In biochemistry , a lyase is an enzyme that catalyzes the breaking of various chemical bond s by means other than hydrolysis and oxidation , often forming a new double bond or a new ring structure. For example, an enzyme that catalyzed this reaction would be a lyase Adenosine triphosphate ATP &rarr cyclic adenosine monophosphate cAMP PP sub i sub Lyases differ from other enzymes in that they require only one substrate biochemistry substrate for the reaction in one direction, but two substrates for the reverse reaction. Nomenclature Systematic names are formed as substrate group lyase. Common names include decarboxylase , dehydratase , aldolase , etc. When the reverse reaction is more important, synthase may be used in the name. Classification Lyases are classified as EC 4 in the Enzyme Commission number EC number classification of enzymes. Lyases can be further classified into seven subclasses Category EC 4.1 EC 4.1 includes lyases that cleave carbon carbon bonds, such as decarboxylase s EC 4.1.1 , aldehyde lyases EC 4.1.2 , oxo acid lyases EC 4.1.3 and others EC 4.1.99 Category EC 4.2 EC 4.2 includes lyases that cleave carbon oxygen bonds, such as dehydratase s Category EC 4.3 EC 4.3 includes lyases that cleave carbon nitrogen bonds Category EC 4.4 EC 4.4 includes lyases that cleave carbon sulfur bonds Category EC 4.5 EC 4.5 includes lyases that cleave carbon halide bonds Category EC 4.6 EC 4.6 includes lyases that cleave phosphorus oxygen bonds, such as adenylate cyclase and guanylate cyclase Category EC 4.99 EC 4.99 includes other lyases, such as ferrochelatase See also List of EC numbers 28EC 4 29 List of EC numbers of enzymes belonging to category EC 4 References http www.chem.qmul.ac.uk iubmb enzyme EC4 intro.html EC 4 Introduction from the Department of Chemistry at Queen Mary, University of London Enzymes Lyases Category Lyases ar bg ca Liasa cs Ly za da Lyase de Lyasen es Liasa fr Lyase gl Liase it Liasi lt Liaz s nl Lyase ja pl Liazy pt Liase ... more details
enzyme Name citramalate lyase EC number 4.1.3.22 CAS number 9027 93 4 IUBMB EC number 4 1 3 22 GO code 0047776 image width caption In enzymology , a citramalate lyase EC number 4.1.3.22 is an enzyme that catalysis catalyzes the chemical reaction 2S 2 hydroxy 2 methylbutanedioate math rightleftharpoons math acetate pyruvate Hence, this enzyme has one substrate biochemistry substrate , 2S 2 hydroxy 2 methylbutanedioate , and two product chemistry products , acetate and pyruvate . This enzyme belongs to the family of lyase s, specifically the oxo acid lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is 2S 2 hydroxy 2 methylbutanedioate pyruvate lyase acetate forming . Other names in common use include citramalate pyruvate lyase , citramalate synthase , citramalic condensing enzyme , citramalate synthetase , citramalic synthase , S citramalate lyase , citramalate pyruvate lyase , citramalate pyruvate lyase , 3S citramalate pyruvate lyase , and 2S 2 hydroxy 2 methylbutanedioate pyruvate lyase . This enzyme participates in c5 branched dibasic acid metabolism . References reflist 1 cite journal author Barker HA date 1967 title Citramalate lyase of Clostridium tetanomorphum journal Arch. Mikrobiol. volume 59 pages 4&ndash 12 pmid 4301387 doi 10.1007 BF00406311 issue 1 cite journal author Dimroth P, Buckel W, Loyal R, Eggerer H date 1977 title Isolation and function of the subunits of citramalate lyase and formation of hybrids with the subunits of citrate lyase journal Eur. J. Biochem. volume 80 pages 469&ndash 77 pmid 923590 doi 10.1111 j.1432 1033.1977.tb11902.x issue 2 4.1 enzyme stub Category EC 4.1.3 Category Enzymes of unknown structure ... more details
enzyme Name cysteine lyase EC number 4.4.1.10 CAS number 9079 86 1 IUBMB EC number 4 4 1 10 GO code 0047803 image width caption In enzymology , a cysteine lyase EC number 4.4.1.10 is an enzyme that catalysis catalyzes the chemical reaction L cysteine sulfite math rightleftharpoons math L cysteate hydrogen sulfide Thus, the two substrate biochemistry substrates of this enzyme are L cysteine and sulfite , whereas its two product chemistry products are L cysteate and hydrogen sulfide . This enzyme belongs to the family of lyase s, specifically the class of carbon sulfur lyases. The systematic name of this enzyme class is L cysteine hydrogen sulfide lyase adding sulfite L cysteate forming . Other names in common use include cysteine sulfite lyase , and L cysteine hydrogen sulfide lyase adding sulfite . This enzyme participates in cysteine metabolism and taurine and hypotaurine metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Tolosa EA, Chepurnova NK, Khomutov RM, Severin ES date 1969 title Reactions catalysed by cysteine lyase from the yolk sac of chicken embryo journal Biochim. Biophys. Acta. volume 171 pages 369&ndash 71 pmid 5813025 issue 2 lyase stub Category EC 4.4.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ja ... more details
