• 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
  • A number of enzymes, belonging to the lyase class, for which fumarate is a substrate, have been shown to share a short conserved sequence around a methionine which is probably involved in the catalytic activity of this type of enzymes [ PMID: 3282546 ]. (ebi.ac.uk)
  • Proteins containing this C-terminal domain consist of a group of secreted bacterial lyase enzymes capable of acting on a variety of substrates. (ebi.ac.uk)
  • Crystal structure of chondroitin AC lyase, a representative of a family of glycosaminoglycan degrading enzymes. (ebi.ac.uk)
  • However, these results have been underestimated because genes for the two key enzymes of the cycle, isocitrate lyase (ICL) and malate synthase (MS), are not annotated in Leishmania genomes. (degruyter.com)
  • 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)
  • PMID
  • 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)
  • 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)
  • One such enzyme is hyaluronate lyase, a Streptococcal surface enzyme that degrades hyaluronan and chondroitin, thereby helping to spread the bacteria throughout host tissues [ PMID: 14523022 ]. (ebi.ac.uk)
  • 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)
  • 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)
  • ASL (argininosuccinate lyase, also known as argininosuccinase) is an enzyme that catalyzes the reversible breakdown of argininosuccinate (ASA) producing the amino acid arginine and dicarboxylic acid fumarate. (wikipedia.org)
  • 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)
  • The protein encoded by this gene belongs to the HMG-CoA lyase family. (nih.gov)
  • proteins
  • These proteins include pectate lyase, iota-carrageenase, and glycoside hydrolases from family 28 (such as galacturonases). (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)
  • 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)
  • 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)
  • 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 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)
  • activity
  • Influence of multiple cysteines on human 3-hydroxy-3-methylglutaryl-CoA lyase activity and formation of inter-subunit adducts. (nih.gov)
  • known
  • 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)
  • crystal
  • Crystal structure of Proteus vulgaris chondroitin sulfate ABC lyase I at 1.9A resolution. (ebi.ac.uk)