides financial loans to new and existing business that catalyse, support and achieve positive environmental and socio-economic outcomes that support rewilding in Europe. European Investment Bank provided Rewilding Europe Capital with a 6 million euro loan finance contract. It is the first project of the “Bank on Nature Initiative”, set up by the European Commission. The signing ceremony took place in the Berlaymont Building, headquarters of the European Commission in Brussels.
The year 2010 marked the 60th anniversary of Chinese-Swedish diplomatic relations. The celebrations drew attention in China, as Sweden had been the first Western country to establish diplomatic relations with the country. This resulted in the creation of the Nordic Confucius Institute in Sweden to further promote and develop Sino- Swedish relationships. The disappearance of five Hong Kong booksellers including notably the extrajudicial rendition of author-publisher Gui Minhai, a Swedish national, from his residence in Thailand in late 2015 would catalyse sharp deterioration in relations.
Enzyme promiscuity is the ability of an enzyme to catalyse a fortuitous side reaction in addition to its main reaction. Although enzymes are remarkably specific catalysts, they can often perform side reactions in addition to their main, native catalytic activity. These promiscuous activities are usually slow relative to the main activity and are under neutral selection. Despite ordinarily being physiologically irrelevant, under new selective pressures these activities may confer a fitness benefit therefore prompting the evolution of the formerly promiscuous activity to become the new main activity.
Protein tyrosine phosphatases are a group of enzymes that remove phosphate groups from phosphorylated tyrosine residues on proteins. Protein tyrosine (pTyr) phosphorylation is a common post-translational modification that can create novel recognition motifs for protein interactions and cellular localization, affect protein stability, and regulate enzyme activity. As a consequence, maintaining an appropriate level of protein tyrosine phosphorylation is essential for many cellular functions. Tyrosine-specific protein phosphatases (PTPase; ) catalyse the removal of a phosphate group attached to a tyrosine residue, using a cysteinyl-phosphate enzyme intermediate.
19, May, 2007. # “24-Hour Knowledge Factory: Using Internet Technology to Leverage Spatial and Temporal Separations” (with S. Seshasai), ACM Transactions on Internet Technology, Vol. 7, No. 3, August 2007, pp 1-22. # “Offshoring: The Transition from Economic Drivers toward Strategic Global Partnership and 24-Hour Knowledge Factory” (with S. Seshasai, S. Mukherji, and A. Ganguly), Journal of Electronic Commerce in Organizations, Vol. 5, No. 2, April-June 2007, pp 1-23. # “A Three-Faceted Educational Approach to Catalyse Innovation”, Journal of Industry and Higher Education, Vol.
Prior to Clear Care, the market only provided a two step system where you first soaked the lenses in peroxide for a short period of time or overnight then replaced it with a neutralizing saline. These systems used a catalyse enzyme in saline form and was preserved. The AOSept system made by American Optical was the peroxide solution uses a disk to neutralize the solution. The Lensept system was also similar and used two different cups, one contained the disc and the other was for soaking.
The Elders is independently funded by a group of donors, including Branson and Gabriel. The Elders use their collective skills to catalyse peaceful resolutions to long-standing conflicts, articulate new approaches to global issues that are causing or may later cause immense human suffering, and share wisdom by helping to connect voices all over the world. They work together to consider carefully which specific issues to approach. In November 2007, Gabriel's non-profit group WITNESS launched The Hub, a participatory media site for human rights.
Most glycosyltransferase enzymes form one of two folds: GT-A or GT-B Glycosyltransferases (GTFs, Gtfs) are enzymes (EC 2.4) that establish natural glycosidic linkages. They catalyze the transfer of saccharide moieties from an activated nucleotide sugar (also known as the "glycosyl donor") to a nucleophilic glycosyl acceptor molecule, the nucleophile of which can be oxygen- carbon-, nitrogen-, or sulfur-based. The result of glycosyl transfer can be a carbohydrate, glycoside, oligosaccharide, or a polysaccharide. Some glycosyltransferases catalyse transfer to inorganic phosphate or water.
The Jamaica College Foundation was established in order to assist the school's administration and Board of Management. The organisation aims to catalyse the transformation into and the maintenance of Jamaica College as a first class institution of learning and physical development. The mandate includes the creation and maintenance of a physical environment which features grounds, structures and facilities as will embed in the young men a sense of being in the presence of excellence, grandeur and history and motivate them to conduct themselves accordingly.
Such materials combine high hydrophobicity and chemical stability with electrical and thermal conductivity and can be used as electrode material for super capacitors. Sulfonic acid functional groups can be attached to activated carbon to give "starbons" which can be used to selectively catalyse the esterification of fatty acids. Formation of such activated carbons from halogenated precursors gives a more effective catalyst which is thought to be a result of remaining halogens improving stability. It is reported about synthesis of activated carbon with chemically grafted superacid sites –CF2SO3H.
When glucose enters a cell it is rapidly changed to glucose 6-phosphate, by hexokinase or glucokinase. The glucose cycle can occur in liver cells due to a liver specific enzyme glucose-6-phosphatase, which catalyse the dephosphorylation of glucose 6-phosphate back to glucose. Glucose-6-phosphate is the product of glycogenolysis or gluconeogenesis, where the goal is to increase free glucose in the blood due body being in catabolic state. Other cells such as muscle and brain cells do not contain glucose 6-phosphatase.
However, the IPCC can be said to stimulate research in climate science. Chapters of IPCC reports often close with sections on limitations and knowledge or research gaps, and the announcement of an IPCC special report can catalyse research activity in that area. Thousands of scientists and other experts contribute on a voluntary basis to writing and reviewing reports, which are then reviewed by governments. IPCC reports contain a "Summary for Policymakers", which is subject to line-by-line approval by delegates from all participating governments.
It supports a peptidyl-RNA synthesis that could be a precursor for the contemporary process of linking amino acids to tRNA molecules. An RNA ligase's catalytic domain, consisting of 93 nucleotides, proved to be sufficient to catalyse a linking reaction between two RNA chains. Similarly, an acyltransferase ribozyme 82 nucleotides long was sufficient to perform an acyltransfer reaction. Altogether, the results concerning the RNA ligase's catalytic domain and the acyltransferase ribozyme are in agreement with the estimated upper limit of 100 nucleotides set by the error threshold problem.
Hair follicle with mesenchymal dermal papilla, labelled at top, location of hair follicle stem cells and thought to be site of action of DHT. Type 1 and 2 5α reductase enzymes are present at pilosebaceous units in papillae of individual hair follicles. They catalyse formation of the androgens testosterone and DHT, which in turn regulate hair growth. Androgens have different effects at different follicles: they stimulate IGF-1 at facial hair, causing hair regrowth, but stimulate TGF β1, TGF β2, dickkopf1 and IL-6 at the scalp, causing hair follicle miniaturisation.
A comparison between major and minor splicing mechanisms Spliceosomes catalyse splicing, an integral step in eukaryotic precursor messenger RNA maturation. A splicing mistake in even a single nucleotide can be devastating to the cell, and a reliable, repeatable method of RNA processing is necessary to ensure cell survival. The spliceosome is a large, protein-RNA complex that consists of five small nuclear RNAs (U1, U2, U4, U5, and U6) and over 150 proteins. The snRNAs, along with their associated proteins, form ribonucleoprotein complexes (snRNPs), which bind to specific sequences on the pre-mRNA substrate.
In enzymology, a Mg2+-importing ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + Mg2+out \rightleftharpoons ADP + phosphate + Mg2+in The 3 substrates of this enzyme are ATP, H2O, and Mg2+, whereas its 3 products are ADP, phosphate, and Mg2+. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (Mg2+-importing). The mgtA gene which encodes this enzyme is thought to be regulated by a magnesium responsive RNA element.
In enzymology, a Cl-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + Cl−out \rightleftharpoons ADP + phosphate + Cl−in The 3 substrates of this enzyme are ATP, H2O, and Cl−, whereas its 3 products are ADP, phosphate, and Cl−. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (Cl−-importing). Other names in common use include Cl−-translocating ATPase, and Cl−-motive ATPase.
In enzymology, a glycerol-3-phosphate-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + glycerol-3-phosphateout \rightleftharpoons ADP + phosphate + glycerol-3-phosphatein The 3 substrates of this enzyme are ATP, H2O, and glycerol-3-phosphate, whereas its 3 products are ADP, phosphate, and glycerol-3-phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (glycerol-3-phosphate-importing). This enzyme participates in abc transporters - general.
An analogous approach is to use mass spectrometry to monitor the incorporation or release of stable isotopes as substrate is converted into product. Occasionally, an assay fails and approaches are essential to resurrect a failed assay. The most sensitive enzyme assays use lasers focused through a microscope to observe changes in single enzyme molecules as they catalyse their reactions. These measurements either use changes in the fluorescence of cofactors during an enzyme's reaction mechanism, or of fluorescent dyes added onto specific sites of the protein to report movements that occur during catalysis.
In enzymology, a phospholipid-translocating ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + phospholipid in \rightleftharpoons ADP + phosphate + phospholipid out The 3 substrates of this enzyme are ATP, H2O, and phospholipid, whereas its 3 products are ADP, phosphate, and phospholipid. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (phospholipid-flipping). Other names in common use include Mg2+-ATPase, flippase, and aminophospholipid-transporting ATPase.
In enzymology, a polar-amino-acid-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + polar amino acidout ADP + phosphate + polar amino acidin The 3 substrates of this enzyme are ATP, H2O, and polar amino acid, whereas its 3 products are ADP, phosphate, and polar amino acid. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (polar-amino-acid-importing). This enzyme is also called histidine permease.