enzyme Name carboxymethyloxysuccinate lyase EC number 4.2.99.12 CAS number 53167 89 8 IUBMB EC number 4 2 99 12 GO code 0047772 image width caption In enzymology , a carboxymethyloxysuccinate lyase EC number 4.2.99.12 is an enzyme that catalysis catalyzes the chemical reaction carboxymethyloxysuccinate math rightleftharpoons math fumarate glycolate Hence, this enzyme has one substrate biochemistry substrate , carboxymethyloxysuccinate , and two product chemistry products , fumarate and glycolate . This enzyme belongs to the family of lyase s, specifically the catch all class of lyases that cleave carbon oxygen bonds. The systematic name of this enzyme class is carboxymethyloxysuccinate glycolate lyase fumarate forming . Other names in common use include carbon oxygen lyase , and carboxymethyloxysuccinate glycolate lyase . References reflist 1 cite journal author Peterson D, Llaneza J date 1974 title Identification of a carbon oxygen lyase activity cleaving the ether linkage in carboxymethyloxysuccinic acid journal Arch. Biochem. Biophys. volume 162 pages 135&ndash 46 pmid 4831330 doi 10.1016 0003 9861 74 90112 X issue 1 4.2 enzyme stub Category EC 4.2.99 Category Enzymes of unknown structure ... more details
enzyme Name ureidoglycolate lyase EC number 4.3.2.3 CAS number 9014 57 7 IUBMB EC number 4 3 2 3 GO code 0050385 image width caption In enzymology , an ureidoglycolate lyase EC number 4.3.2.3 is an enzyme that catalysis catalyzes the chemical reaction S ureidoglycolate math rightleftharpoons math glyoxylate urea Hence, this enzyme has one substrate biochemistry substrate , S ureidoglycolate , and two product chemistry products , glyoxylate and urea . This enzyme belongs to the family of lyase s, specifically amidine lyases. The systematic name of this enzyme class is S ureidoglycolate urea lyase glyoxylate forming . Other names in common use include ureidoglycolatase , ureidoglycolase , ureidoglycolate hydrolase , and S ureidoglycolate urea lyase . This enzyme participates in purine metabolism . References reflist 1 cite journal author Trijbels F, Vogels GD date 1967 title Allantoate and ureidoglycolate degradation by Pseudomonas aeruginosa journal Biochim. Biophys. Acta. volume 132 pages 115&ndash 26 pmid 6030341 issue 1 enzyme stub Category EC 4.3.2 Category Enzymes of unknown structure ... more details
enzyme Name S alkylcysteine lyase EC number 4.4.1.6 CAS number 62213 27 8 IUBMB EC number 4 4 1 6 GO code 0050271 image width caption In enzymology , a S alkylcysteine lyase EC number 4.4.1.6 is an enzyme that catalysis catalyzes the chemical reaction an S alkyl L cysteine H sub 2 sub O math rightleftharpoons math an alkyl thiol NH sub 3 sub pyruvate Thus, the two substrate biochemistry substrates of this enzyme are S alkyl L cysteine and water H sub 2 sub O , whereas its 3 product chemistry products are alkyl thiol , ammonia NH sub 3 sub , and pyruvate . This enzyme belongs to the family of lyase s, specifically the class of carbon sulfur lyases. The systematic name of this enzyme class is S alkyl L cysteine alkyl thiol lyase deaminating pyruvate forming . Other names in common use include S alkylcysteinase , alkylcysteine lyase , S alkyl L cysteine sulfoxide lyase , S alkyl L cysteine lyase , S alkyl L cysteinase , alkyl cysteine lyase , and S alkyl L cysteine alkylthiol lyase deaminating . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Nomura J, Nishizuka Y and Hayaishi O date 1963 title S Alkylcysteinase enzymatic cleavage of S methyl L cysteine and its sulfoxide journal J. Biol. Chem. volume 238 pages 1441&ndash 1446 enzyme stub Category EC 4.4.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name 4 amino 4 deoxychorismate lyase EC number 4.1.3.38 CAS number IUBMB EC number 4 1 3 38 GO code 0008696 image width caption In enzymology , an aminodeoxychorismate lyase EC number 4.1.3.38 is an enzyme that catalysis catalyzes the chemical reaction 4 amino 4 deoxychorismate math rightleftharpoons math 4 aminobenzoate pyruvate Hence, this enzyme has one substrate biochemistry substrate , 4 amino 4 deoxychorismate , and two product chemistry products , 4 aminobenzoate and pyruvate . This enzyme belongs to the family of lyase s, specifically the oxo acid lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is 4 amino 4 deoxychorismate pyruvate lyase 4 aminobenzoate forming . Other names in common use include enzyme X , 4 amino 4 deoxychorismate lyase , and 4 amino 4 deoxychorismate pyruvate lyase . This enzyme participates in folate biosynthesis . References reflist 1 cite journal author Ye QZ, Liu J, Walsh CT date 1990 title p Aminobenzoate synthesis in Escherichia coli purification and characterization of PabB as aminodeoxychorismate synthase and enzyme X as aminodeoxychorismate lyase journal Proc. Natl. Acad. Sci. U. S. A. volume 87 pages 9391&ndash 5 pmid 2251281 doi 10.1073 pnas.87.23.9391 issue 23 pmc 55171 cite journal author Green JM, Merkel WK, Nichols BP date 1992 title Characterization and sequence of Escherichia coli pabC, the gene encoding aminodeoxychorismate lyase, a pyridoxal phosphate containing enzyme journal J. Bacteriol. volume 174 pages 5317&ndash 23 pmid 1644759 issue 16 pmc 206368 cite journal author Yoshimura T, Esaki N date Tokyo title Three dimensional structure of 4 amino 4 deoxychorismate lyase from Escherichia coli journal J. volume Biochem. pages 29&ndash 38 pmid 10876155 issue 1 4.1 enzyme stub Category EC 4.1.3 Category Enzymes of unknown structure ... more details
