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  • enzymology
  • In enzymology, a chorismate lyase (EC 4.1.3.40) is an enzyme that catalyzes the chemical reaction chorismate ⇌ {\displaystyle \rightleftharpoons } 4-hydroxybenzoate + pyruvate Hence, this enzyme has one substrate, chorismate, and two products, 4-hydroxybenzoate and pyruvate. (wikipedia.org)
  • In enzymology, a xanthan lyase (EC 4.2.2.12) is an enzyme that catalyzes the chemical reaction of cleaving the beta-D-mannosyl-beta-D-1,4-glucuronosyl bond on the polysaccharide xanthan. (wikipedia.org)
  • In enzymology, a pectin lyase also known as pectolyase is a naturally occurring pectinase a type of enzyme that degrades pectin. (wikipedia.org)
  • In enzymology, a mandelonitrile lyase (EC 4.1.2.10, (R)-HNL, (R)-oxynitrilase, (R)-hydroxynitrile lyase) is an enzyme that catalyzes the chemical reaction mandelonitrile ⇌ {\displaystyle \rightleftharpoons } hydrogen cyanide + benzaldehyde Hence, this enzyme has one substrate, mandelonitrile, and two products, hydrogen cyanide and benzaldehyde. (wikipedia.org)
  • In enzymology, a selenocysteine lyase (EC 4.4.1.16) is an enzyme that catalyzes the chemical reaction L-selenocysteine + reduced acceptor ⇌ {\displaystyle \rightleftharpoons } selenide + L-alanine + acceptor Thus, the two substrates of this enzyme are L-selenocysteine and reduced acceptor, whereas its 3 products are selenide, L-alanine, and acceptor. (wikipedia.org)
  • In enzymology, an oligogalacturonide lyase (EC 4.2.2.6) is an enzyme that catalyzes the chemical reaction 4-(4-deoxy-beta-D-gluc-4-enuronosyl)-D-galacturonate ⇌ {\displaystyle \rightleftharpoons } 2 5-dehydro-4-deoxy-D-glucuronate Hence, this enzyme has one substrate, 4-(4-deoxy-beta-D-gluc-4-enuronosyl)-D-galacturonate, and one product, 5-dehydro-4-deoxy-D-glucuronate. (wikipedia.org)
  • In enzymology, a lactoylglutathione lyase (EC 4.4.1.5) (also known as glyoxalase I) is an enzyme that catalyzes the isomerization of hemithioacetal adducts, which are formed in a spontaneous reaction between a glutathionyl group and aldehydes such as methylglyoxal. (wikipedia.org)
  • In enzymology, a hyaluronate lyase (EC 4.2.2.1) is an enzyme that catalyzes the chemical reaction Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. (wikipedia.org)
  • enzymes
  • Genomic and functional characterization of the oas gene family encoding O-acetylserine (thiol) lyases , enzymes catalyzing the final step in cysteine biosynthesis in Arabidopsis thaliana. (thefreedictionary.com)
  • These enzymes are grouped into six classes: hydrolases (including proteases, amylases and lipases that break down the main nutrients - fats, carbohydrates and proteins), isomerases, ligases, lyases , oxidoreductases and transferases. (thefreedictionary.com)
  • A number of enzymes, belonging to the lyase class, for which fumarate is a substrate have been shown [ PMID: 3282546 ] to share a short conserved sequence around a methionine which is probably involved in the catalytic activity of this type of enzymes. (ebi.ac.uk)
  • For example, an enzyme that catalyzed this reaction would be a lyase: ATP → cAMP + PPi Lyases differ from other enzymes in that they require only one substrate for the reaction in one direction, but two substrates for the reverse reaction. (wikipedia.org)
  • Lyases are classified as EC 4 in the EC number classification of enzymes. (wikipedia.org)
  • Hydroperoxide lyases are enzymes that catalyze the cleavage of C-C bonds in the hydroperoxides of fatty acids. (wikipedia.org)
  • Isochorismate lyase, or PchB, is part of the lyase class of enzymes. (wikipedia.org)
  • ASL, δ-crystallin, class II fumarase, aspartase, adenylosuccinase lyase, and 3-carboxy-cis and cis-muconate lactonizing enzyme are all members of the same homotetrameric superfamily of enzymes, in which most catalyze the same type of elimination reactions where a C-O or C-N bond is broken and fumarate is released as a product. (wikipedia.org)
  • pectin lyase
  • Bacillus cereus GS-2 isolated from fruit industrial dump site effectively produces pectin lyase (PL) and Polygalacturonase (PG). (thefreedictionary.com)
  • This entry covers proteins that are closely related to the pectolytic enzyme, pectin lyase, which act as virulence factors. (ebi.ac.uk)
  • When the backbone of pectin is methylated it is known as pectin, and can be cleaved by pectin lyase, a microbial virulence factor [ PMID: 9195887 ]. (ebi.ac.uk)
  • Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases. (ebi.ac.uk)
  • Pectin lyase is an enzyme that catalyzes the chemical reaction Eliminative cleavage of (1->4)-alpha-D-galacturonan methyl ester to give oligosaccharides with 4-deoxy-6-O-methyl-alpha-D-galact-4-enuronosyl groups at their non-reducing ends This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. (wikipedia.org)
  • The first report on retting of sunn hemp (Crotalaria juncea) by pectin lyase produced by Aspergillus flavus MTCC 7589 was published in 2008 but this aspect of pectin lyases needs to be extensively investigated further. (wikipedia.org)