In enzymology, a lysophospholipase () is an enzyme that catalyzes the chemical reaction :2-lysophosphatidylcholine + H2O \rightleftharpoons glycerophosphocholine + a carboxylate Thus, the two substrates of this enzyme are 2-lysophosphatidylcholine and H2O, whereas its two products are glycerophosphocholine and carboxylate. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. This family consists of lysophospholipase / phospholipase B and cytosolic phospholipase A2 which also has a C2 domain . Phospholipase B enzymes catalyse the release of fatty acids from lysophospholipids and are capable in vitro of hydrolyzing all phospholipids extractable from yeast cells.
Main hall of the Shrine of the Lord Genghis Khan, in Ordos City, China. Nationwide reverence of Genghis Khan had existed until the 1930s, centered on a shrine which preserved mystical relics of Genghis, that was located in the Ordos Loop of the region of Inner Mongolia, in China. The Japanese, during the occupation of China, tried to take possession of the relics in order to catalyse a pro-Japanese Mongol nationalism, but they failed. Within the Mongolian People's Republic (1924–92) the Mongolian native religion was suppressed, and Genghis' shrines destroyed.
In November 2017, a similar campaign, called Europe Beyond Coal, was launched in Europe. This campaign is inspired by the US Beyond Coal campaign but is independent from it. Europe Beyond Coal is an alliance of civil society groups working to catalyse the closures of coal mines and power plants, prevent the building of any new coal projects and hasten the just transition to clean, renewable energy and energy efficiency. Over 30 NGOs, including Greenpeace, WWF, EEB, Climate Action Network Europe and many others, take part in the European campaign.
The link between these two protein within the JAK1-SNX8 complex allows JAK1 to catalyse SNX8's tyrosines phosphorylation in positions 95 and 126. This phosphorylation activates the JAK1-SNX, and the SNX8 acts as an adaptor or scaffolding protein by permitting the recruitment of the inhibitor of nuclear factor-kappa-B kinase subunit beta (IKKβ) to JAK1 in the JAK1-SNX8-IKKβ complex. This linkage is essential for IKKβ activation through autophosphorylation at serine in position 177 (as SNX8 lacks enzymatic activity) and further dimerization and oligomerization.
Several assays were developed to study the enzyme kinetics and inhibition of ICL. The most frequently-used assays involved the use of chemical or enzyme- coupled ultraviolet–visible (UV/vis) spectroscopy to measure the amount of glyoxylate that is being formed. For example, glyoxylate can be reacted with phenylhydrazine to form hydrazone that can be analysed by UV/vis spectroscopy. Alternatively, lactate dehydrogenase can be used to catalyse the reduction of glyoxylate to glycolate in the presence of nicotinamide adenine dinucleotide (NADH), which is a cosubstrate of lactate dehydrogenase.
Although enzymes are typically highly specific, some are able to perform catalysis on more than one substrate, a property termed enzyme promiscuity. An enzyme may have many native substrates and broad specificity (e.g. oxidation by cytochrome p450s) or it may have a single native substrate with a set of similar non-native substrates that it can catalyse at some lower rate. The substrates that a given enzyme may react with in vitro, in a laboratory setting, may not necessarily reflect the physiological, endogenous substrates of the enzyme's reactions in vivo.
According to The Guardian Munich Machine was an important record that helped to catalyse electroclash. According to the music magazine De:Bug: “Munich Machine feels like the result of a dynamic collaboration by Munich residents engaged in the club scene and who know how to work with it. Every aspect of it has been carefully crafted and sometimes it seems as if DJ Hell is using this kind of mega-mix to grow beyond himself. This is particularly evident when he mixes together very different sources.”„DJ Hell – Munich Machine (V2)“, article issued 1.1.2000.
United Nations Democracy Fund (UNDEF), established by the Secretary-General in July 2005 to support democratization throughout the world. It focuses on strengthening the voice of civil society, promoting human rights and ensuring the participation of all groups in democratic processes. The Office also provides partnership advisory and outreach services in response to demand from the United Nations system, governments and non-State actors to catalyse public-private partnerships through high-impact events and advice to potential partners regarding opportunities and good practices to promote the Sustainable Development Goals as a framework for action.
A recent (2001 Pilkington Glass) innovation is so-called self-cleaning glass, aimed at building, automotive and other technical applications. A nanometre-scale coating of titanium dioxide on the outer surface of glass introduces two mechanisms which lead to the self-cleaning property. The first is a photo-catalytic effect, in which ultra-violet rays catalyse the breakdown of organic compounds on the window surface; the second is a hydrophilic effect in which water is attracted to the surface of the glass, forming a thin sheet which washes away the broken-down organic compounds.
A new tech incubator concept will be delivered within the iCentrumTM building, called "Serendip". It will promote unique collaborations across sectors, supported by corporate mentors from: Built Environment; Internet of Things; Intelligent Mobility; and [Digital Health]. This new concept in incubation will ensure iCentrumTM is a lighthouse, promoting and driving Birmingham’s Smart City agenda. The Serendip space will strike a balance between order and chaos, with proactive and energetic management used to catalyse interaction between start-ups, SMEs, public sector organisations and large corporates to drive delivery of innovative new products and services.
The aminoacyl-tRNA synthetases catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction. These proteins differ widely in size and oligomeric state, and have limited sequence homology. The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossmann fold catalytic domain and are mostly monomeric. Class II aminoacyl-tRNA synthetases share an anti-parallel beta-sheet fold flanked by alpha-helices, and are mostly dimeric or multimeric, containing at least three conserved regions.
March, J. (1992) Advanced Organic Chemistry, 4th ed., Wiley, New York. p. 723. Treatment of an arenediazonium salt with CuCl leads to an aryl chloride, for example: (Example Sandmeyer reaction using CuCl) The reaction has wide scope and usually gives good yields. Early investigators observed that copper(I) halides catalyse 1,4-addition of Grignard reagents to alpha,beta-unsaturated ketones led to the development of organocuprate reagents that are widely used today in organic synthesis:Jasrzebski, J. T. B. H.; van Koten, G. (2002) Modern Organocopper Chemistry, N. Krause (ed.).
Enzymes are evolved to catalyse a particular reaction on a particular substrate with a high catalytic efficiency (kcat/KM, cf. Michaelis–Menten kinetics). However, in addition to this main activity, they possess other activities that are generally several orders of magnitude lower, and that are not a result of evolutionary selection and therefore do not partake in the physiology of the organism. This phenomenon allows new functions to be gained as the promiscuous activity could confer a fitness benefit under a new selective pressure leading to its duplication and selection as a new main activity.
For example, ceric ammonium nitrate is a common oxidising agent in organic chemistry, releasing organic ligands from metal carbonyls. In the Belousov–Zhabotinsky reaction, cerium oscillates between the +4 and +3 oxidation states to catalyse the reaction. Cerium(IV) salts, especially cerium(IV) sulfate, are often used as standard reagents for volumetric analysis in cerimetric titrations. The nitrate complex is the most common cerium complex encountered when using cerium(IV) is an oxidising agent: it and its cerium(III) analogue have 12-coordinate icosahedral molecular geometry, while has 10-coordinate bicapped dodecadeltahedral molecular geometry.
Iopanoic acid is an iodine-containing radiocontrast medium used in cholecystography. Both iopanoic acid and ipodate sodium are potent inhibitors of thyroid hormone release from thyroid gland, as well as of peripheral conversion of thyroxine (T4) to triiodothyronine (T3). These compounds inhibit 5'deiodinase (5'DID-1 and 5'DID-2) enzymes, which catalyse T4-T3 conversion in the thyroid cell, liver, kidney, skeletal muscle, heart, brain, pituitary. This accounts for the dramatic improvement in both subjective and objective symptoms of hyperthyroidism, particularly when they are used as an adjunctive therapy with thioamides (propylthiouracil, carbimazole).
Simplistically, SDH uses NAD+ as an oxidant to catalyse the reversible pyridine nucleotide dependent oxidative deamination of the substrate, Saccharopine, in order to form the products, lysine and alpha- ketoglutarate. This can be described by the following equation: ::::SDH Saccharopine ⇌ lysine + alpha-ketoglutarate Saccharopine dehydrogenase EC catalyses the condensation to of l-alpha-aminoadipate-delta-semialdehyde (AASA) with l-glutamate to give an imine, which is reduced by NADPH to give saccharopine. In some organisms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase (PF). Homospermidine synthase proteins (EC).
The "action experiment" of tapping the power of the mainstream middle class urban English media to reflect unheard rural voices spoken in local languages, grounded in very local realities, got a measure of success. Recognizing the potential of writing in mainstream media to highlight rural development issues and catalyse change, Sanjoy conceived of CHARKHA. CHARKHA appears to have been initiated to exploit the legitimate opportunities available in the national media for influencing policies related to rural development. It also addressed the concern that such a massive task, required more support than his single voice.
Several mechanisms have been proposed for the production of hemozoin in Plasmodium, and the area is highly controversial, with membrane lipids, histidine-rich proteins, or even a combination of the two, being proposed to catalyse the formation of hemozoin. Other authors have described a Heme Detoxification Protein, which is claimed to be more potent than either lipids or histidine-rich proteins. It is possible that many processes contribute to the formation of hemozoin. The formation of hemozoin in other blood-feeding organisms is not as well-studied as in Plasmodium.
Kauffman, supra have suggested the relevance of autocatalysis models for life processes. In this construct, a group of elements catalyse reactions in a cyclical, or topologically circular, fashion. Several investigators have used these insights to suggest essential elements of a thermodynamic definition of the life process, which might briefly be summarized as stable, patterned (correlated) processes which intake (and dissipate) energy, and reproduce themselves.See Brooks and Wylie, Smolin, Kauffman, supra, and Pearce Ulanowicz, a theoretical ecologist, has extended the relational analysis of life processes to ecosystems, using information theory tools.