enzyme Name peptidylamidoglycolate lyase EC number 4.3.2.5 CAS number 131689 50 4 IUBMB EC number 4 3 2 5 GO code 0004598 image width caption In enzymology , a peptidylamidoglycolate lyase EC number 4.3.2.5 is an enzyme that catalysis catalyzes the chemical reaction peptidylamidoglycolate math rightleftharpoons math peptidyl amide glyoxylate Hence, this enzyme has one substrate biochemistry substrate , peptidylamidoglycolate , and two product chemistry products , peptidyl amide and glyoxylate . This enzyme belongs to the family of lyase s, specifically amidine lyases. The systematic name of this enzyme class is peptidylamidoglycolate peptidyl amide lyase glyoxylate forming . Other names in common use include alpha hydroxyglycine amidating dealkylase , peptidyl alpha hydroxyglycine alpha amidating lyase , HGAD , PGL , PAL , and peptidylamidoglycolate peptidylamide lyase . References reflist 1 cite journal author Katopodis AG, Ping D, May SW date 1990 title A novel enzyme from bovine neurointermediate pituitary catalyzes dealkylation of alpha hydroxyglycine derivatives, thereby functioning sequentially with peptidylglycine alpha amidating monooxygenase in peptide amidation journal Biochemistry. volume 29 pages 6115&ndash 20 pmid 2207061 doi 10.1021 bi00478a001 issue 26 enzyme stub Category EC 4.3.2 Category Enzymes of unknown structure ... more details
enzyme Name Glucuronan lyase EC number 4.2.2.14 CAS number IUBMB EC number 4 2 2 14 GO code image width caption In enzymology , a glucuronan lyase EC number 4.2.2.14 is an enzyme that catalysis catalyzes the chemical reaction of eliminative cleavage of 1 4 beta D glucuronans. This produces either oligosaccharides with 4 deoxy beta D gluc 4 enuronosyl groups at their non reducing ends, or, if the substrate is completely degraded, glucuronans produce tetrasaccharides. This enzyme belongs to the family of lyase s, specifically those carbon oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is 1 4 beta D glucuronan lyase . This enzyme is also called 1,4 beta D glucuronan lyase . References reflist 1 cite journal author Courtois B, Courtois J date 1997 title Identification of glucuronan lyase from a mutant strain of Rhizobium meliloti journal Int. J. Biol. Macromol. volume 21 pages 3&ndash 9 pmid 9283009 doi 10.1016 S0141 8130 97 00033 0 issue 1 2 4.2 enzyme stub Category EC 4.2.2 Category Enzymes of unknown structure ... more details
enzyme Name alkylmercury lyase EC number 4.99.1.2 CAS number 72560 99 7 IUBMB EC number 4 99 1 2 GO code 0018836 image 3f0p.png width caption Structure of the mercury bound form of E.coli MerB. PDB PDBe 3f0p ref cite pmid 19004822 ref In enzymology , an alkylmercury lyase EC number 4.99.1.2 is an enzyme that catalysis catalyzes the chemical reaction an alkylmercury H sup sup math rightleftharpoons math an alkane Hg sub 2 sub Thus, the two substrate biochemistry substrates of this enzyme are alkylmercury and hydrogen ion H sup sup , whereas its two product chemistry products are alkane and a Mercury element mercury ion. This enzyme belongs to the family of lyase s, specifically the catch all class of lyases that do not fit into any other sub class. The systematic name of this enzyme class is alkylmercury mercuric lyase alkane forming . Other names in common use include organomercury lyase , organomercurial lyase , and alkylmercury mercuric lyase . The enzyme converts methyl mercury to the much less toxic elemental form of the metal. References reflist 1 cite journal author Tezuka T, Tonomura K date Tokyo title Purification and properties of an enzyme catalyzing the splitting of carbon mercury linkages from mercury resistant Pseudomonas K 62 strain. I. Splitting enzyme 1 journal J. volume Biochem. pages 79&ndash 87 pmid 9382 issue 1 lyase stub Category EC 4.99.1 Category Enzymes of known structure ... more details
enzyme Name hydroxymandelonitrile lyase EC number 4.1.2.11 CAS number 9075 38 1 IUBMB EC number 4 1 2 11 GO code 0050419 image width caption In enzymology , a hydroxymandelonitrile lyase EC number 4.1.2.11 is an enzyme that catalysis catalyzes the chemical reaction S 4 hydroxymandelonitrile math rightleftharpoons math cyanide 4 hydroxybenzaldehyde Hence, this enzyme has one substrate biochemistry substrate , S 4 hydroxymandelonitrile , and two product chemistry products , cyanide and 4 hydroxybenzaldehyde . This enzyme belongs to the family of lyase s, specifically the aldehyde lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is S 4 hydroxymandelonitrile 4 hydroxybenzaldehyde lyase cyanide forming . Other names in common use include hydroxynitrile lyase , oxynitrilase , Sorghum