Merge Cystathionine beta lyase date May 2011 Unreferenced date September 2009 Cystathionine beta lyase is an enzyme used in the biosynthesis of methionine . It is not present in humans. It is classified under EC number 4.4.1.8 . See also Cystathionine Carbon sulfur lyases lyase stub Category Enzymes Category Essential amino acids Category Lyases Category Sulfur amino acids ... more details
enzyme Name cystathionine gamma lyase EC number 4.4.1.1 CAS number 9012 96 8 IUBMB EC number 4 4 1 1 GO code 0004123 image Cysteine Biosynthesis.png width caption Cysteine metabolism. Cystathionase catalyzes the lower reaction. Cystathionine gamma lyase or cystathionase is an enzyme which breaks down cystathionine into cysteine and ketobutyrate . Pyridoxal phosphate is a prosthetic group of this enzyme. Cystathionine gamma lyase also catalyses the following elimination reactions L homoserine to form H sub 2 sub O, NH sub 3 sub and 2 oxobutanoate L cystine , producing thiocysteine, pyruvic acid pyruvate and NH sub 3 sub L cysteine producing pyruvate, NH sub 3 sub and H sub 2 sub S In some bacteria and mammal s, including humans, this enzyme takes part in generating hydrogen sulfide . ref name Wang 2010 cite journal author Wang R title Toxic Gas, Lifesaver journal Scientific American volume issue pages 52 year 2010 month March pmid doi url http www.scientificamerican.com article.cfm?id toxic gas lifesaver ref Examples The following cystathionine gamma lyase is expressed in humans protein Name cystathionase cystathionine gamma lyase caption image width HGNCid 2501 Symbol CTH AltSymbols EntrezGene 1491 OMIM 607657 RefSeq NM 001902 UniProt P32929 PDB ECnumber 4.4.1.1 Chromosome 1 Arm p Band 31.1 LocusSupplementaryData Pathology An deficiency is associated with cystathioninuria . See also Cysteine metabolism External links MeshName Cystathionine gamma lyase References Reflist lyase stub Carbon sulfur lyases Amino acid metabolism enzymes ... more details
Merge Cystathionine beta lyase date May 2011 enzyme Name cystathionine beta lyase EC number 4.4.1.8 CAS number 9055 05 4 IUBMB EC number 4 4 1 8 GO code 0004121 image width caption Orphan date February 2009 In enzymology , a cystathionine beta lyase EC number 4.4.1.8 is an enzyme that catalysis catalyzes the chemical reaction L cystathionine H sub 2 sub O math rightleftharpoons math L homocysteine NH sub 3 sub pyruvate Thus, the two substrate biochemistry substrates of this enzyme are L cystathionine and water H sub 2 sub O , whereas its 3 product chemistry products are L homocysteine , 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 L cystathionine L homocysteine lyase deaminating pyruvate forming . Other names in common use include beta cystathionase , cystine lyase , cystathionine L homocysteine lyase deaminating , and L cystathionine L homocysteine lyase deaminating . This enzyme participates in 5 metabolism metabolic pathways methionine metabolism , cysteine metabolism , selenoamino acid metabolism , nitrogen metabolism , and sulfur metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . Structural studies As of late 2007, 5 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1CL1 , PDB link 1CL2 , PDB link 1IBJ , PDB link 2FQ6 , and PDB link 2GQN . References reflist 1 cite journal author Anderson NW and Thompson JF date 1979 title Cystine lyase beta cystathionase from turnip roots journal Phytochemistry journal Phytochemistry volume 18 pages 1953&ndash 1958 doi 10.1016 S0031 9422 00 82710 7 issue 12 cite journal author FLAVIN M, SLAUGHTER C date 1964 title CYSTATHIONINE CLEAVAGE ENZYMES OF NEUROSPORA journal J. Biol. Chem. volume 239 pages ... of known structure lyase stub ... more details
chembox verifiedrevid 443553935 ImageFile Ref chemboximage correct ?? ImageFile Cystathionine.png ImageName Skeletal formula ImageFile1 Cystathionine 3D balls.png ImageSize1 230px ImageName1 Ball and stick model IUPACName 2 amino 4 2 amino 2 carboxy ethyl thio butanoic acid OtherNames small L small Cystathionine S 2 R 2 Amino 2 carboxyethyl small L small homocysteine Section1 Chembox Identifiers KEGG Ref keggcite correct kegg KEGG C00542 InChI 1 C7H14N2O4S c8 4 6 10 11 1 2 14 3 5 9 7 12 13 h4 5H,1 3,8 9H2, H,10,11 H,12,13 InChIKey ILRYLPWNYFXEMH UHFFFAOYAH ChEMBL Ref ebicite correct EBI ChEMBL 209241 StdInChI Ref stdinchicite correct chemspider StdInChI 1S C7H14N2O4S c8 4 6 10 11 1 2 14 3 5 9 7 12 13 h4 5H,1 3,8 9H2, H,10,11 H,12,13 StdInChIKey Ref stdinchicite correct chemspider StdInChIKey ILRYLPWNYFXEMH UHFFFAOYSA N CASNo Ref cascite correct CAS CASNo 56 88 2 PubChem 834 ChemSpiderID Ref chemspidercite correct chemspider ChemSpiderID 811 ChEBI Ref ebicite correct EBI ChEBI 17755 SMILES O C O C N CSCCC C O O N MeSHName Cystathionine Section2 Chembox Properties Formula C sub 7 sub H sub 14 sub N sub 2 sub O sub 4 sub S MolarMass 222.263 g mol Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition Cystathionine is an intermediate in the synthesis of cysteine . It is generated from homocysteine and serine by cystathionine beta synthase . It is cleaved into cysteine and ketobutyrate by cystathionine gamma lyase . An excess in the urine is called cystathioninuria . File Cysteine Biosynthesis.png thumb left 150px Cysteine metabolism. Cystathionine beta synthase catalyzes the upper reaction and cystathionine gamma lyase catalyzes the lower reaction. Amino acid metabolism intermediates biochem stub Category Sulfur amino acids fr Cystathionine ja ... more details