A bilby as illustrated by John Gould Bilbies are native Australian marsupials that are endangered. To raise money and increase awareness of conservation efforts, bilby-shaped chocolates and related merchandise are sold within many stores throughout Australia as an alternative to Easter bunnies. The first documented use of the Easter Bilby concept was in March 1968 when a 9-year-old girl Rose- Marie Dusting, wrote a story, "Billy The Aussie Easter Bilby," which she published as a book 11 years later. The story helped catalyse the public's interest in saving the bilby.
There are a number of mechanisms of ice nucleation in the atmosphere through which ice nuclei can catalyse the formation of ice particles. In the upper troposphere, water vapor can deposit directly onto solid particle. In clouds warmer than about −37 °C where liquid water can persist in a supercooled state, ice nuclei can trigger droplets to freeze. Contact nucleation can occur if an ice nucleus collides with a supercooled droplet, but the more important mechanism of freezing is when an ice nucleus becomes immersed in a supercooled water droplet and then triggers freezing.
This system has allowed researchers to manipulate a variety of genetically modified organisms to control gene expression, delete undesired DNA sequences and modify chromosome architecture. The Cre protein is a site-specific DNA recombinase that can catalyse the recombination of DNA between specific sites in a DNA molecule. These sites, known as loxP sequences, contain specific binding sites for Cre that surround a directional core sequence where recombination can occur. A diagram describing how Lox71 and Lox66 sites can be used to combine two plasmids into one contiguous plasmid.
The Coleman Institute for Cognitive Disabilities was established in 2001, and dedicates its advanced development and research capacities towards the improvement of the afflicted, and exists solely to catalyse and integrate advances in science, engineering and technology to promote the quality of life and independent living of those with cognitive disabilities.Coleman Institutes Welcome Page. Coleman Institute for Cognitive Disabilities, accessed December 22, 2010. Their original endowment towards the institute was a sum of $250 million, and they have continued their donations towards the annually to further its programs and research projects.
Aluminium chloride finds a wide variety of other applications in organic chemistry.Galatsis, P. (1999) Handbook of Reagents for Organic Synthesis: Acidic and Basic Reagents, H. J. Reich, J. H. Rigby (eds.) Wiley, New York City. pp. 12–15. . For example, it can catalyse the "ene reaction", such as the addition of 3-buten-2-one (methyl vinyl ketone) to carvone: :400px It is used to induce a variety of hydrocarbon couplings and rearrangements. Aluminium chloride combined with aluminium in the presence of an arene can be used to synthesize bis(arene) metal complexes, e.g.
Two thioether bonds of cysteine residues bind to the vinyl sidechains of heme, and the histidine residue coordinates one axial binding site of the heme iron. Less common binding motifs can include a single thioether linkage, a lysine or a methionine instead of the axial histidine or a CXnCH binding motif with n>2. The second axial site of the iron can be coordinated by amino acids of the protein, substrate molecules or water. Cytochromes c possess a wide range of properties and function as electron transfer proteins or catalyse chemical reactions involving redox processes.
The 2-oxoglutarate (2OG)-dependent oxygenases are a superfamily of non-haem iron dependent oxygenases, most of which use the Krebs cycle intermediate, 2OG, as a co-substrate. The group are interested in understanding these enzymes for their ability to catalyse synthetically difficult or 'impossible' reactions (e.g. the stereoselective hydroxylation of unactivated carbon- hydrogen bonds), for their diverse physiological roles, and for their links to disease. The research focuses on members of the family that are linked to disease, or can be targeted for the treatment of disease.
One niche use of CrCl3 in organic synthesis is for the in situ preparation of chromium(II) chloride, a reagent for the reduction of alkyl halides and for the synthesis of (E)-alkenyl halides. The reaction is usually performed using two moles of CrCl3 per mole of lithium aluminium hydride, although if aqueous acidic conditions are appropriate zinc and hydrochloric acid may be sufficient. :500px Chromium(III) chloride has also been used as a Lewis acid in organic reactions, for example to catalyse the nitroso Diels- Alder reaction.
Most metals catalyse HDS, but it is those at the middle of the transition metal series that are most active. Although not practical, ruthenium disulfide appears to be the single most active catalyst, but binary combinations of cobalt and molybdenum are also highly active.Chianelli, R. R.; Berhault, G.; Raybaud, P.; Kasztelan, S.; Hafner, J. and Toulhoat, H., "Periodic trends in hydrodesulfurization: in support of the Sabatier principle", Applied Catalysis, A, 2002, volume 227, pages 83-96. Aside from the basic cobalt-modified MoS2 catalyst, nickel and tungsten are also used, depending on the nature of the feed.
Among this group are the metal selective deoxyribozymes such as Pb2+-specific 17E, UO22+-specific 39E, and Na+-specific A43. First crystal structure of a DNAzyme was reported in 2016. 10-23 core based DNAzymes and the respective MNAzymes that catalyse reactions at ambient temperatures were described in 2018 and open doors for use of these nucleic acid based enzymes for many other applications without the need for heating. This link and this link describe the DNA molecule 5'-GGAGAACGCGAGGCAAGGCTGGGAGAAATGTGGATCACGATT-3' , which acts as a deoxyribozyme that uses light to repair a thymine dimer, using serotonin as cofactor.
Prenylated flavin mononucleotide (prFMN) is a cofactor produced by the flavin prenyltransferase UbiX and utilised by UbiD enzymes in their function as reversible decarboxylases. Hence, prFMN is pivotal for catalysis in the ubiquitous microbial UbiDX system. prFMN is flavin prenylated at the N5 and C6 positions resulting in the formation of a fourth non-aromatic ring (Figure 1) prFMN was discovered in 2015 in the University of Manchester by David Leys’ group. upright=2 Two studies in 2015 characterised UbiX as a flavin prenyltransferase, supplying prFMN to UbiD/Fdc1 which utilises the cofactor to catalyse a reversible decarboxylation reaction.
In enzymology, a K+-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + K+out ADP + phosphate + K+in The 3 substrates of this enzyme are ATP, H2O, and K+, whereas its 3 products are ADP, phosphate, and K+. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (K+-importing). Other names in common use include K+-translocating Kdp-ATPase, and multi-subunit K+-transport ATPase. This enzyme participates in two-component system - general.
In enzymology, a xenobiotic-transporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + xenobioticin \rightleftharpoons ADP + phosphate + xenobioticout The 3 substrates of this enzyme are ATP, H2O, and xenobiotic, whereas its 3 products are ADP, phosphate, and xenobiotic. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (xenobiotic-exporting). Other names in common use include multidrug-resistance protein, MDR protein, P-glycoprotein, pleiotropic-drug-resistance protein, PDR protein, steroid- transporting ATPase, and ATP phosphohydrolase (steroid-exporting).
In enzymology, a Zn2+-exporting ATPase () is an enzyme that catalyzes the chemical reaction :ATP + H2O + Zn2+in \rightleftharpoons ADP + phosphate + Zn2+out The 3 substrates of this enzyme are ATP, H2O, and Zn2+, whereas its 3 products are ADP, phosphate, and Zn2+. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (Zn2+-exporting). Other names in common use include Zn(II)-translocating P-type ATPase, P1B-type ATPase, and AtHMA4 (the A. thaliana protein).
Protein tyrosine (pTyr) phosphorylation is a common post-translational modification which can create novel recognition motifs for protein interactions and cellular localisation, affect protein stability, and regulate enzyme activity. Consequently, maintaining an appropriate level of protein tyrosine phosphorylation is essential for many cellular functions. Tyrosine-specific protein phosphatases (PTPase; EC) catalyse the removal of a phosphate group attached to a tyrosine residue, using a cysteinyl-phosphate enzyme intermediate. These enzymes are key regulatory components in signal transduction pathways (such as the MAP kinase pathway) and cell cycle control, and are important in the control of cell growth, proliferation, differentiation and transformation.
Lewis acids are used to catalyse a wide variety of reactions. The mechanism steps are: # Lewis acid forms a polar coordinate with a basic site on the reactant (such as an O or N) # Its electrons are drawn towards the catalyst, thus activating the reactant # The reactant is then able to be transformed by a substitution reaction or addition reaction # The product dissociates and catalyst is regenerated Common Lewis acids include aluminium chloride, ferric chloride and boron trifluoride. These reactions are usually carried out in organic solvents; AlCl3, for example, reacts violently with water. Typical solvents are dichloromethane and benzene.
In the years following the war, Sieger worked in both the UK and US as a consultant for a number of companies in various industries. But upon returning to the UK in 1956, Sieger realised that his time would be better spent focusing on developing his own ideas and innovations, and selling them to companies with manufacturing capabilities. During his time on the south coast working on radar, Sieger had developed an interest in boating and had acquired a number of friends with yachts and vessels. It was this interest that would catalyse the next chapter in his life story.
Polyphenol oxidase (PPO; also polyphenol oxidase i, chloroplastic), an enzyme involved in fruit browning, is a tetramer that contains four atoms of copper per molecule, and binding sites for two aromatic compounds and oxygen. PPO may accept monophenols and/or o-diphenols as substrates. The enzyme works by catalyzing the o-hydroxylation of monophenol molecules in which the benzene ring contains a single hydroxyl substituent to o-diphenols (phenol molecules containing two hydroxyl substituents at the 1, 2 positions, with no carbon between). It can also further catalyse the oxidation of o-diphenols to produce o-quinones.
DUBs are categorised into 5 main groups, ubiquitin-specific proteases (USP), ubiquitin c-terminal hydrolases (UCH), ovarian tumour proteases (OTU), Machado-Joseph disease proteases (MJD), and JAB1/MPN/MOV34 proteases (JAMM/MPN+). The first four groups are cysteine proteases, whereas the last group are Zn metalloproteases. USP20 belongs to the USP group and, like most DUBs, catalyse the breakage of an isopeptide bond between a lysine residue of the target protein and the terminal glycine residue of a ubiquitin protein. This occurs via a conserved cysteine and histidine residue in the catalytic site of the enzyme.