hydroxynitrile lyase , and S 4 hydroxymandelonitrile hydroxybenzaldehyde lyase . This enzyme participates in cyanoamino acid metabolism . Structural studies As of late 2007, only one tertiary structure structure has been solved for this class of enzymes, with the Protein Data Bank PDB accession code PDB link 1GXS . References reflist 1 cite journal author AJ date 2006 title Population pharmacokinetics of liposomal amphotericin B in pediatric patients with malignant diseases journal Antimicrob. Agents. Chemother. volume 50 pages 935&ndash 42 pmid 16495254 doi 10.1128 AAC.50.3.935 942.2006 last2 Shaw first2 PJ last3 Nath first3 CE last4 Yadav first4 SP last5 Stephen first5 KR last6 Earl first6 JW last7 McLachlan first7 AJ issue 3 pmc 1426421 cite journal author Seely MK, Criddle RS, Conn EE date 1966 title The metabolism of aromatic compounds in higher plants. 8. On the requirement of hydroxynitrile lyase for flavin journal J. Biol. Chem. volume 241 pages 4457&ndash 62 pmid 5922969 issue 19 4.1 enzyme stub Category EC 4.1.2 Category Enzymes of known structure ... more details
enzyme Name heparin lyase EC number 4.2.2.7 CAS number 9025 39 2 IUBMB EC number 4 2 2 7 GO code 0047488 image width caption In enzymology , a heparin lyase EC number 4.2.2.7 is an enzyme that catalysis catalyzes the chemical reaction Eliminative cleavage of polysaccharides containing 1,4 linked D glucuronate or L iduronate residues and 1,4 alpha linked 2 sulfoamino 2 deoxy 6 sulfo D glucose residues to give oligosaccharides with terminal 4 deoxy alpha D gluc 4 enuronosyl groups at their non reducing ends This enzyme belongs to the family of lyase s, specifically those carbon oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is heparin lyase . Other names in common use include heparin eliminase , and heparinase . References reflist 1 cite journal author Hovingh P, Linker A date 1970 title The enzymatic degradation of heparin and heparitin sulfate. 3 Purification of a heparitinase and a heparinase from flavobacteria journal J. Biol. Chem. volume 245 pages 6170&ndash 5 pmid 5484472 issue 22 4.2 enzyme stub Category EC 4.2.2 Category Enzymes of unknown structure ... more details
enzyme Name oxalomalate lyase EC number 4.1.3.13 CAS number 37290 63 4 IUBMB EC number 4 1 3 13 GO code 0050204 image width caption In enzymology , an oxalomalate lyase EC number 4.1.3.13 is an enzyme that catalysis catalyzes the chemical reaction 3 oxalomalate math rightleftharpoons math oxaloacetate glyoxylate Hence, this enzyme has one substrate biochemistry substrate , 3 oxalomalate , and two product chemistry products , oxaloacetate and glyoxylate . This enzyme belongs to the family of lyase s, specifically the oxo acid lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is 3 oxalomalate glyoxylate lyase oxaloacetate forming . This enzyme is also called 3 oxalomalate glyoxylate lyase . This enzyme participates in glyoxylate and dicarboxylate metabolism . References reflist 1 cite journal author Sekizawa Y, Maragoudakis ME, King TE, Cheldelin VH date 1966 title Glutamate biosynthesis in an organism lacking a Krebs tricarboxylic acid cycle. V. Isolation of alpha hydroxy gamma ketoglutarate HKG in Acetobacter suboxydans journal Biochemistry. volume 5 pages 2392&ndash 8 pmid 6005666 doi 10.1021 bi00871a032 issue 7 4.1 enzyme stub Category EC 4.1.3 Category Enzymes of unknown structure ... more details
enzyme Name oligogalacturonide lyase EC number 4.2.2.6 CAS number 9031 33 8 IUBMB EC number 4 2 2 6 GO code 0047487 image width caption In enzymology , an oligogalacturonide lyase EC number 4.2.2.6 is an enzyme that catalysis catalyzes the chemical reaction 4 4 deoxy beta D gluc 4 enuronosyl D galacturonate math rightleftharpoons math 2 5 dehydro 4 deoxy D glucuronate Hence, this enzyme has one substrate biochemistry substrate , 4 4 deoxy beta D gluc 4 enuronosyl D galacturonate , and one product chemistry product , 5 dehydro 4 deoxy D glucuronate . This enzyme belongs to the family of lyase s, specifically those carbon oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is oligogalacturonide lyase . Other names in common use include oligogalacturonate lyase , unsaturated oligogalacturonate transeliminase , and OGTE . This enzyme participates in pentose and glucuronate interconversions . References reflist 1 cite journal author Moran F, Nasuno S, Starr MP date 1968 title Oligogalacturonide trans eliminase of Erwinia carotovora journal Arch. Biochem. Biophys. volume 125 pages 734&ndash 41 pmid 5671040 doi 10.1016 0003 9861 68 90508 0 issue 3 4.2 enzyme stub Category EC 4.2.2 Category Enzymes of unknown structure ... more details