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
Orphan date July 2011 enzyme Name cystathionine gamma synthase EC number 2.5.1.48 CAS number 9030 70 0 IUBMB EC number 2 5 1 48 GO code 0003962 image width caption In enzymology , a cystathionine gamma synthase EC number 2.5.1.48 is an enzyme that catalysis catalyzes the chemical reaction O sub 4 sub succinyl L homoserine L cysteine math rightleftharpoons math L cystathionine succinate Thus, the two substrate biochemistry substrates of this enzyme are O4 succinyl L homoserine and L cysteine , whereas its two product chemistry products are L cystathionine and succinate . This enzyme belongs to the family of transferase s, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is O4 succinyl L homoserine L cysteine S 3 amino 3 carboxypropyl transferase . Other names in common use include O succinyl L homoserine succinate lyase adding cysteine , O succinylhomoserine thiol lyase , homoserine O transsuccinylase , O succinylhomoserine synthase , O succinylhomoserine synthetase , cystathionine synthase , cystathionine synthetase , homoserine transsuccinylase , 4 O succinyl L homoserine L cysteine , and S 3 amino 3 carboxypropyl transferase . This enzyme participates in 4 metabolism metabolic pathways methionine metabolism , cysteine metabolism , selenoamino acid metabolism , and sulfur metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Flavin M, Slaughter C year 1967 title Enzymatic synthesis of homocysteine or methionine directly from O succinyl homoserine journal Biochim. Biophys. Acta. volume 132 pages 400&ndash 5 pmid 5340123 issue 2 cite journal author Kaplan MM, Flavin M year 1966 title Cystathionine gamma synthetase of Salmonella. Catalytic ... MC, Messerschmidt A year 1998 title Crystal structure of Escherichia coli cystathionine gamma synthase ... 2 title Cystathionine gamma synthase from Arabidopsis thaliana purification and biochemical characterization ... more details
PBB geneid 875 Cystathionine synthase , also known as CBS , is an enzyme EC number 4.2.1.22 that in humans ... homocysteine to cystathionine ref cite web title Entrez Gene CBS cystathionine beta synthase url ... L serine homocysteine L homocysteine math rightleftharpoons math cystathionine L cystathionine ... adoMet . This enzyme belongs to the family of lyase s, to be specific, the hydro lyases, which cleave ... Regulation of human cystathionine beta synthase by S adenosyl L methionine evidence for two catalytically ... url issn ref Nomenclature The systematic name of this enzyme class is L serine hydro lyase adding homocysteine L cystathionine forming . Other names in common use include beta thionase, cysteine synthase, L serine hydro lyase adding homocysteine , methylcysteine synthase, serine sulfhydrase, and serine ... of the CBS enzyme. ref name pmid11483494 The human enzyme cystathionine synthase is a tetrameric ... CG title Redox regulation and reaction mechanism of human cystathionine beta synthase a PLP dependent ... cystathionine beta synthase journal Journal of Inorganic Biochemistry volume 100 issue 12 pages 1988 ... proteins. ref name Ruma CBS has a C terminal inhibitory domain. The C terminal domain of cystathionine ... R title Human cystathionine beta synthase is a target for sumoylation journal Biochemistry volume ... activity enzyme Name cystathionine beta synthase EC number 4.2.1.22 CAS number 9023 99 8 IUBMB ... Cysteine metabolism. Cystathionine beta synthase catalyzes the upper reaction and cystathionine gamma lyase catalyzes the lower reaction. Transsulfuration, catalyzed by CBS, converts homocysteine to cystathionine , which cystathione gamma lyase converts to cysteine . ref name pmid11106665 cite journal ... and molecular characterization of cystathionine beta synthase and serine acetyltransferase from ... at C generate the external aldimine of cystathionine . A final transaldimination reaction releases the final product, cystathionine. ref name Ruma The final product, L cystathionine can ... more details
Refimprove date June 2007 Cystathionine y synthase CGS is an enzyme which plays an important role in regulating the biosynthesis of methionine in bacteria and plants . External links Cite journal author Hacham Y, Avraham T, Amir R title The N terminal region of Arabidopsis cystathionine gamma synthase plays an important regulatory role in methionine metabolism journal Plant Physiol. volume 128 issue 2 pages 454 62 year 2002 month February pmid 11842149 pmc 148908 doi 10.1104 pp.010819 url http www.plantphysiol.org cgi pmidlookup?view long&pmid 11842149 DEFAULTSORT Cystathionine Synthase Category Enzymes Enzyme stub ... 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
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