enzyme Name arachidonateCoAligase EC number 6.2.1.15 CAS number 82047 87 8 IUBMB EC number 6 2 1 15 GO code 0047676 image width caption In enzymology , an arachidonateCoAligase EC number 6.2.1.15 is an enzyme that catalysis catalyzes the chemical reaction ATP arachidonateCoA math rightleftharpoons math AMP diphosphate arachidonoyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , arachidonate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and arachidonoyl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is arachidonateCoAligase AMP forming . This enzyme is also called arachidonoyl CoA synthetase . References reflist 1 cite journal author Wilson DB, Prescott SM, Majerus PW date 1982 title Discovery of an arachidonoyl coenzyme A synthetase in human platelets journal J. Biol. Chem. volume 257 pages 3510&ndash 5 pmid 7061494 issue 7 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure ... more details
enzyme Name 4 Coumarate CoAligase EC number 6.2.1.12 CAS number 37332 51 7 IUBMB EC number 6 2 1 12 GO code 0016207 image width caption In enzymology , a 4 coumarate CoAligase EC number 6.2.1.12 is an enzyme that catalysis catalyzes the chemical reaction ATP 4 coumarate CoA math rightleftharpoons math AMP diphosphate 4 coumaroyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , 4 coumarate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and 4 coumaroyl CoA . This enzyme belongs to the family of ligase s, to be specific those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is 4 coumarate CoAligase AMP forming . Other names in common use include 4 coumaroyl CoA synthetase , p coumaroyl CoAligase , p coumaryl coenzyme A synthetase , p coumaryl CoA synthetase , p coumaryl CoAligase , feruloyl CoAligase , hydroxycinnamoyl CoA synthetase , 4 coumarate coenzyme A ligase , caffeolyl coenzyme A synthetase , p hydroxycinnamoyl coenzyme A synthetase , feruloyl coenzyme A synthetase , sinapoyl coenzyme A synthetase , 4 coumaryl CoA synthetase , hydroxycinnamate CoAligase , p coumaryl CoAligase , p hydroxycinnamic acid CoAligase , and 4CL . This enzyme participates in phenylpropanoid biosynthesis . References reflist 1 cite journal author Gross GG, Zenk MH date 1974 title Isolation and properties of hydroxycinnamate CoAligase from lignifying tissue of Forsythia journal Eur. J. Biochem. volume 42 pages 453 9 pmid 4364250 doi 10.1111 j.1432 1033.1974.tb03359.x issue 2 cite journal author Lindl T, Kreuzaler F, Hahlbrock K date 1973 title Synthesis of p coumaroyl coenzyme a with a partially purified p coumarate CoAligase from cell ... pmid 4699252 issue 2 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure fr 4 coumarate CoAligase ... more details
enzyme Name 4 hydroxybenzoate CoAligase EC number 6.2.1.27 CAS number 119699 80 8 IUBMB EC number 6 2 1 27 GO code 0018859 image width caption In enzymology , a 4 hydroxybenzoate CoAligase EC number 6.2.1.27 is an enzyme that catalysis catalyzes the chemical reaction ATP 4 hydroxybenzoate CoA math rightleftharpoons math AMP diphosphate 4 hydroxybenzoyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , 4 hydroxybenzoate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and 4 hydroxybenzoyl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is 4 hydroxybenzoate CoAligase AMP forming . Other names in common use include 4 hydroxybenzoate CoA synthetase , 4 hydroxybenzoate coenzyme A ligase AMP forming , 4 hydroxybenzoyl coenzyme A synthetase , and 4 hydroxybenzoyl CoAligase . This enzyme participates in benzoate degradation via coa ligation . References reflist 1 cite journal author Merkel SM, Eberhard AE, Gibson J, Harwood CS date 1989 title Involvement of coenzyme A thioesters in anaerobic metabolism of 4 hydroxybenzoate by Rhodopseudomonas palustris journal J. Bacteriol. volume 171 pages 1&ndash 7 pmid 2914844 issue 1 pmc 209545 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure ... more details