Orphan date February 2009 enzyme Name Chorismate lyase EC number 4.1.3.40 CAS number 157482 18 3 IUBMB EC number 4 1 3 40 GO code image width caption Infobox protein family Symbol Chor lyase Name Chorismate lyase image PDB 1tt8 EBI.jpg width caption chorismate lyase with product, 1.0 a resolution Pfam PF04345 Pfam clan CL0122 InterPro IPR007440 SMART PROSITE MEROPS SCOP 1jd3 TCDB OPM family OPM protein CAZy CDD In enzymology , a chorismate lyase EC number 4.1.3.40 is an enzyme that catalysis catalyzes the chemical reaction chorismate math rightleftharpoons math 4 hydroxybenzoate pyruvate Hence, this enzyme has one substrate biochemistry substrate , chorismate , and two product chemistry products , 4 hydroxybenzoate and pyruvate . This enzyme belongs to the family of lyase s, specifically the oxo acid lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is chorismate pyruvate lyase 4 hydroxybenzoate forming . Other names in common use include CL , CPL , and UbiC . This enzyme catalysis catalyses the first step in ubiquinone biosynthesis , the removal of pyruvate from chorismate, to yield 4 hydroxybenzoate in Escherichia coli and other Gram negative bacteria . ref name pmid1644758 cite journal author Nichols BP, Green JM title Cloning and sequencing of Escherichia coli ubiC and purification of chorismate lyase journal J. Bacteriol. volume 174 issue 16 pages 5309 16 year 1992 month August pmid 1644758 pmc 206367 doi url ref Its activity does not require metal Cofactor biochemistry cofactors . ref name pmid8012607 cite journal author Siebert M, Severin K, Heide L title Formation of 4 hydroxybenzoate in Escherichia coli characterization of the ubiC gene and its encoded enzyme chorismate pyruvate lyase journal Microbiology Reading, Engl. volume 140 ... and sequencing of Escherichia coli ubiC and purification of chorismate lyase journal J. Bacteriol. volume ... gene and its encoded enzyme chorismate pyruvate lyase journal Microbiology. volume 140 pages ... more details
enzyme Name mandelonitrile lyase EC number 4.1.2.10 CAS number 9024 43 5 IUBMB EC number 4 1 2 10 GO code 0046593 image width caption Image Mandelonitrile lyase.png thumb Model of mandelonitrile lyase based on PDB entry 1JU2 In enzymology , a mandelonitrile lyase EC number 4.1.2.10 is an enzyme that catalysis catalyzes the chemical reaction mandelonitrile math rightleftharpoons math cyanide benzaldehyde Hence, this enzyme has one substrate biochemistry substrate , mandelonitrile , and two product chemistry products , cyanide and benzaldehyde . This enzyme belongs to the family of lyase s, specifically the aldehyde lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is mandelonitrile benzaldehyde lyase cyanide forming . Other names in common use include hydroxynitrile lyase , R oxynitrilase , oxynitrilase , D oxynitrilase , D alpha hydroxynitrile lyase , and mandelonitrile benzaldehyde lyase . This enzyme participates in cyanoamino acid metabolism . It has 2 cofactor biochemistry cofactors Flavin group flavin , and flavoprotein . Structural studies As of late 2007, only one tertiary structure structure has been solved for this class of enzymes, with the Protein Data Bank PDB accession code PDB link 1JU2 . References reflist 1 cite journal author BECKER W, BENTHIN U, ESCHENHOF E, PFEIL E date 1963 title On the knowledge of cyanhydrin synthesis. II. Purification and properties of hydroxynitrilase from bitter almonds Prunus communis Stokes journal Biochem. Z. volume 337 pages 156&ndash 66 pmid 13970146 cite journal author Becker W and Pfeil E date 1964 title Die Darstellung kristallisierter Oxynitrilase aus bitteren Mandeln Prunus comm. Stks journal ... hydrolase activity employing purified mandelonitrile lyase journal Anal. Biochem. volume 119 pages ... BK, Conn EE date 1986 title Purification and characterization of mandelonitrile lyase from Prunus lyonii ... of multiple forms of mandelonitrile lyase from mature black cherry Prunus serotina Ehrh. seeds ... more details
enzyme Name 2,3 dimethylmalate lyase EC number 4.1.3.32 CAS number 73562 28 4 IUBMB EC number 4 1 3 32 GO code 0047529 image width caption In enzymology , a 2,3 dimethylmalate lyase EC number 4.1.3.32 is an enzyme that catalysis catalyzes the chemical reaction 2R,3S 2,3 dimethylmalate math rightleftharpoons math propanoate pyruvate Hence, this enzyme has one substrate biochemistry substrate , 2R,3S 2,3 dimethylmalate , and two product chemistry products , propanoate and pyruvate . This enzyme belongs to the family of lyase s, specifically the oxo acid lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is 2R,3S 2,3 dimethylmalate pyruvate lyase propanoate forming . Other names in common use include 2,3 dimethylmalate pyruvate lyase , and 2R,3S 2,3 dimethylmalate pyruvate lyase . This enzyme participates in c5 branched dibasic acid metabolism . References reflist 1 cite journal author Pirzer P, Lill U, Eggerer H date 1979 title Nicotinic acid metabolism. 2,3 Dimethylmalate lyase journal Hoppe. Seylers. Z. Physiol. Chem. volume 360 pages 1693&ndash 702 pmid 527937 issue 12 doi 10.1515 bchm2.1979.360.2.1693 cite journal author Alhapel A, Darley DJ, Wagener N, Eckel E, Elsner N, Pierik AJ date 2006 title Molecular and functional analysis of nicotinate catabolism in Eubacterium barkeri journal Proc. Natl. Acad. Sci. U. S. A. volume 103 pages 12341&ndash 6 pmid 16894175 doi 10.1073 pnas.0601635103 issue 33 pmc 1562527 4.1 enzyme stub Category EC 4.1.3 Category Enzymes of unknown structure ... more details