Todd describes her "Eureka moment", "It all began when Elisa joined my group at Johnson & Johnson Research (JJR), we were already exploring ways to exploit DNAzymes (deoxyribozymes) for diagnostic applications. These fascinating molecules are simple, short, synthetic DNA sequences (oligonucleotides) that can catalyse reactions in a manner analogous to protein enzymes. Although catalytic RNA (ribozymes) had been found in nature, catalytic DNA had not, and it had been assumed DNA would not have similar properties. However, a few years earlier, undeterred by dogma, Jerry Joyce and co-workers at Scripps had conducted ‘evolution in a test tube’".
Whereas promiscuity is mainly studied in terms of standard enzyme kinetics, drug binding and subsequent reaction is a promiscuous activity as the enzyme catalyses an inactivating reaction towards a novel substrate it did not evolve to catalyse. This could be because of the demonstration that there are only a small number of distinct ligand binding pockets in proteins. Mammalian xenobiotic metabolism, on the other hand, was evolved to have a broad specificity to oxidise, bind and eliminate foreign lipophilic compounds which may be toxic, such as plant alkaloids, so their ability to detoxify anthropogenic xenobiotics is an extension of this.
Sphingomyelin phosphodiesterase D (, sphingomyelinase D) is an enzyme of the sphingomyelin phosphodiesterase family with systematic name sphingomyelin ceramide-phosphohydrolase. These enzymes catalyse the hydrolysis of sphingomyelin, resulting in the formation of ceramide 1-phosphate and choline: : sphingomyelin + H2O \rightleftharpoons ceramide 1-phosphate + choline or the hydrolysis of 2-lysophosphatidylcholine to give choline and 2-lysophosphatidate. Sphingomyelin phosphodiesterase D activity is shared by enzymes with a wider substrate range, classified as phospholipases D or lipophosphodiesterase II . Sphingomyelinases D are produced by some spiders in their venoms, specifically the brown recluse (loxosceles reclusa), by arthropods such as ticks, or pathogenic bacteria and fungi.
With primary amines, thionyl chloride gives sulfinylamine derivatives (RNSO), one example being N-sulfinylaniline. Thionyl chloride reacts with primary formamides to form isocyanides and with secondary formamides to give chloroiminium ions; as such a reaction with dimethylformamide will form the Vilsmeier reagent. By an analogous process primary amides will react with thionyl chloride to form imidoyl chlorides, with secondary amides also giving chloroiminium ions. These species are highly reactive and can be used to catalyse the conversion of carboxylic acids to acyl chlorides, they are also exploited in the Bischler–Napieralski reaction as a means of forming isoquinolines.
Ubiquitination is the process of chemically attaching ubiquitin monomers to a protein, thereby targeting it for degradation. As this is a multi-step process, several different enzymes are involved, the final one being a member of the E3 family of ligases. Cbl functions as an E3 ligase, and therefore is able to catalyse the formation of a covalent bond between ubiquitin and Cbl's protein substrate - typically a receptor tyrosine kinase. The RING-finger domain mediates this transfer, however like other E3 ligases of the RING type no intermediate covalent bond is formed between ubiquitin and the RING-finger domain.
Hyaluronidases are a family of enzymes that catalyse the degradation of hyaluronic acid (HA). Karl Meyer classified these enzymes in 1971, into three distinct groups, a scheme based on the enzyme reaction products. The three main types of hyaluronidases are two classes of eukaryotic endoglycosidase hydrolases and a prokaryotic lyase-type of glycosidase. In humans, there are five functional hyaluronidases: HYAL1, HYAL2, HYAL3, HYAL4 and HYAL5 (also known as SPAM1 or PH-20); plus a pseudogene, HYAL6 (also known as HYALP1). The genes for HYAL1-3 are clustered in chromosome 3, while HYAL4-6 are clustered in chromosome 7.
The NHL repeat, named after ncl-1, HT2A and lin-41, is an amino acid sequence found largely in a large number of eukaryotic and prokaryotic proteins. For example, the repeat is found in a variety of enzymes of the copper type II, ascorbate-dependent monooxygenase family which catalyse the C-terminus alpha- amidation of biological peptides. In many it occurs in tandem arrays, for example in the RING finger beta-box, coiled-coil (RBCC) eukaryotic growth regulators. The arthropod 'Brain Tumor' protein (Brat; ) is one such growth regulator that contains a 6-bladed NHL-repeat beta-propeller.
Contrary to the above definition, which applies to the field of Artificial chemistry, no agreed-upon notion of autocatalytic sets exists today. While above, the notion of catalyst is secondary insofar that only the set as a whole has to catalyse its own production, it is primary in other definitions, giving the term "Autocatalytic Set" a different emphasis. There, every reaction (or function, transformation) has to be mediated by a catalyst. As a consequence, while mediating its respective reaction, every catalyst denotes its reaction, too, resulting in a self denoting system, which is interesting for two reasons.
Asparagine peptide lyase are one of the seven groups in which proteases, also termed proteolytic enzymes, peptidases, or proteinases, are classified according to their catalytic residue. The catalytic mechanism of the asparagine peptide lyases involves an asparagine residue acting as nucleophile to perform a nucleophilic elimination reaction, rather than hydrolysis, to catalyse the breaking of a peptide bond. The existence of this seventh catalytic type of proteases, in which the peptide bond cleavage occurs by self-processing instead of hydrolysis, was demonstrated with the discovery of the crystal structure of the self-cleaving precursor of the Tsh autotransporter from E. coli.
Hitler had been appointed Chancellor of Germany only four weeks previously, on 30 January 1933, when he was invited by President von Hindenburg to lead a coalition government. Hitler's government had urged von Hindenburg to dissolve the Reichstag and to call elections for 5 March. On the evening of 27 February 1933—six days before the parliamentary election—fire broke out in the Reichstag chambers. While the exact circumstances of the fire remain unclear to this day, what is clear is that Hitler and his supporters quickly capitalized on the fire as a means by which to catalyse their consolidation of power.
This enzyme catalyses the first step in the biosynthesis of histidine in bacteria, fungi and plants. It is a member of the larger phosphoribosyltransferase superfamily of enzymes which catalyse the condensation of 5-phospho-alpha-D-ribose 1-diphosphate with nitrogenous bases in the presence of divalent metal ions. Histidine biosynthesis is an energetically expensive process and ATP phosphoribosyltransferase activity is subject to control at several levels. Transcriptional regulation is based primarily on nutrient conditions and determines the amount of enzyme present in the cell, while feedback inhibition rapidly modulates activity in response to cellular conditions.
Alcohol dehydrogenases (ADHs) and retinal dehydrogenase (RALDH) enzymes catalyse the oxidation of dietary vitamin A to retinoic acid. It is the presence of this retinoic acid which induces the expression of CCR9 and α4β7. Lower concentrations of retinoic acid, inside the cell, result in a decreased expression of the chemokine receptor CCR9 which in turn limits the ability of the cell to enter the gut mucosa. While the expression of α4β7 is also reduced under lower retinoic acid concentrations, it is predicted that the retinoic acid levels must be depleted to a greater extent to affect α4β7 expression compared to CCR9.
Structures of both proteins have been determined by X-ray crystallography; however, the location and mechanism of the active site in pMMO is still poorly understood and is an area of active research. The particulate methane monooxygenase and related ammonia monooxygenase are integral membrane proteins, occurring in methanotrophs and ammonia oxidisers, respectively, which are thought to be related. These enzymes have a relatively wide substrate specificity and can catalyse the oxidation of a range of substrates including ammonia, methane, halogenated hydrocarbons, and aromatic molecules. These enzymes are homotrimers composed of 3 subunits - A (), B () and C () and most contain two monocopper centers.
Similarly, DFP also reacts with the active site of acetylcholine esterase in the synapses of neurons, and consequently is a potent neurotoxin, with a lethal dose of less than 100 mg. Suicide inhibition is an unusual type of irreversible inhibition where the enzyme converts the inhibitor into a reactive form in its active site. An example is the inhibitor of polyamine biosynthesis, α-difluoromethylornithine or DFMO, which is an analogue of the amino acid ornithine, and is used to treat African trypanosomiasis (sleeping sickness). Ornithine decarboxylase can catalyse the decarboxylation of DFMO instead of ornithine, as shown above.
In molecular biology, the HMG-CoA reductase family is a family of enzymes which participate in the mevalonate pathway, the metabolic pathway that produces cholesterol and other isoprenoids. There are two distinct classes of hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase enzymes: class I consists of eukaryotic and most archaeal enzymes , while class II consists of prokaryotic enzymes . Class I HMG-CoA reductases catalyse the NADP-dependent synthesis of mevalonate from 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA). In vertebrates, membrane-bound HMG-CoA reductase is the rate-limiting enzyme in the biosynthesis of cholesterol and other isoprenoids.
Without the secondary loop provided by catalysis, I chains would compete and select against each other instead of cooperating. The reproduction is possible thanks to translation and polymerization functions encoded in I chains. In his principal work, Manfred Eigen stated that the E coded by the I chain can be a specific polymerase or an enhancer (or a silencer) of a more general polymerase acting in favour of formation of the successor of nucleotide chain I. Later, he indicated that a general polymerase leads to the death of the system. Moreover, the whole cycle must be closed, so that En must catalyse I1 formation for some integer n > 1.
The Council manages a suite of interlinked programmes funding researchers across all career stages and disciplines. It is the key national funder of basic research across all disciplines, and the only national funder that supports basic research in the arts, humanities and social sciences. The Council supports the career development of early-stage researchers; power enterprise and skills; cultivate Ireland's success under Horizon 2020; catalyse research addressing the grand societal challenges; provide access to research infrastructures and; communicate the value of research. Selection for funding is based upon individual merit, and the decision process is overseen by independent assessment panels composed by internationally recognised experts.