enzyme Name phytanate CoAligase EC number 6.2.1.24 CAS number 105238 50 4 IUBMB EC number 6 2 1 24 GO code 0050197 image width caption In enzymology , a phytanate CoAligase EC number 6.2.1.24 is an enzyme that catalysis catalyzes the chemical reaction ATP phytanate CoA math rightleftharpoons math AMP diphosphate phytanoyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , phytanate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and phytanoyl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is phytanate CoAligase AMP forming . This enzyme is also called phytanoyl CoAligase . References reflist 1 cite journal author Muralidharan FN, Muralidharan VB date 1986 title Phytanoyl CoAligase activity in rat liver journal Biochem. Int. volume 13 pages 123&ndash 30 pmid 3753503 issue 1 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure ... more details
enzyme Name dicarboxylate CoAligase EC number 6.2.1.23 CAS number 99332 77 1 IUBMB EC number 6 2 1 23 GO code 0047851 image width caption In enzymology , a dicarboxylate CoAligase EC number 6.2.1.23 is an enzyme that catalysis catalyzes the chemical reaction ATP an alphaomega dicarboxylic acid CoA math rightleftharpoons math AMP diphosphate an omega carboxyacyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , alphaomega dicarboxylic acid , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and omega carboxyacyl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is omega dicarboxylate CoAligase AMP forming . Other names in common use include carboxylyl CoA synthetase , and dicarboxylyl CoA synthetase . References reflist 1 cite journal author Vamecq J, de Hoffmann E, Van Hoof F date 1985 title The microsomal dicarboxylyl CoA synthetase journal Biochem. J. volume 230 pages 683&ndash 93 pmid 4062873 issue 3 pmc 1152672 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure ... more details
enzyme Name acetoacetate CoAligase EC number 6.2.1.16 CAS number 39394 62 2 IUBMB EC number 6 2 1 16 GO code 0030729 image width caption In enzymology , an acetoacetate CoAligase EC number 6.2.1.16 is an enzyme that catalysis catalyzes the chemical reaction ATP acetoacetate CoA math rightleftharpoons math AMP diphosphate acetoacetyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , acetoacetate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and acetoacetyl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is acetoacetate CoAligase AMP forming . This enzyme is also called acetoacetyl CoA synthetase . This enzyme participates in butanoate metabolism . References reflist 1 cite journal author Fukui T, Ito M, Tomita K date 1982 title Purification and characterization of acetoacetyl CoA synthetase from Zoogloea ramigera I 16 M journal Eur. J. Biochem. volume 127 pages 423&ndash 8 pmid 7140777 doi 10.1111 j.1432 1033.1982.tb06889.x issue 2 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure ... more details
enzyme Name biotin CoAligase EC number 6.2.1.11 CAS number 37318 60 8 IUBMB EC number 6 2 1 11 GO code 0047707 image width caption In enzymology , a biotin CoAligase EC number 6.2.1.11 is an enzyme that catalysis catalyzes the chemical reaction ATP biotin CoA math rightleftharpoons math AMP diphosphate biotinyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , biotin , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and biotinyl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is biotin CoAligase AMP forming . Other names in common use include biotinyl CoA synthetase , biotin CoA synthetase , and biotinyl coenzyme A synthetase . This enzyme participates in biotin metabolism . References reflist 1 cite journal author CHRISTNER JE, SCHLESINGER MJ, COON MJ date 1964 title ENZYMATIC ACTIVATION OF BIOTIN. BIOTINYL ADENYLATE FORMATION journal J. Biol. Chem. volume 239 pages 3997&ndash 4005 pmid 14257635 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure ... more details