enzyme Name methylisocitrate lyase EC number 4.1.3.30 CAS number 57827 77 7 IUBMB EC number 4 1 3 30 GO code 0046421 image width caption In enzymology , a methylisocitrate lyase EC number 4.1.3.30 is an enzyme that catalysis catalyzes the chemical reaction 2S,3R 3 hydroxybutane 1,2,3 tricarboxylate math rightleftharpoons math pyruvate succinate File MICLreac.png Hence, this enzyme has one substrate biochemistry substrate , 2S,3R 3 hydroxybutane 1,2,3 tricarboxylate also known as 2 methylisocitrate , and two product chemistry products , pyruvate and succinate . The reaction is similar to that of isocitrate lyase , except that an additional methyl group marked with an asterisk in the above scheme is present, meaning that citrate is replaced by methylcitrate and glyoxylate by pyruvate . This enzyme belongs to the family of lyase s, specifically the oxo acid lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is 2S,3R 3 hydroxybutane 1,2,3 tricarboxylate pyruvate lyase succinate forming . Other names in common use include 2 methylisocitrate lyase , MICL , and 2S,3R 3 hydroxybutane 1,2,3 tricarboxylate pyruvate lyase . This enzyme participates in propanoate metabolism . Methylisocitrate lyase was discovered in 1976. ref cite journal author Tabuchi T and Satoh T date 1976 title Distinction between isocitrate lyase and methylisocitrate lyase in Candida lipolytica journal Agric. Biol. Chem. volume 40 pages 1863&ndash 1869 ref Structural studies As of late 2007, 6 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1MUM , PDB link 1O5Q , PDB link 1OQF , PDB link 1UJQ , PDB link ... lyase is used in the methylcitrate cycle ref cite journal author Upton AM and McKinney JD date 2007 ... microorganism s. Methylisocitrate lyase plays a regulatory function in this cycle it is activated ... author Tabuchi T and Satoh T date 1977 title Purification and properties of methylisocitrate lyase ... more details
enzyme Name selenocysteine lyase EC number 4.4.1.16 CAS number 82047 76 5 IUBMB EC number 4 4 1 16 GO code 0009000 image width caption In enzymology , a selenocysteine lyase EC number 4.4.1.16 is an enzyme that catalysis catalyzes the chemical reaction L selenocysteine reduced acceptor math rightleftharpoons math selenide L alanine acceptor Thus, the two substrate biochemistry substrates of this enzyme are L selenocysteine and reduced acceptor , whereas its 3 product chemistry products are selenide , L alanine , and Electron acceptor acceptor . This enzyme belongs to the family of lyase s, specifically the class of carbon sulfur lyases. The systematic name of this enzyme class is L selenocysteine selenide lyase L alanine forming . Other names in common use include selenocysteine reductase , and selenocysteine beta lyase . This enzyme participates in selenoamino acid metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . Structural studies As of late 2007, 4 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1I29 , PDB link 1JF9 , PDB link 1KMJ , and PDB link 1KMK . References reflist 1 cite journal author Esaki N, Nakamura T, Tanaka H, Soda K date 1982 title Selenocysteine lyase, a novel enzyme that specifically acts on selenocysteine. Mammalian distribution and purification and properties of pig liver enzyme journal J. Biol. Chem. volume 257 pages 4386&ndash 91 pmid 6461656 issue 8 enzyme stub Category EC 4.4.1 Category Pyridoxal phosphate enzymes Category Enzymes of known structure ... more details
enzyme Name xanthan lyase EC number 4.2.2.12 CAS number 113573 69 6 IUBMB EC number 4 2 2 12 GO code 0047492 image width caption In enzymology , a xanthan lyase EC number 4.2.2.12 is an enzyme that catalysis catalyzes the chemical reaction of cleaving the beta D mannosyl beta D 1,4 glucuronosyl bond on the polysaccharide xanthan . This enzyme belongs to the family of lyase s, specifically those carbon oxygen lyases acting on polysaccharides. Xanthan lyase was first identified and partially purified in 1987. ref cite journal author Sutherland IW title Xanthan lyases novel enzymes found in various bacterial species journal J. Gen. Microbiol. volume 133 issue 11 pages 3129 34 year 1987 pmid 3446747 ref Xanthan is a polysaccharide secreted by several different bacterial taxa, such as the plant pathogen Xanthomonas campestris , and it consists of a main linear chain based on cellulose with side chains attached to alternate glucosyl glucose residues. ref name Hashimoto cite journal author Hashimoto W, Miki H, Tsuchiya N, Nankai H, Murata K title Xanthan lyase of Bacillus sp. strain GL1 liberates pyruvylated mannose from xanthan side chains journal Appl. Environ. Microbiol. volume 64 issue 10 pages 3765 8 date 1 October 1998 pmid 9758797 pmc 106543 ref These side chains contain three monosaccharide residues. Xanthan lyase is produced by bacteria that degrade this polysaccharide, such as Bacillus , Corynebacterium and Paenibacillus species. ref name Hashimoto ref name Ruijssenaars cite journal author Ruijssenaars HJ, de Bont JA, Hartmans S title A pyruvated mannose specific xanthan lyase involved in xanthan degradation by Paenibacillus alginolyticus XL 1 journal Appl. Environ. Microbiol ... and explosives. ref name Ruijssenaars The use of xanthan lyase as a means of altering the physical ... Crystal structure of Bacillus sp. GL1 xanthan lyase, which acts on the side chains of xanthan journal ... 3129&ndash 34 pmid 3446747 issue 11 DEFAULTSORT Xanthan Lyase Category EC 4.2.2 Category Enzymes of known ... more details