  • Application of mass spectrometry to determine the activity and specificity of pectin lyase A". Carbohydr. (wikipedia.org)
  • PMID
  • When the backbone of pectin is demethylated it is known as pectate, and can be cleaved by pectate lyase virulence factors, or hydrolysed by polygalacturonases [ PMID: 12324535 , PMID: 11518536 ]. (ebi.ac.uk)
  • Adenylosuccinase, EC:4.3.2.2 (adenylosuccinate lyase) [ PMID: 1574589 ], which catalyses the eighth step in the de novo biosynthesis of purines, the formation of 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide and fumarate from 1-(5-phosphoribosyl)-4-(N-succino-carboxamide). (ebi.ac.uk)
  • catalyses
  • This enzyme catalyses the following chemical reaction S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O ⇌ {\displaystyle \rightleftharpoons } (2E,6E)-farnesal + L-cysteine + H2O2 Farnesylcysteine lyase is a flavoprotein (FAD). (wikipedia.org)
  • Arginosuccinase, EC:4.3.2.1 (argininosuccinate lyase), which catalyses the formation of arginine and fumarate from argininosuccinate, the last step in the biosynthesis of arginine. (ebi.ac.uk)
  • A combination of both an elimination and a Michael addition is seen in O-succinylhomoserine (thiol)-lyase (MetY or MetZ) which catalyses first the γ-elimination of O-succinylhomoserine (with succinate as a leaving group) and then the addition of sulfide to the vinyl intermediate, this reaction was first classified as a lyase (EC 4.2.99.9), but was then reclassified as a transferase (EC 2.5.1.48). (wikipedia.org)
  • Ligases
  • He covers chiral discrimination in the active site of oxidoreductases, transferases and chiral discrimination, the influence of chirality on the hydrolysis reactions within the active site of hydrolases, the influence of chirality on the reactions in the active site of lyases , and chiral discrimination in the active site of ligases. (thefreedictionary.com)
  • enzyme that catalyzes
  • In biochemistry, a lyase is an enzyme that catalyzes the breaking (an "elimination" reaction) of various chemical bonds by means other than hydrolysis (a "substitution" reaction) and oxidation, often forming a new double bond or a new ring structure. (wikipedia.org)
  • thiol
  • O-acetylserine (thiol) lyase is a pyridoxal phosphate-dependent enzyme, and a lysine residue at the N-terminal region of this protein is involved in binding this cofactor (Saito et al. (thefreedictionary.com)
  • Pseudomonas
  • Benzaldehyde lyase from Pseudomonas fluorescens Biovar I. (BAL, EC 4.1.2.38) is a versatile catalyst for the organic synthesis of chiral α -hydroxy ketones. (hindawi.com)
  • Protein
  • Delta-crystallin shares around 90% sequence identity with arginosuccinate lyase, showing that it is an example of a 'hijacked' enzyme - accumulated mutations have, however, rendered the protein enzymatically inactive. (ebi.ac.uk)
  • synthase
  • Methylisocitrate lyase is used in the methylcitrate cycle, a modified version of the Krebs cycle that metabolizes propionyl coenzyme A instead of acetyl coenzyme A. The enzyme 2-methylcitrate synthase adds propionyl coenzyme A to oxaloacetate, yielding methylcitrate instead of citrate. (wikipedia.org)
  • reaction
  • Among the depolymerases, polygalacturonase is the major enzyme with a hydrolytic function and lyases (or transeleminases) which cleaves glycosidic bonds forming unsaturated product[DELTA](4,5-D-galacturonate) through transelimination reaction . (thefreedictionary.com)
  • It is this reaction that is catalyzed by hydroperoxide lyases. (wikipedia.org)
  • include
  • Other names in common use include alpha-hydroxyglycine amidating dealkylase, peptidyl-alpha-hydroxyglycine alpha-amidating lyase, HGAD, PGL, PAL, and peptidylamidoglycolate peptidylamide-lyase. (wikipedia.org)
  • Other names in common use include ureidoglycolatase, ureidoglycolase, ureidoglycolate hydrolase, and (S)-ureidoglycolate urea-lyase. (wikipedia.org)
  • Other names in common use include selenocysteine reductase, and selenocysteine beta-lyase. (wikipedia.org)
  • Other names in common use include oligogalacturonate lyase, unsaturated oligogalacturonate transeliminase, and OGTE. (wikipedia.org)
  • other names include methylglyoxalase, aldoketomutase, ketone-aldehyde mutase, and (R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing). (wikipedia.org)
  • known
  • Pectin lyases are the only known pectinases capable of degrading highly esterified pectins (like those found in fruits) into small molecules via [beta]-elimination mechanism without producing methanol. (thefreedictionary.com)
  • Carboxy-lyases, also known as decarboxylases, are carbon-carbon lyases that add or remove a carboxyl group from organic compounds. (wikipedia.org)
  • Pectin lyases are the only known pectinases capable of degrading highly esterified pectins (like those found in fruits) into small molecules via β-elimination mechanism without producing methanol (which is toxic), in contrast with the combination of PG and PE, which are normally found in commercial products. (wikipedia.org)