enzyme Name propionate CoAligase EC number 6.2.1.17 CAS number 55326 49 3 IUBMB EC number 6 2 1 17 GO code 0050218 image width caption In enzymology , a propionate CoAligase EC number 6.2.1.17 is an enzyme that catalysis catalyzes the chemical reaction ATP propanoate CoA math rightleftharpoons math AMP diphosphate propanoyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , propanoate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and propanoyl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is propanoate CoAligase AMP forming . This enzyme is also called propionyl CoA synthetase . This enzyme participates in propanoate metabolism . References reflist 1 cite journal author Ricks CA, Cook RM date 1981 title Regulation of volatile fatty acid uptake by mitochondrial acyl CoA synthetases of bovine liver journal J. Dairy. Sci. volume 64 pages 2324&ndash 35 pmid 7341659 doi 10.3168 jds.S0022 0302 81 82854 8 issue 12 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure ... more details
enzyme Name phenylacetate CoAligase EC number 6.2.1.30 CAS number 57219 71 3 IUBMB EC number 6 2 1 30 GO code 0047475 image width caption In enzymology , a phenylacetate CoAligase is an enzyme that catalysis catalyzes the chemical reaction ATP phenylacetate CoA math rightleftharpoons math AMP diphosphate phenylacetyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , phenylacetic acid phenylacetate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and phenylacetyl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is phenylacetate CoAligase AMP forming . Other names in common use include phenylacetyl CoAligase , PA CoAligase , and phenylacetyl CoAligase AMP forming . This enzyme participates in tyrosine metabolism and phenylalanine metabolism . References reflist 1 cite journal author Martinez Blanco H, Reglero A, Rodriguez Aparicio LB, Luengo JM date 1990 title Purification and biochemical characterization of phenylacetyl CoAligase from Pseudomonas putida. A specific enzyme for the catabolism of phenylacetic acid journal J. Biol. Chem. volume 265 pages 7084&ndash 90 pmid 2324116 issue 12 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure ... more details
enzyme Name glutarate CoAligase EC number 6.2.1.6 CAS number 9023 68 1 IUBMB EC number 6 2 1 6 GO code 0047948 image width caption In enzymology , a glutarate CoAligase EC number 6.2.1.6 is an enzyme that catalysis catalyzes the chemical reaction ATP glutarate CoA math rightleftharpoons math ADP phosphate glutaryl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , glutarate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and glutaryl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is glutarate CoAligase ADP forming . Other names in common use include glutaryl CoA synthetase , and glutaryl coenzyme A synthetase . This enzyme participates in fatty acid metabolism and lysine degradation . References reflist 1 cite journal author Menon GKK, Friedman DL and Stern JR year 1960 title Enzymic synthesis of glutaryl coenzyme A journal Biochim. Biophys. Acta volume 44 pages 375&ndash 377 doi 10.1016 0006 3002 60 91583 3 pmid 13769477 Category EC 6.2.1 Category Enzymes of unknown structure ligase stub ... more details
enzyme Name malate CoAligase EC number 6.2.1.9 CAS number 37318 58 4 IUBMB EC number 6 2 1 9 GO code 0050074 image width caption In enzymology , a malate CoAligase EC number 6.2.1.9 is an enzyme that catalysis catalyzes the chemical reaction ATP malate CoA math rightleftharpoons math ADP phosphate malyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , malate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and malyl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is malate CoAligase ADP forming . Other names in common use include malyl CoA synthetase , malyl coenzyme A synthetase , and malate thiokinase . This enzyme participates in glyoxylate and dicarboxylate metabolism . References reflist 1 cite journal author Mue S, Tuboi S and Kikuchi G year 1964 month December title On malyl coenzyme A synthetase journal J. Biochem. volume 56 pages 545&ndash 551 pmid 14244056 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure ... more details