However, unlike uncatalysed chemical reactions, enzyme-catalysed reactions display saturation kinetics. For a given enzyme concentration and for relatively low substrate concentrations, the reaction rate increases linearly with substrate concentration; the enzyme molecules are largely free to catalyse the reaction, and increasing substrate concentration means an increasing rate at which the enzyme and substrate molecules encounter one another. However, at relatively high substrate concentrations, the reaction rate asymptotically approaches the theoretical maximum; the enzyme active sites are almost all occupied by substrates resulting in saturation, and the reaction rate is determined by the intrinsic turnover rate of the enzyme.Fromm H.J., Hargrove M.S. (2012) Enzyme Kinetics.
Structure of Heme D. Cytochrome d is, as other proteins of its family, a membrane-bound hemeprotein, but unlike cytochromes a and b, cytochrome D has a heme D instead of a heme A or heme B group. Cytochrome d is part of the cytochrome bd terminal oxidase which catalyse the two electron oxidation of ubiquinol. This process is an oxidative phosphorylation that oxidizes the ubiquinol-8 to ubiquinone. The chemical reaction followed by this process is: :Ubiquinol-8 + O2 -> Ubiquinone-8 + H2OCytochrome d ubiquinol oxidase subunit 1 By a similar reaction, it also catalyses the reduction of oxygen to water, which involves 4 electrons.
ERN Bridge, is a virtual bridge set up in hopes to close the gap between the needs of the vast numbers of rewilding initiatives with students and volunteers searching to gain experience by working in nature conservation and rewilding. Direct access to Rewilding Europe Capital (REC), Europe's first ‘rewilding enterprise’ funding facility that provides financial loans to new and existing business that catalyse, support and achieve positive environmental and socio-economic outcomes that support rewilding in Europe. ERN members are eligible for a direct access to European Wildlife Bank, a tool designed to facilitate the reintroduction and restocking of herbivores to rewilding areas across the European continent.
The L-arabinose operon, also called the ara or araBAD operon, is an operon required for the breakdown of the five-carbon sugar L-arabinose in Escherichia coli. The L-arabinose operon contains three structural genes: araB, araA, araD (collectively known as araBAD), which encode for three metabolic enzymes that are required for the metabolism of L-arabinose. AraB (ribulokinase), AraA (an isomerase), AraD (an epimerase) produced by these genes catalyse conversion of L-arabinose to an intermediate of the pentose phosphate pathway, D-xylulose-5-phosphate. The structural genes of the L-arabinose operon are transcribed from a common promoter into a single transcript, a mRNA.
Because of the property of Ero1p to transfer electrons directly to molecular oxygen via a flavin-dependent reaction, its activity may produce reactive oxygen species (ROS). In bacteria, this problem is solved by coupling oxidative folding to the respiratory chain. There, the reduction of molecular oxygen to water is carried out by a complex series of proteins, which catalyse this reaction very efficiently. In eukaryotes, the respiratory chain is separated from oxidative folding since cellular respiration takes place in the mitochondria and the formation of disulfide bonds occurs in the ER. Because of this, there is much more risk that ROS are produced in eukaryotic cells during oxidative folding.
Incubation of SAM and chloride ion with the fluorinase does not result in generation of 5'-chloro-5'-deoxyadenosine (ClDA), unless an additional enzyme, an L-amino acid oxidase, is added. The amino acid oxidase removes the L-methionine from the reaction, converting it to the corresponding oxo-acid. The fluorinase can also catalyse the reaction between chloride ion and the co-factor S-adenosyl-L-methioinine (SAM) to generate 5'-chloro-5'-deoxyadenosine (ClDA) and L-methionine (L-Met). The reaction only proceeds when L-methionine is removed from the reaction by an L-amino acid oxidase, driving the reaction equilibrium towards ClDA.
Ubiquitin carboxyl-terminal hydrolase 20 is an enzyme that in humans is encoded by the USP20 gene. Ubiquitin-specific protease 20 (USP20), also known as ubiquitin-binding protein 20 and VHL protein-interacting deubiquitinating enzyme 2 (VDU2), is a cysteine protease deubiquitinating enzyme (DUB). The catalytic site of USP20, like other DUBs, contains conserved cysteine and histidine residues that catalyse the proteolysis of an isopeptide bond between a lysine residue of a target protein and a glycine residue of a ubiquitin molecule. USP20 is known to deubiquitinate a number of proteins including thyronine deiodinase type 2 (D2), Hypoxia-inducible factor 1α (HIF1α), and β2 adrenergic receptor (β2AR).
Transition state analogue example one Methylthioadenosine nucleosidase are enzymes that catalyse the hydrolytic deadenylation reaction of 5'-methylthioadenosine and S-adenosylhomocysteine. It is also regarded as an important target for antibacterial drug discovery because it is important in the metabolic system of bacteria and only produced by bacteria. Given the different distance between nitrogen atom of adenine and the ribose anomeric carbon (see in the diagram in this section), the transition state structure can be defined by early or late dissociation stage. Based on the finding of different transition state structures, Schramm and coworkers designed two transition state analogues mimicking the early and late dissociative transition state.
Vanadium bromoperoxidases have been found in bacteria, fungi, marine macroalgae (seaweeds), and marine microalgea (diatoms) which produce brominated organic compounds. It has not been definitively identified as the bromoperoxidase of higher eukaryotes, such as murex snails, which have a very stable and specific bromoperoxidase, but perhaps not a vanadium dependent one. While the purpose of the bromoperoxidase is still unknown, the leading theories include that it’s a way of regulating hydrogen peroxide produced by photosynthisis and/or as a self-defense mechanism by producing hypobromic acid which prevents the growth of bacteria. The enzymes catalyse the oxidation of bromide (0.0067% of sea water) by hydrogen peroxide.
The nucleotide adenosine is present in cofactors that catalyse many basic metabolic reactions such as methyl, acyl, and phosphoryl group transfer, as well as redox reactions. This ubiquitous chemical scaffold has, therefore, been proposed to be a remnant of the RNA world, with early ribozymes evolving to bind a restricted set of nucleotides and related compounds. Adenosine-based cofactors are thought to have acted as interchangeable adaptors that allowed enzymes and ribozymes to bind new cofactors through small modifications in existing adenosine-binding domains, which had originally evolved to bind a different cofactor. This process of adapting a pre-evolved structure for a novel use is known as exaptation.
Serine C-palmitoyltransferase is a member of the AOS (a-oxoamine synthase) family of PLP-dependent enzymes, which catalyse the condensation of amino acids and acyl-CoA thioester substrates. The human enzyme is a heterodimer consisting of two monomeric subunits known as long chain base 1 and 2 (LCB1/2) encoded by separate genes. The active site of LCB2 contains lysine and other key catalytic residues that are not present in LCB1, which does not participate in catalysis but is nevertheless required for the synthesis and stability of the enzyme. As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
Carpentier contributed $250,000 to an endowment that initiated Chinese studies at Columbia University and helped to catalyse broader East Asian studies at the university. This was done in honor of his valet , who in 1902 had contributed $12,000 of his savings to the establishment of Chinese Studies at Columbia. In the same year, sinologist Friedrich Hirth was appointed the first Dean Lung professor of Chinese, soon receiving a substantial collection of books from the Chinese government. To mark the establishment of the foundation of the Dean Lung Chair of Chinese at Columbia, Herbert Giles gave a series of lectures titled "China and the Chinese".
Recently, Leigh and co- workers described a new pathway to mechanically interlocked architectures involving a transition-metal center that can catalyse a reaction through the cavity of a macrocycle. (a) A rotaxane is formed from an open ring (R1) with a flexible hinge and a dumbbell-shaped DNA origami structure (D1). The hinge of the ring consists of a series of strand crossovers into which additional thymines are inserted to provide higher flexibility. Ring and axis subunits are first connected and positioned with respect to each other using 18 nucleotide long, complementary sticky ends 33 nm away from the center of the axis (blue regions).
The metallo-beta-lactamase protein fold is a protein domain contained in class B beta-lactamases and a number of other proteins. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor. Metallo-beta-lactamases are important enzymes because they are involved in the breakdown of antibiotics by antibiotic-resistant bacteria.
As the origin of the fragments and their name implies, they have a twofold effect: first, just as in R.E.M. sleep, these brain-stem fragments essentially activate the dream mechanism. Second, they do catalyse a near- waking state. However, this spark is often not powerful enough to jar us completely out of deep sleep, and so only our mind fully awakens, leaving our body trapped in the atonia of deep sleep. Another reason why hypnopompic hallucinations are often such horrible experiences, is because micro-wake fragments appear to be related to serotonin and dopamine deficits—these deficits predispose us to negative mental states, which likely causes the hallucinations to resemble our worst dreams.
In molecular biology, the trappin protein transglutaminase binding domain or cementoin is a protein domain found at the N-terminus of Whey Acidic Protein (WAP) domain-containing protease inhibitors such as trappin-2. This N-terminal domain enables it to become cross-linked to extracellular matrix proteins by transglutaminase. This domain contains several repeated motifs with the consensus sequence Gly-Gln-Asp-Pro-Val-Lys, and these together can anchor the whole molecule to extracellular matrix proteins, such as laminin, fibronectin, beta-crystallin, collagen IV, fibrinogen, and elastin, by transglutaminase- catalysed cross-links. The whole domain is rich in glutamine and lysine, thus allowing transglutaminase(s) to catalyse the formation of an intermolecular epsilon-(gamma-glutamyl)lysine isopeptide bond.