enzyme Name pectin lyase EC number 4.2.2.10 CAS number 9033 35 6 IUBMB EC number 4 2 2 10 GO code 0047490 image width caption In enzymology , a pectin lyase also known as pectolyase is a naturally occurring pectinase a type of enzyme that degrades pectin . It is produced commercially for the food industry from fungi and used to destroy residual fruit starch , known as pectin , in wine and cider . In plant cell culture, it is used in combination with the enzyme cellulase to generate protoplast s by degrading the plant cell walls . Pectin lyase is an enzyme that catalysis 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 lyase s, specifically those carbon oxygen lyases acting on polysaccharides. Nomenclature The systematic name of this enzyme class is 1 4 6 O methyl alpha D galacturonan lyase . Other names in common use include div col colwidth 20em endo pectin lyase, pectin methyltranseliminase, pectin trans eliminase, pectolyase, PL, PMGL, PNL, and polymethylgalacturonic transeliminase. Div col end Structural studies As of late 2007, 3 tertiary structure structures have been solved for this class ... hemp Crotalaria juncea by pectin lyase produced by Aspergillus flavus MTCC 7589 was published in 2008 ... of an acidic pectin lyase produced byAspergillus ficuum strain MTCC 7591 suitable for clarification ... 2008 title Purification and characterization of an alkaline pectin lyase from Aspergillus flavus journal ... of fruit juices by fungal pectin lyase journal Food Biotechnol volume 19 issue 3 pages ... R, Jenkins J year 1997 title Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven ... of pectin lyase B, a novel pectinolytic enzyme from Aspergillus niger journal FEMS Microbiol ... spectrometry to determine the activity and specificity of pectin lyase A journal Carbohydr. Res ... more details
PBB geneid 158 infobox enzyme Name Adenylosuccinate lyase EC number 4.3.2.2 CAS number 9027 81 0 IUBMB ... of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic ... 10.1016 S0969 2126 00 00092 7 ref Adenylosuccinate lyase or adenylosuccinase is an enzyme that in humans is encoded by the ADSL gene . ref name entrez cite web title Entrez Gene Adenylosuccinate lyase ... 48 48.081 08 00 ref Adenylosuccinate lyase converts adenylosuccinate to Adenosine monophosphate ... SAICAR into AICAR and fumarate. Adenylosuccinate lyase is part of the elimination superfamily of enzymes ... lyase deficiency . This protein may use the morpheein model of allosteric regulation ... by ASL Steps in red show the dephosphorylation of ASL s substrates Adenylosuccinate lyase ASL ... journal author Spiegel EK, Colman RF, Patterson D title Adenylosuccinate lyase deficiency journal Mol ... lyase provide new insights into the enzymatic mechanism journal J. Mol. Biol. volume 370 ... and Yeates. ref name pmid10673438 Structure Subunits Adenylosuccinate lyase belongs to the elimination ... lyase has three domains. In Thermotoga maritima , domain 1 contains 7 helices in residues 1 93, including ... where three domains meet. ref name pmid10673438 Adenylosuccinate lyase in humans and Bacillus subtilis ... catalyzed by adenylosuccinate lyase, and enzyme kinetics kinetic studies with APBADP show that the substrates ... mutants in the signature sequence of adenylosuccinate lyase of Bacillus subtilis and Homo sapiens ... Escherichia coli adenylosuccinate lyase identifies His171 as a catalytic acid journal Acta Crystallogr ... pmid 19724117 pmc 2795585 doi 10.1107 S1744309109029674 ref Mutations Adenylosuccinate lyase mutants ... and biophysical analysis of five disease associated human adenylosuccinate lyase mutants journal Biochemistry ... lyase was a concerted catalysis where the hydrogen on the carbon with respect to the leaving ... lyase from Plasmodium falciparum journal Biochim. Biophys. Acta volume 1794 issue 4 pages 642 54 ... more details