enzyme Name oxalate CoAligase EC number 6.2.1.8 CAS number 37318 57 3 IUBMB EC number 6 2 1 8 GO code 0050203 image width caption In enzymology , an oxalate CoAligase EC number 6.2.1.8 is an enzyme that catalysis catalyzes the chemical reaction ATP oxalate CoA math rightleftharpoons math AMP diphosphate oxalyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , oxalate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and oxalyl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is oxalate CoAligase AMP forming . Other names in common use include oxalyl CoA synthetase , and oxalyl coenzyme A synthetase . This enzyme participates in glyoxylate and dicarboxylate metabolism . References reflist 1 cite journal author Giovanelli J date 1966 title Oxalyl coenzyme A synthetase from pea seeds journal Biochim. Biophys. Acta. volume 118 pages 124&ndash 43 pmid 4288975 issue 1 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure ... more details
enzyme Name 2 furoate CoAligase EC number 6.2.1.31 CAS number 122320 08 5 IUBMB EC number 6 2 1 31 GO code 0047541 image width caption In enzymology , a 2 furoate CoAligase EC number 6.2.1.31 is an enzyme that catalysis catalyzes the chemical reaction ATP 2 furoate CoA math rightleftharpoons math AMP diphosphate 2 furoyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , 2 furoate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and 2 furoyl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is 2 furoate CoAligase AMP forming . This enzyme is also called 2 furoyl coenzyme A synthetase . References reflist 1 cite journal author Koenig K, Andreesen JR date 1989 title Molybdenum Involvement in Aerobic Degradation of 2 Furoic Acid by Pseudomonas putida Fu1 journal Appl. Environ. Microbiol. volume 55 pages 1829&ndash 1834 pmid 16347977 issue 7 pmc 202958 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure ... more details
enzyme Name anthranilate CoAligase EC number 6.2.1.32 CAS number 112692 58 7 IUBMB EC number 6 2 1 32 GO code 0018860 image width caption In enzymology , an anthranilate CoAligase EC number 6.2.1.32 is an enzyme that catalysis catalyzes the chemical reaction ATP anthranilate CoA math rightleftharpoons math AMP diphosphate anthranilyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , anthranilate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and anthranilyl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is anthranilate CoAligase AMP forming . Other names in common use include anthraniloyl coenzyme A synthetase , 2 aminobenzoate CoAligase , 2 aminobenzoate coenzyme A ligase , and 2 aminobenzoate coenzyme A ligase . This enzyme participates in 3 metabolism metabolic pathways carbazole degradation , benzoate degradation via coa ligation , and acridone alkaloid biosynthesis . References reflist 1 cite journal author Altenschmidt U, Eckerskorn C, Fuchs G date 1990 title Evidence that enzymes of a novel aerobic 2 amino benzoate metabolism in denitrifying Pseudomonas are coded on a small plasmid journal Eur. J. Biochem. volume 194 pages 647&ndash 53 pmid 2176602 doi 10.1111 j.1432 1033.1990.tb15664.x issue 2 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure ... more details