Upon nucleotide hydrolysis the loop does not significantly change the protein conformation, but stays bound to the remaining phosphate groups. Walker motif A-binding has been shown to cause structural changes in the bound nucleotide, along the line of the induced fit model of enzyme binding. PTPs (protein tyrosine phosphatases) that catalyse the hydrolysis of an inorganic phosphate from a phosphotyrosine residue (the reverse of a tyrosine kinase reaction) contain a motif which folds into a P-loop-like structure with an arginine in the place of the conserved lysine. The conserved sequence of this motif is C-x(5)-R-[ST], where C and R denote cysteine and arginine residues respectively.
Workers Aid never saw itself as a charity, but as a campaigning organisation aiming to catalyse a response from the broader labour movement across Europe. The group continued its work in the former Yugoslavia, first visiting Kosovo in January 1996. Under its new name, Workers Aid for Kosova (Kosova is the Albanian name of Kosovo), it was one of the first organisations to take aid to Kosovo during the NATO intervention of July 1999. During July and August of that year they supported miners in and around Kosovska Mitrovica and Pristina, and - with support from the Students' Representative Council of the University of Aberdeen together with Aid Convoy - supplied the students' union of the University of Pristina.
The 407 residue, 46 kDa, protein eIF4A is the prototypical member of the DEAD box helicase family, so-called due to their conserved four-residue D-E-A-D sequence. This family of helicases is found in a range of prokaryotic and eukaryotic organisms including humans, wherein they catalyse a variety of processes including embryogenesis and RNA splicing as well as translation initiation. Crystallographic analysis of yeast eIF4A carried out by Carruthers et al. (2000) revealed that the molecule is approximately 80 Å in length and has a “dumbbell” shape where the proximal section represents an 11 residue (18 Å) linker postulated to confer a degree of flexibility and distension to the molecule in solution.
The UGTs serve a major role in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. UGT2B7 has unique specificity for 3,4-catechol estrogens and estriol, suggesting that it may play an important role in regulating the level and activity of these potent estrogen metabolites. This enzyme is located on the endoplasmic reticulum and nuclear membranes of cells. Its function is to catalyse the conjugation of a wide variety of lipophilic aglycon substrates with glucuronic acid, using uridine diphosphate glucuronic acid. Together with UGT2B4, UGT2B7 is capable of glucosidation of hyodesoxycholic acid in the liver, but, unlike the 2B4 isoform, 2B7 is also able to glucuronidate various steroid hormones (androsterone, epitestosterone) and fatty acids.
A protein phosphatase is a phosphatase enzyme that removes a phosphate group from the phosphorylated amino acid residue of its substrate protein. Protein phosphorylation is one of the most common forms of reversible protein posttranslational modification (PTM), with up to 30% of all proteins being phosphorylated at any given time. Protein kinases (PKs) are the effectors of phosphorylation and catalyse the transfer of a γ-phosphate from ATP to specific amino acids on proteins. Several hundred PKs exist in mammals and are classified into distinct super-families. Proteins are phosphorylated predominantly on Ser, Thr and Tyr residues, which account for 79.3, 16.9 and 3.8% respectively of the phosphoproteome, at least in mammals.
Phosphorylation involves the transfer of phosphate groups from ATP to the enzyme, the energy for which comes from hydrolysing ATP into ADP or AMP. However, dephosphorylation releases phosphates into solution as free ions, because attaching them back to ATP would require energy input. Cysteine- dependent phosphatases (CDPs) catalyse the hydrolysis of a phosphoester bond via a phospho-cysteine intermediate. Mechanism of Tyrosine dephosphorylation by a CDP The free cysteine nucleophile forms a bond with the phosphorus atom of the phosphate moiety, and the P-O bond linking the phosphate group to the tyrosine is protonated, either by a suitably positioned acidic amino acid residue (Asp in the diagram below) or a water molecule.
The other helices were not found to host residues critical for catalytic activity, and may serve in structural roles. Mycobacterium tuberculosis bifunctional histidine/tryptophan biosynthesis isomerase (PriA) () possesses the ability to catalyse two reactions: (i) HisA reaction: the conversion of N-[(5-phosphoribosyl) formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (ProFAR) to N-[(5-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR), and (ii) TrpF reaction: N-(5’-phosphoribosyl)-anthranilate (PRA) to 1-(O-carboxyphenylamino)- 1’-deoxyribulose-5’-phosphate (CdRP). PriA is a TIM barrel enzyme that accommodates both substrates using active site loops (loops 1, 5, and 6, extended βα loops at the C-terminal end of the β-barrel) that change conformation depending on the reactant present.
Amine oxidase (copper-containing) (AOC) ( and ; formerly ) is a family of amine oxidase enzymes which includes both primary-amine oxidase and diamine oxidase; these enzymes catalyze the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. They act as a disulphide-linked homodimer. They catalyse the oxidation of primary amines to aldehydes, with the subsequent release of ammonia and hydrogen peroxide, which requires one copper ion per subunit and topaquinone as cofactor: :RCH2NH2 \+ H2O + O2 \rightleftharpoons RCHO + NH3 \+ H2O2 The 3 substrates of this enzyme are primary amines (RCH2NH2), H2O, and O2, whereas its 3 products are RCHO, NH3, and H2O2. Copper-containing amine oxidases are found in bacteria, fungi, plants and animals.
Whilst many FANC protein mutations account for only 1% of the total observed cases, they are also stabilized by FANCA within the complex. For example, FANCA stabilises FANCG within the core complex, and hence mutations in FANCG are compensated for as the complex can still catalyse FANCD2-ubiquitination further downstream. FANCA upregulation also increases expression of FANCG in cells, and the fact this transduction is not mutual – FANCG upregulation does not cause increased expression of FANCA – suggests that FANCA is not only the primary stabilizing protein in the core complex, but may act as a natural regulator in patients who would otherwise suffer from mutations in FANC genes other than FANCA or FANCD2.
The resulting peroxyflavin is the catalytic entity oxygenating the substrate, and theoretical studies suggest that the reaction proceeds through the same Criegee intermediate as observed in the chemical reaction. After the rearrangement step forming the ester product, a hydroxyflavin remains, which spontaneously eliminates water to form oxidized flavin, thereby closing the catalytic cycle. BVMOs are closely related to the flavin-containing monooxygenases (FMOs), enzymes that also occur in the human body, functioning within the frontline metabolic detoxification system of the liver along the cytochrome P450 monooxygenases. Human FMO5 was in fact shown to be able to catalyse Baeyer-Villiger reactions, indicating that the reaction may occur in the human body as well.
In this Dictionary the termination is uniformly written ize. (In > the Greek -, the i was short, so originally in Latin, but the double > consonant z (= dz, ts) made the syllable long; when the z became a simple > consonant, /idz/ became īz, whence English /aɪz/.) The Oxford use of ize does not extend to the spelling of words not traced to the Greek izo suffix. One group of such words is those ending in lyse, such as analyse, paralyse and catalyse, which come from the Greek verb , lyo, the perfective (aorist) stem of which is lys-: for these lyse is the more etymological spelling. Others include arise, chastise, disguise, prise (in the sense of open), and televise, though the last is a hybrid word.
After one or several turnovers the enzyme becomes active and can catalyse physiological NADH:ubiquinone reaction at a much higher rate (k~104 min−1). In the presence of divalent cations (Mg2+, Ca2+), or at alkaline pH the activation takes much longer. The high activation energy (270 kJ/mol) of the deactivation process indicates the occurrence of major conformational changes in the organisation of the complex I. However, until now, the only conformational difference observed between these two forms is the number of cysteine residues exposed at the surface of the enzyme. Treatment of the D-form of complex I with the sulfhydryl reagents N-Ethylmaleimide or DTNB irreversibly blocks critical cysteine residue(s), abolishing the ability of the enzyme to respond to activation, thus inactivating it irreversibly.
Azerbaijan has more than 35 scientific institutions that provide scientific investigations in the fields of social sciences, humanitarian sciences, medical-biological sciences, chemical sciences, earth sciences and technical sciences etc. Institution of Information Technology, Institute of Radiation problems, Astrophysical Observatory named after Nasreddin Tusi, Institute of Control Systems, Institute of Mathematics and Mechanics and Institute of Physics provide researches in the field of Physics, Mathematics and Technical Sciences. İnstitute of Catalyse and Inorganic Chemistry, Institute of Polymer materials, Institute of Petrochemical Processes and Institute of Chemical Additives acts under the Department of Chemical Sciences. Other scientific institutions include the Institute of Geography, Institute of Geology and Geophysics, Institute of Oil and Gas, which generate scientific researches under the Department of Earth Sciences.
To save money during construction, stainless steel bolts were used to secure the external aluminium panels in place; however, this resulted in galvanic corrosion of the more reactive aluminium, so the bolts have been replaced by aluminium ones. Salts in water catalyse corrosion, a problem for the c2c fleet as they run beside the sea. After repair at Derby Litchurch Lane Works, 357203 was repainted and re-entered service on 30 July 2009. Similar work was carried out on the rest of the fleet over the next 21 months at Bombardier's Ilford Depot, where the units were repainted into their original white colour, but with dark blue doors, and branded with both "national express" and "c2c" logos in lower-case.
First, a new information carrier Inew created by the mutation must be better recognized by one of the hypercycle's members Ii than the chain Ii+1 that was previously recognized by it. Secondly, the new member Inew of the cycle has to better catalyse the formation of the polynucleotide Ii+1 that was previously catalysed by the product of its predecessor Ii. In theory, it is possible to incorporate into the hypercycle mutations that do not satisfy the second condition. They would form parasitic branches that use the system for their own replication but do not contribute to the system as a whole. However, it was noticed that such mutants do not pose a threat to the hypercycle, because other constituents of the hypercycle grow nonlinearly, which prevents the parasitic branches from growing.