enzyme Name pectate lyase EC number 4.2.2.2 CAS number 9015 75 2 IUBMB EC number 4 2 2 2 GO code 0030570 image width caption Pfam box Symbol Amb allergen Name Pectate lyase Amb allergen Pfam PF00544 InterPro IPR002022 SMART SM00656 SCOP PDB PDB 1air PDB 1bn8 PDB 1idj PDB 1idk PDB 1jrg PDB 1jta PDB 1o88 PDB 1o8d PDB 1o8e PDB 1o8f Pectate lyase EC number 4.2.2.2 is an enzyme involved in the maceration and soft rotting of plant tissue. Pectate lyase is responsible for the eliminative cleavage of pectate, yielding oligosaccharides with 4 deoxy alpha D mann 4 enuronosyl groups at their non reducing ... expression of pectate lyase genes might relate to a requirement for pectin degradation during ... kinetics of one member of this family, pectate lyase C pelC 1 from Erwinia chrysanthemi has ... DE, Woody RW title Folding kinetics of the protein pectate lyase C reveal fast forming intermediates ..., Keen NT, Jurnak F title New domain motif the structure of pectate lyase C, a secreted plant virulence ... aII family include Tobacco Nicotiana tabacum, Common tobacco pectate lyase, which is similar to the deduced amino acid sequences of two pollen specific pectate lyase genes identified in Lycopersicon ... A, Lonsdale DM title Isolation and characterization of a tobacco gene with homology to pectate lyase ... to the family of lyase s, specifically those carbon oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is 1 4 alpha D galacturonan lyase . Other names in common use include polygalacturonic transeliminase , pectic acid transeliminase , polygalacturonate lyase , endopectin methyltranseliminase , pectate transeliminase , endogalacturonate transeliminase , pectic acid lyase , pectic lyase , alpha 1,4 D endopolygalacturonic acid lyase , PGA lyase , PPase N , endo alpha 1,4 polygalacturonic acid lyase , polygalacturonic acid lyase , pectin trans eliminase , and Polygalacturonic ... Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change ... more details
enzyme Name hyaluronate lyase EC number 4.2.2.1 CAS number 37259 53 3 IUBMB EC number 4 2 2 1 GO code 0030340 image width caption In enzymology , a hyaluronate lyase EC number 4.2.2.1 is an enzyme that catalysis 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 lyase s, specifically those carbon oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is hyaluronate lyase . Other names in common use include hyaluronidase but cf. internal xref ec num 3,2,1,35 , hyalurononglucosaminidase and internal xref ec num 3,2,1,36 , hyaluronoglucuronidase , glucuronoglycosaminoglycan lyase , spreading factor , and mucinase . Structural studies As of late 2007, 27 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1C82 , PDB link 1EGU , PDB link 1F1S , PDB link 1F9G , PDB link 1I8Q , PDB link 1LOH , PDB link 1LXK , PDB link 1LXM , PDB link 1N7N , PDB link 1N7O , PDB link 1N7P , PDB link 1N7Q , PDB link 1N7R , PDB link 1OJM , PDB link 1OJN , PDB link 1OJO , PDB link 1OJP , PDB link 1W3Y , PDB link 2BRP , PDB link 2BRV , PDB link 2BRW , PDB link 2C3F , PDB link 2DP5 , PDB link 2PK1 , PDB link 2YVV , PDB link 2YW0 , and PDB link 2YX2 . References reflist 1 cite journal author Linker A, Hoffman P, Meyer K, Sampson P and Korn ED date 1960 title The formation of unsaturated disacharides from mucopoly saccharides and their cleavage to alpha keto acid by bacterial enzymes journal J. Biol. Chem. volume 235 pages 3061 5 pmid 13762462 cite journal author MEYER K, RAPPORT MM date 1952 title Hyaluronidases journal Adv. Enzymol. Relat. Subj. Biochem. volume 13 pages 199&ndash 236 pmid 14943668 cite journal author Moran F, Nasuno S, Starr MP date 1968 title Extracellular and intracellular polygllacturonic acid ... more details
Pfam box Symbol Lyase 1 Name Lyase image width caption Pfam PF00206 InterPro IPR000362 SMART Prosite PDOC00147 SCOP 1jsw TCDB OPM family OPM protein PDB PDB3 1yis A 13 309 PDB3 1re5 A 8 300 PDB3 1q5n A 90 301 PDB3 1dof B 88 286 PDB3 1c3u B 3 286 PDB3 1c3c A 3 286 PDB3 1tj7 B 6 301 PDB3 1k62 B 11 305 PDB3 1aos B 20 305 PDB3 1i0a A 11 305 PDB3 1u15 B 11 305 PDB3 1u16 A 11 305 PDB3 1hy0 A 11 305 PDB3 1xwo B 11 305 PDB3 1k7w A 13 307 PDB3 1tjv B 13 307 PDB3 1tju A 13 307 PDB3 1hy1 B 13 307 PDB3 1tjw A 13 307 PDB3 1auw A 19 307 PDB3 1jsw A 13 345 PDB3 1j3u B 13 342 PDB3 1yfm 36 367 PDB3 1kq7 B 12 342 PDB3 1yfe A 12 342 PDB3 1fup A 12 342 PDB3 1fur B 12 342 PDB3 2fus A 12 342 PDB3 1fuq B 12 342 PDB3 1fuo B 12 342 PDB3 1vdk B 11 342 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 ref name PUB00000586 cite journal author Guest JR, Woods SA, Schwartzbach SD title Two biochemically distinct classes of fumarase in Escherichia coli journal Biochim. Biophys. Acta volume 954 issue 1 pages 14 26 year 1988 pmid 3282546 ref ref name PUB00001722 cite journal author Guest JR, Woods SA, Miles JS title Sequence homologies between arginosuccinase, aspartase and fumarase a family of strycturally related enzymes journal FEMS Microbiol. Lett. volume 51 issue pages 181 186 year 1988 ref . The following are examples of members of this family 3 carboxymuconate lactonizing enzyme, EC number 5.5.1.2 3 carboxy cis,cis muconate ... 90 sequence identity with arginosuccinate lyase, showing that it is an example of a hijacked enzyme ... . Arginosuccinase, EC number 4.3.2.1 argininosuccinate lyase , which catalyzes the formation of arginine ... lyase, EC number 4.3.1.1 aspartase , which catalyzes the reversible conversion of aspartate to fumarate ... related. Adenylosuccinase, EC number 4.3.2.2 adenylosuccinate lyase ref name PUB00004940 cite ... more details
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