enzyme Name butyrate CoAligase EC number 6.2.1.2 CAS number 9080 51 7 IUBMB EC number 6 2 1 2 GO code 0047760 image width caption In enzymology , a butyrate CoAligase EC number 6.2.1.2 is an enzyme that catalysis catalyzes the chemical reaction ATP an acid CoA math rightleftharpoons math AMP diphosphate an acyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , acid , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and acyl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is butanoate CoAligase AMP forming . Other names in common use include butyryl CoA synthetase , fatty acid thiokinase medium chain , acyl activating enzyme , fatty acid elongase , fatty acid activating enzyme , fatty acyl coenzyme A synthetase , medium chain acyl CoA synthetase , butyryl coenzyme A synthetase , L 3 hydroxybutyryl CoAligase , and short chain acyl CoA synthetase . This enzyme participates in butanoate metabolism . References reflist 1 cite journal author MAHLER HR, WAKIL SJ, BOCK RM date 1953 title Studies on fatty acid oxidation. I. Enzymatic activation of fatty acids journal J. Biol. Chem. volume 204 pages 453&ndash 68 pmid 13084616 issue 1 cite journal author Massaro EJ and Lennarz WJ date 1965 title The partial purification and characterization of a bacterial fatty acyl coenzyme A synthetase journal Biochemistry volume 4 pages 85&ndash 90 doi 10.1021 bi00877a015 pmid 14285249 cite journal author Websterlt JR, Gerowin LD and Rakita L date 1965 title Purification and characteristics of a butyryl coenzyme A synthetase from bovine heart mitochondria journal J. Biol. Chem. volume 240 pages 29&ndash 33 pmid 14253428 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure ... more details
enzyme Name citrate CoAligase EC number 6.2.1.18 CAS number 856428 87 0 IUBMB EC number 6 2 1 18 GO code 0047779 image width caption In enzymology , a citrate CoAligase EC number 6.2.1.18 is an enzyme that catalysis catalyzes the chemical reaction ATP citrate CoA math rightleftharpoons math ADP phosphate 3S citryl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , citrate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and 3S citryl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is citrate CoAligase ADP forming . Other names in common use include citryl CoA synthetase , citrate CoAligase , and citrate thiokinase . This enzyme participates in citric acid cycle . References reflist 1 cite journal author Lill U, Schreil A, Eggerer H date 1982 title Isolation of enzymically active fragments formed by limited proteolysis of ATP citrate lyase journal Eur. J. Biochem. volume 125 pages 645&ndash 50 pmid 6749502 doi 10.1111 j.1432 1033.1982.tb06731.x issue 3 cite journal author Aoshima M, Ishii M, Igarashi Y date 2004 title A novel enzyme, citryl CoA synthetase, catalysing the first step of the citrate cleavage reaction in Hydrogenobacter thermophilus TK 6 journal Mol. Microbiol. volume 52 pages 751&ndash 61 pmid 15101981 doi 10.1111 j.1365 2958.2004.04009.x issue 3 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure ... more details
enzyme Name benzoate CoAligase EC number 6.2.1.25 CAS number 95329 17 2 IUBMB EC number 6 2 1 25 GO code 0018858 image width caption In enzymology , a benzoate CoAligase EC number 6.2.1.25 is an enzyme that catalysis catalyzes the chemical reaction ATP benzoate CoA math rightleftharpoons math AMP diphosphate benzoyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , benzoate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and benzoyl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is benzoate CoAligase AMP forming . Other names in common use include benzoate coenzyme A ligase , benzoyl coenzyme A synthetase , and benzoyl CoA synthetase AMP forming . This enzyme participates in benzoate degradation via coa ligation . 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 2V7B . References reflist 1 cite journal author Hutber GN and Ribbons DW date 1983 title Involvement of coenzyme A esters in the metabolism of benzoate and cyclohexanecarboxylate by Rhodopseudomonas palustris journal J. Gen. Microbiol. volume 129 pages 2413&ndash 2420 cite journal author Schennen U, Braun K, Knackmuss HJ date 1985 title Anaerobic degradation of 2 fluorobenzoate by benzoate degrading, denitrifying bacteria journal J. Bacteriol. volume 161 pages 321&ndash 5 pmid 2857161 issue 1 pmc 214874 ligase stub Category EC 6.2.1 Category Enzymes of known structure ... more details