Science Week Ireland is an annual week-long event in Ireland each November, celebrating science in our everyday lives. Science Week is an initiative of Science Foundation Ireland (SFI) It is the largest science festival in the country, engaging tens of thousands of members of the general public in workshops, science shows, talks, laboratory demonstrations, science walks and other science-related events. Science Week is a collaboration of events involving industry, colleges, schools, libraries, teachers, researchers and students throughout Ireland. Science Week supports Science Foundation Ireland’s mission to catalyse, inspire and guide the best in science, technology, engineering and maths (STEM) education and public engagement. The ultimate aim of this effort is that Ireland will have the most engaged and scientifically informed public by 2020 as outlined in Science Foundation Ireland’s strategy Agenda 2020.
In March 2014, the Council of Ministers of Higher Education and Scientific Research in the Arab World endorsed the draft Arab Strategy for Science, Technology and Innovation at its 14th congress in Riyadh, Saudi Arabia. The strategy has three main thrusts: academic training in science and engineering, scientific research and regional and international scientific co-operation. One of the strategy's key objectives is to involve the private sector more in regional and interdisciplinary collaboration, in order to add economic and development value to research and make better use of available expertise. Up to now, science, technology and innovation policies in Arab states have failed to catalyse knowledge production effectively or add value to products and services because they focus on developing research without taking the business community on board.
In March 2014, the Council of Ministers of Higher Education and Scientific Research in the Arab World endorsed the draft Arab Strategy for Science, Technology and Innovation at its 14th congress in Riyadh, Saudi Arabia. The strategy has three main thrusts: academic training in science and engineering, scientific research and regional and international scientific co-operation. One of the strategy's key objectives is to involve the private sector more in regional and interdisciplinary collaboration, in order to add economic and development value to research and make better use of available expertise. Up to now, science, technology and innovation policies in Arab states have failed to catalyse knowledge production effectively or add value to products and services because they focus on developing research without taking the business community on board.
Science Week Ireland is an annual week-long event in Ireland each November, celebrating science in our everyday lives. Science Week is an initiative of Science Foundation Ireland (SFI) It is the largest science festival in the country, engaging tens of thousands of members of the general public in workshops, science shows, talks, laboratory demonstrations, science walks and other science-related events. Science Week is a collaboration of events involving industry, colleges, schools, libraries, teachers, researchers and students throughout Ireland. It supports Science Foundation Ireland’s mission to catalyse, inspire and guide the best in science, technology, engineering and maths (STEM) education and public engagement. The ultimate aim of this effort is that Ireland will have the most engaged and scientifically informed public by 2020 as outlined in Science Foundation Ireland’s strategy Agenda 2020.
7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase (, FO synthase) and 5-amino-6-(D-ribitylamino)uracil—L-tyrosine 4-hydroxyphenyl transferase () are two enzymes always complexed together to achieve synthesis of FO, a precursor to Coenzyme F420. Their systematic names are 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil ammonia-lyase (7,8-didemethyl-8-hydroxy-5-deazariboflavin-forming) and 5-amino-6-(D-ribitylamino)uracil:L-tyrosine, 4-hydroxyphenyl transferase respectively. The enzymes catalyse the following chemical reactions: : (2.5.1.147) 5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L- methionine = 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosin : (4.3.1.32) 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl- L-methionine = 7,8-didemethyl-8-hydroxy-5-deazariboflavin + NH3 \+ L-methionine + 5'-deoxyadenosine Enzyme 2.5.
Instead, the still-excited electrons are transferred to a photosystem I complex, which boosts their energy level to a higher level using a second solar photon. The highly excited electrons are transferred to the acceptor molecule, but this time are passed on to an enzyme called Ferredoxin-NADP+ reductase which uses them to catalyse the reaction (as shown): :NADP+ \+ 2H+ \+ 2e− -> NADPH + H+ This consumes the H+ ions produced by the splitting of water, leading to a net production of 1/2O2, ATP, and NADPH+H+ with the consumption of solar photons and water. The concentration of NADPH in the chloroplast may help regulate which pathway electrons take through the light reactions. When the chloroplast runs low on ATP for the Calvin cycle, NADPH will accumulate and the plant may shift from noncyclic to cyclic electron flow.
In an address to The World Economic Forum on 31 January 1999, Secretary-General Annan argued that the "goals of the United Nations and those of business can, indeed, be mutually supportive" and proposed that the private sector and the United Nations initiate "a global compact of shared values and principles, which will give a human face to the global market". On 26 July 2000, the United Nations Global Compact was officially launched at UN headquarters in New York. It is a principle-based framework for businesses which aims to "Catalyse actions in support of broader UN goals, such as the Millennium Development Goals (MDGs)". The Compact established ten core principles in the areas of human rights, labour, the environment and anti-corruption, and under the Compact, companies commit to the ten principles and are brought together with UN agencies, labour groups and civil society to effectively implement them.
Cells can grow by increasing the overall rate of cellular biosynthesis such that production of biomolecules exceeds the overall rate of cellular degradation of biomolecules via the proteasome, lysosome or autophagy. Biosynthesis of biomolecules is initiated by expression of genes which encode RNAs and/or proteins, including enzymes that catalyse synthesis of lipids and carbohydrates. Individual genes are generally expressed via transcription into messenger RNA (mRNA) and translation into proteins, and the expression of each gene occurs to various different levels in a cell-type specific fashion (in response to gene regulatory networks). To drive cell growth, the global rate of gene expression can be increased by enhancing the overall rate of transcription by RNA polymerase II (for active genes) or the overall rate of mRNA translation into protein by increasing the abundance of ribosomes and tRNA, whose biogenesis depends on RNA polymerase I and RNA polymerase III.
The ambitious BFI Institute aims to overcome barriers that prevent capital from flowing to SDG-related projects in emerging markets. The BFI Institute hopes to align global partners to support the incubation of innovative financing for inclusive business and the SDGs, seeks to overcome barriers to investing in high-impact sectors in emerging markets, creates a hub of best practice for developing country infrastructure finance institutions, accelerates on-ground pipeline development (especially for natural solutions, clean energy and circular economy), and convenes leaders around catalytic financial instruments to crowd in commercial investment at scale. The institute will create shared institutional learnings across stakeholders, match-make capital to projects, catalyse leadership and forge new collaboration between public, private, civil society and academia to scale up innovation and investment for sustainable and inclusive development. The BFI Institute is expected to be officially launched in November 2020.
Sir John Warcup Cornforth Jr., AC, CBE, FRS, FAA (7 September 1917 – 8 December 2013) was an AustralianBritish chemist who won the Nobel Prize in Chemistry in 1975 for his work on the stereochemistry of enzyme-catalysed reactions, becoming the only Nobel laureate born in New South Wales. Cornforth investigated enzymes that catalyse changes in organic compounds, the substrates, by taking the place of hydrogen atoms in a substrate's chains and rings. In his syntheses and descriptions of the structure of various terpenes, olefins, and steroids, Cornforth determined specifically which cluster of hydrogen atoms in a substrate were replaced by an enzyme to effect a given change in the substrate, allowing him to detail the biosynthesis of cholesterol.Deaf Scientist Corner – John Warcup Cornforth, Texas Woman's University For this work, he won a share of the Nobel Prize in Chemistry in 1975, alongside co-recipient Vladimir Prelog, and was knighted in 1977.
Deslandres' undergraduate years at the École Polytechnique were played out against the aftermath of the Franco-Prussian War and the chaos of the Paris Commune so, on graduation in 1874, he responded to the continuing military tension with the emerging Germany by embarking on a military career. Rising to the rank of captain in the engineers, he became increasingly interested in physics and, in 1881, resigned his commission to join Alfred Cornu's laboratory at the École Polytechnique, working on spectroscopy. He continued his spectroscopic work at the Sorbonne, earning his doctorate in 1888 and finding numerical patterns in spectral lines that paralleled the work of Johann Balmer and were to catalyse the development of quantum mechanics in the 20th century. In 1868, Pierre Janssen's solar observations had led him to report to the Académie des Sciences that It is no longer geometry and mechanics which dominate [in astronomy] but physics and chemistry.
Establishment of the Kiira Vehicle Plant is expected to catalyse investment by small and medium enterprises in the manufacture of vehicle parts, components and autonomy systems (Brake pads, seats, bolts and nuts, bumpers, vehicle electronics, navigation system, among others). Kiira Motors Corporation has developed a roadmap for the Domestic Manufacture of Auto-Parts in Uganda and secured accreditation from PPDA for an alternative system for procurement of Auto-Parts Suppliers providing for sample parts development and accreditation of the production part manufacturing system. Establishment of the Kiira Vehicle Plant is projected to increase demand for the utilization of Uganda's natural resources such as steel from iron ore deposits; plastics from oil and gas, lithium ion batteries from graphite, lithium and cobalt deposits, vehicle upholstery and interior padding from cotton and leather, glass from silica and sand among others. The Kiira Vehicle Plant's contribution to employment in Uganda is estimated at 940 jobs from the Start-Up Investment.
The social impact bond is a non-tradeable version of social policy bonds, first conceived by Ronnie Horesh, a New Zealand economist, in 1988. Since then, the idea of the social impact bond has been promoted and developed by a number of agencies and individuals in an attempt to address the paradox that investing in prevention of social and health problems saves the public sector money, but that it is currently difficult for public bodies to find the funds and incentives to do so. The first social impact bond was announced in the UK on 18 March 2010 by then Justice Secretary Jack Straw, to finance a prisoner rehabilitation program. In the UK, the Prime Minister's Council on Social Action (a group of ‘innovators from every sector’ brought together to ‘generate ideas and initiatives through which Government and other key stakeholders can catalyse, celebrate and develop social action’) was asked in 2007 to explore alternative models for financing social action.