enzyme Name 6 carboxyhexanoate CoAligase EC number 6.2.1.14 CAS number 55467 50 0 IUBMB EC number 6 2 1 14 GO code 0042410 image width caption In enzymology , a 6 carboxyhexanoate CoAligase EC number 6.2.1.14 is an enzyme that catalysis catalyzes the chemical reaction ATP 6 carboxyhexanoate CoA math rightleftharpoons math AMP diphosphate 6 carboxyhexanoyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , 6 carboxyhexanoate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and 6 carboxyhexanoyl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is 6 carboxyhexanoate CoAligase AMP forming . Other names in common use include 6 carboxyhexanoyl CoA synthetase , and pimelyl CoA synthetase . This enzyme participates in biotin metabolism . References reflist 1 cite journal author Izumi Y, Morita H, Sato K, Tani Y, Ogata K date 1972 title Synthesis of biotin vitamers from pimelic acid and coenzyme A by cell free extracts of various bacteria journal Biochim. Biophys. Acta. volume 264 pages 210&ndash 3 pmid 4623286 issue 1 cite journal author Izumi Y, Morita H, Tani Y and Ogata K date 1974 title The pimelyl CoA synthetase responsible for the first step in biotin biosynthesis by microorganisms journal Agric. Biol. Chem. volume 38 pages 2257&ndash 2262 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure ... more details
Orphan date November 2010 enzyme Name 4 chlorobenzoate CoAligase EC number 6.2.1.33 CAS number 141583 20 2 IUBMB EC number 6 2 1 33 GO code 0018861 image width caption In enzymology , a 4 chlorobenzoate CoAligase EC number 6.2.1.33 is an enzyme that catalysis catalyzes the chemical reaction 4 chlorobenzoate CoA ATP math rightleftharpoons math 4 chlorobenzoyl CoA AMP diphosphate The 3 substrate biochemistry substrates of this enzyme are 4 chlorobenzoate , coenzyme A CoA , and adenosine triphosphate ATP , whereas its 3 product chemistry products are 4 chlorobenzoyl CoA , adenosine monophosphate AMP , and diphosphate . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is 4 chlorobenzoate CoAligase . This enzyme participates in 2,4 dichlorobenzoate degradation . It employs one cofactor biochemistry cofactor , magnesium . Structural studies As of late 2007, two tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1T5D and PDB link 1T5H . References reflist 1 cite journal author Dunaway Mariano D, Babbitt PC year 1994 title On the origins and functions of the enzymes of the 4 chlorobenzoate to 4 hydroxybenzoate converting pathway journal Biodegradation. volume 5 pages 259&ndash 76 pmid 7765837 doi 10.1007 BF00696464 issue 3 4 cite journal author Loffler F, Muller R, Lingens F year 1992 title Purification and properties of 4 halobenzoate coenzyme A ligase from Pseudomonas sp. CBS3 journal Biol. Chem. Hoppe Seyler volume 373 pages 1001&ndash 7 pmid 1418673 issue 10 cite journal author Chang KH, Liang PH, Beck W, Scholten JD, Dunaway Mariano D year 1992 title Isolation and characterization of the three polypeptide components of 4 chlorobenzoate dehalogenase from Pseudomonas sp. strain CBS 3 journal ... EC 6.2.1 Category Magnesium enzymes Category Enzymes of known structure ligase stub ... more details
enzyme Name o succinylbenzoate CoAligase EC number 6.2.1.26 CAS number 72506 70 8 IUBMB EC number 6 2 1 26 GO code 0008756 image width caption In enzymology , an o succinylbenzoate CoAligase EC number 6.2.1.26 is an enzyme that catalysis catalyzes the chemical reaction ATP o succinylbenzoate CoA math rightleftharpoons math AMP diphosphate o succinylbenzoyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , o succinylbenzoate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and o succinylbenzoyl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is 2 succinylbenzoate CoAligase AMP forming . Other names in common use include 2 succinylbenzoyl coenzyme A synthetase , and 2 succinylbenzoate CoAligase AMP forming . This enzyme participates in ubiquinone biosynthesis . Structural studies As of late 2007, two tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 2OKT and PDB link 2OLA . References reflist 1 cite journal author Heide L, Arendt S, Leistner E date 1982 title Enzymatic synthesis, characterization, and metabolism of the coenzyme A ester of o succinylbenzoic acid, an intermediate in menaquinone vitamin K2 biosynthesis journal J. Biol. Chem. volume 257 pages 7396&ndash 400 pmid 7045104 issue 13 cite journal author Kolkmann R, Leistner E date 1987 title 4 2 Carboxyphenyl 4 oxobutyryl coenzyme A ester, an intermediate in vitamin K2 menaquinone biosynthesis journal Z. Naturforsch. C . volume 42 pages 1207&ndash 14 pmid 2966501 issue 11 12 cite journal author Meganathan R, Bentley R date 1979 title Menaquinone vitamin K2 biosynthesis conversion of o succinylbenzoic acid to 1,4 dihydroxy ... 8 pmid 500558 issue 1 pmc 216783 ligase stub Category EC 6.2.1 Category Enzymes of known structure ... more details
enzyme Name biotin methylcrotonoyl CoA carboxylase ligase EC number 6.3.4.11 CAS number 37318 68 6 IUBMB EC number 6 3 4 11 GO code 0004078 image width caption In enzymology , a biotin methylcrotonoyl CoA carboxylase ligase EC number 6.3.4.11 is an enzyme that catalysis catalyzes the chemical reaction ATP biotin apo 3 methylcrotonoyl CoA carbon dioxide ligase ADP forming math rightleftharpoons math AMP diphosphate 3 methylcrotonoyl CoA carbon dioxide ligase ADP forming The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , biotin , and apo 3 methylcrotonoyl CoA carbon dioxide ligase ADP forming , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and 3 methylcrotonoyl CoA carbon dioxide ligase ADP forming . This enzyme belongs to the family of ligase s, specifically those forming generic carbon nitrogen bonds. The systematic name of this enzyme class is biotin apo 3 methylcrotonoyl CoA carbon dioxide ligase ADP forming ligase AMP forming . Other names in common use include biotin methylcrotonoyl CoA carboxylase synthetase , biotin beta methylcrotonyl coenzyme A carboxylase synthetase , beta methylcrotonyl coenzyme A holocarboxylase synthetase , and holocarboxylase synthetase . This enzyme participates in biotin metabolism . References reflist 1 cite journal author Hopner T, Knappe J date 1965 title Synthesis of biotin in beta methylcrotonyl CoA carboxylase by holocarboxylase synthetase journal Biochem. Z. volume 342 pages 190&ndash 206 pmid 5867144 issue 2 ligase stub Category EC 6.3.4 Category Enzymes of unknown structure ... more details
enzyme Name acid CoAligase GDP forming EC number 6.2.1.10 CAS number 37318 59 5 IUBMB EC number 6 2 1 10 GO code 0047612 image width caption In enzymology , an acid CoAligase GDP forming EC number 6.2.1.10 is an enzyme that catalysis catalyzes the chemical reaction GTP an acid CoA math rightleftharpoons math GDP phosphate acyl CoA The 3 substrate biochemistry substrates of this enzyme are guanosine triphosphate GTP , acid , and coenzyme A CoA , whereas its 3 product chemistry products are guanosine diphosphate GDP , phosphate , and acyl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is acid CoAligase GDP forming . Other names in common use include acyl CoA synthetase GDP forming , and acyl coenzyme A synthetase guanosine diphosphate forming . References reflist 1 cite journal author Rossi CR and Gibson DM date 1964 title Activation of fatty acids by a guanosine triphosphate specific thiokinase from liver mitochondria journal J. Biol. Chem. volume 239 pages 1694&ndash 1699 pmid 14213337 url http www.jbc.org content 239 6 1694.full.pdf format PDF issue 6 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure ... more details