She established the mechanism of complex I inhibition by the anti-diabetic drug metformin, and has used kinetic and thermodynamic strategies to define how superoxide production by complex I, responds to the intramitochondrial NADH/NAD+ ratio to directly link two pathological effects of complex I dysfunction. This seminal work has brought understanding that is fundamental to critical issues of health and disease on a global stage.' Hirst was awarded Keilin Memorial Lecture and Medal in 2020 for research which 'has made pivotal contributions to understanding energy conversion in complex redox enzymes: how they capture the energy released by a redox reaction to power proton translocation across a membrane, or catalyse the interconversion of chemical bond energy and electrical potential. She is known particularly for her work on mammalian respiratory complex I (NADH: ubiquinone oxidoreductase), an energy-transducing, mitochondrial redox enzyme of fundamental and medical importance, and for solving its structure by electron cryomicroscopy'.
Each reaction can be applied individually or sequentially as dictated by the characteristics of the stream to be treated. The process consist of three main sections: An absorber (gas washing section), a bioreactor (sulfide oxidation and regeneration of washing liquid) and Sulfur handling section as shown in the figure below: The washing step uses a dilute alkaline solution to remove hydrogen sulfide (H2S) from the sour gas according to: :H2S + NaOH → NaHS + H2O The loaded washing liquid is transported to a bioreactor where a biocatalyst oxidises the aqueous NaHS to elemental sulfur with about 95% selectivity according to: :NaHS + ½ O2 → S + NaOH Combined reaction equation: :H2S + ½ O2 → S + H2O The regenerated washing liquid is sent back to the washing column. The controlled partial oxidation of sulfide to elemental sulfur (2) is catalyzed by naturally occurring microorganisms of the genus Halothiobacillus in the bioreactor. These natural, living microorganisms present in the bioreactor catalyse the sulfur conversions and are, by their nature, resilient and adaptive.
As Mayor of Vincent, he advocated for greater transparency and accountability in local government, writing and releasing a public discussion paper "Raising the Bar", and introduced a series of measures to enhance public reporting at the City of Vincent, including an online gifts register and WA's first contact with developers register. During his tenure in 2016 with a new CEO at the helm and council, the City of Vincent was independently rated first among 25 councils, receiving an overall performance score of 82 out of 100, compared to 16th out of 18 councils in 2010.The Catalyse Community Scorecard surveys households across a local government area, and found the City of Vincent ranked highest in 18 out of 40 benchmarks, including place to live, governing organisation, and the city's leadership within the community. On his election at the State Member for Perth, he was appointed the Parliamentary Secretary to the Premier; Minister for Public Sector Management; State Development, Jobs and Trade; Federal-State Relations.
By publishing the outcome in a summary document or report, ECETOC can broadly communicate the defined science gaps related to the issue and catalyse active research programmes which address safety, human health and environmental concerns that have been raised. Supporting the Cefic Long-range Research Initiative (LRI) Cefic LRI Projects under ECETOC Management Since the establishment of the Cefic Long-range Research Initiative (LRI) programme in 1998, ECETOC has been a partner organisation with 3 Key Leadership Roles: Project Proposals These proposals are based on the ability of ECETOC to have multi-stakeholder (industry, regulatory bodies and academia) dialogue and consultation. Project Selection When proposals are received by LRI to address specific projects, ECETOC organises selection teams and, by following a transparent and impartial process, identifies the proposal considered to be the most worthy for receiving LRI funding. Project Management An ECETOC Monitoring Team follows the progress of each LRI project providing help and guidance to the researchers as requested.
BVMOs have been widely studied due to their potential as biocatalysts, that is, for an application in organic synthesis. Considering the environmental concerns for most of the chemical catalysts, the use of enzymes is considered a greener alternative. BVMOs in particular are interesting for application because they fulfil a range of criteria typically sought for in biocatalysis: besides their ability to catalyse a synthetically useful reaction, some natural homologs were found to have a very large substrate scope (i.e. their reactivity was not restricted to a single compound, as often assumed in enzyme catalysis), they can be easily produced on a large scale, and because the three-dimensional structure of many BVMOs has been determined, enzyme engineering could be applied to produce variants with improved thermostability and/or reactivity. Another advantage of using enzymes for the reaction is their frequently observed regio- and enantioselectivity, owed to the steric control of substrate orientation during catalysis within the enzyme’s active site.
Village scene with poultry, sheep and goats from a copy of the Maqamat al-Hariri illustrated by al-Wasiti, 1237 The twelfth century agronomist Abū l-Khayr al-Ishbīlī of Seville described in detail in his Kitāb al-Filāha (Treatise on Agriculture) how olive trees should be grown, grafted (with an account of his own experiments), treated for disease, and harvested, and gave similar detail for crops such as cotton. Medieval Islamic agronomists including Ibn Bassal and Abū l-Khayr described agricultural and horticultural techniques including how to propagate the olive and the date palm, crop rotation of flax with wheat or barley, and companion planting of grape and olive. These books demonstrate the importance of agriculture both as a traditional practice and as a scholarly science. In al-Andalus, there is evidence that the almanacs and manuals of agronomy helped to catalyse change, causing scholars to seek out new kinds of vegetable and fruit, and to carry out experiments in botany; in turn, these helped to improve actual practice in the region's agriculture.
Enzymes are generally in a state that is not only a compromise between stability and catalytic efficiency, but also for specificity and evolvability, the latter two dictating whether an enzyme is a generalist (highly evolvable due to large promiscuity, but low main activity) or a specialist (high main activity, poorly evolvable due to low promiscuity). Examples of these are enzymes for primary and secondary metabolism in plants (§ Plant secondary metabolism below). Other factors can come into play, for example the glycerophosphodiesterase (gpdQ) from Enterobacter aerogenes shows different values for its promiscuous activities depending on the two metal ions it binds, which is dictated by ion availability. In some cases promiscuity can be increased by relaxing the specificity of the active site by enlarging it with a single mutation as was the case of a D297G mutant of the E. coli L-Ala-D/L-Glu epimerase (ycjG) and E323G mutant of a pseudomonad muconate lactonizing enzyme II, allowing them to promiscuously catalyse the activity of O-succinylbenzoate synthase (menC).
CYP24A1 is an enzyme expressed in the mitochondrion of humans and other species. It catalyzes hydroxylation reactions which lead to the degradation of 1,25-dihydroxyvitamin D3, the physiologically active form of vitamin D. Hydroxylation of the side chain produces calcitroic acid and other metabolites which are excreted in bile. CYP24A1 was identified in the early 1970s and was first thought to be involved in vitamin D metabolism as the renal 25-hydroxyvitamin D3-24-hydroxylase, modifying calcifediol (25-hydroxyvitamin D) to produce 24,25-dihydroxycholecalciferol (24,25-dihydroxyvitamin D). Subsequent studies using recombinant CYP24A1 showed that it could also catalyze multiple other hydroxylation reactions at the side chain carbons known as C-24 and C-23 in both 25-OH-D3 and the active hormonal form, 1,25-(OH)2D3. It is now considered responsible for the entire five-step, 24-oxidation pathway from 1,25-(OH)2D3 producing calcitroic acid. CYP24A1 also is able to catalyse another pathway which starts with 23-hydroxylation of 1,25-(OH)2D3 and culminates in 1,25-(OH)2D3-26,23-lactone.
Mechanism of Inhibitors of AChE Chronic exposure to high level of nitrogen dioxide results in the allosteric inhibition of glutathione peroxidase and glutathione S-transferase, both of which are important enzymes found in the mucous membrane antioxidant defense system, that catalyse nucleophilic attack by reduced glutathione (GSH) on non- polar compounds that contain an electrophillic carbon and nitrogen. These inhibition mechanisms generates free radicals that causes peroxidation from the lipids in the mucous membrane leading to increased peroxidized erythrocyte lipids, a reaction that proceeds by a free radical chain reaction mechanism that result in oxidative stress. The oxidative stress on the mucous membrane causes the dissociation of the GSTp-JNK complex, oligomerization of GSTP and induction of the JNK pathway, resulting in apoptosis or inflammation of the bronchioles and pulmonary alveolus in mild cases. On migrating to the bloodstream, nitrogen dioxide poisoning results in an irreversible inhibition of the erythrocite membrane acetylcholinesterase which may lead to muscular paralysis, convulsions, bronchoconstriction, the narrowing of the airways in the lungs (bronchi and bronchioles) and death by asphyxiation.
She was then recruited back to Lehman Bros in London in a strategic role to attract more women and ethnic minorities to the bank. Afterwards she moved to Nomura, when Lehman was bought by them in the UK.. She was previously a Director at Neuberger Berman In September, 2011, Essomé was appointed chief executive officer of the African Private Equity and Venture Capital Association (AVCA), a pan-African industry body which aims to catalyse investment in Africa, to promote the continent and enable private equity and venture capital investment there. She describes the reason for her recruitment as being to drive the company forward from its then position as a defunct association, into an organisation with global reach, able to provide world class research, networking and convening opportunities for fund managers and advocates on their behalf to the world. When she joined, she had to wind down the legacy entity and set up a new one in the UK, recruit the board and new members, establish good governance, attract a team and build up a research capability to prove Africa’s attractiveness as an investment location.
The first was the elucidation of the mechanism by which thrombin acts as a protease to catalyse the formation of the major component of blood clots, the insoluble protein fibrin, from its soluble precursor fibrinogen by Laszlo Lorand, a young PhD student who had fled his native Hungary to join Astbury. Lorand's work was a major discovery in our understanding of the process by which blood clots form. The second development was a series of new X-ray photographs of B-form DNA taken in 1951 by Astbury's research assistant Elwyn Beighton which the historian of science, Professor Robert Olby has since said was 'clearly the famous B-pattern found by Rosalind Franklin and R. Gosling'. Olby was referring to an X-ray image of B-form DNA that was taken a year later by Rosalind Franklin and her PhD student Raymond Gosling at King's College a year later which came to be known as 'Photo 51' Despite its modest name this image was to play an important role in the story of DNA and a plaque on the wall outside King's College, London hails it as 'one of the most important photographs in the world'.

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