enzyme Name 3 alpha,7 alpha dihydroxy 5 beta cholestanate CoAligase EC number 6.2.1.28 CAS number 118732 03 9 IUBMB EC number 6 2 1 28 GO code 0047476 image width caption In enzymology , a 3alpha,7alpha dihydroxy 5beta cholestanate CoAligase EC number 6.2.1.28 is an enzyme that catalysis catalyzes the chemical reaction ATP 25R 3alpha,7alpha dihydroxy 5beta cholestan 26 oate CoA math rightleftharpoons math AMP diphosphate 25R 3alpha,7alpha dihydroxy 5beta cholestanoyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , 25R 3alpha,7alpha dihydroxy 5beta cholestan 26 oate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and 25R 3alpha,7alpha dihydroxy 5beta cholestanoyl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is 25R 3alpha,7alpha dihydroxy 5beta cholestan 26 oate CoAligase AMP forming . Other names in common use include 3alpha,7alpha dihydroxy 5beta cholestanoyl coenzyme A synthetase , DHCA CoAligase , and 3alpha,7alpha dihydroxy 5beta cholestanate CoAligase AMP forming . This enzyme participates in bile acid biosynthesis . References reflist 1 cite journal author Prydz K, Kase BF, Bjorkhem I, Pedersen JI date 1988 title Subcellular localization of 3 alpha, 7 alpha dihydroxy and 3 alpha,7 alpha,12 alpha trihydroxy 5 beta cholestanoyl coenzyme A ligase s in rat liver journal J. Lipid. Res. volume 29 pages 997&ndash 1004 pmid 3183523 issue 8 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure ... more details
enzyme Name biotin methylmalonyl CoA carboxytransferase ligase EC number 6.3.4.9 CAS number 37318 66 4 IUBMB EC number 6 3 4 9 GO code 0004079 image width caption In enzymology , a biotin methylmalonyl CoA carboxytransferase ligase EC number 6.3.4.9 is an enzyme that catalysis catalyzes the chemical reaction ATP biotin apo methylmalonyl CoA pyruvate carboxytransferase math rightleftharpoons math AMP diphosphate methylmalonyl CoA pyruvate carboxytransferase The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , biotin , and apo methylmalonyl CoA pyruvate carboxytransferase , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and methylmalonyl CoA pyruvate carboxytransferase . This enzyme belongs to the family of ligase s, specifically those forming generic carbon nitrogen bonds. The systematic name of this enzyme class is biotin apo methylmalonyl CoA pyruvate carboxytransferase ligase AMP forming . Other names in common use include biotin methylmalonyl CoA carboxyltransferase synthetase , biotin methylmalonyl coenzyme A carboxyltransferase synthetase , biotin transcarboxylase synthetase , methylmalonyl coenzyme A holotranscarboxylase synthetase , biotin methylmalonyl CoA carboxyltransferase ligase , biotin apo methylmalonyl CoA pyruvate carboxyltransferase ligase , and AMP forming . This enzyme participates in biotin metabolism . References reflist 1 cite journal author Lane MD, Young DL and Lynen F date 1964 title The enzymatic synthesis of holotranscarboxylase from apotranscarboxylase and biotin. I. Purification of the apoenzyme and synthetase characteristics of the reaction journal J. Biol. Chem. volume 239 pages 2858&ndash 2864 ligase stub Category EC 6.3.4 Category Enzymes of unknown structure ... more details
enzyme Name biotin acetyl CoA carboxylase ligase EC number 6.3.4.15 CAS number 37340 95 7 IUBMB EC number 6 3 4 15 GO code 0004077 image width caption In enzymology , a biotin acetyl CoA carboxylase ligase EC number 6.3.4.15 is an enzyme that catalysis catalyzes the chemical reaction ATP biotin apo acetyl CoA carbon dioxide ligase ADP forming math rightleftharpoons math AMP diphosphate acetyl CoA carbon dioxide ligase ADP forming The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , biotin , and apo acetyl CoA carbon dioxide ligase ADP forming , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and acetyl CoA carbon dioxide ligase ADP forming . This enzyme belongs to the family of ligase s, specifically those forming generic carbon nitrogen bonds. The systematic name of this enzyme class is biotin apo acetyl CoA carbon dioxide ligase ADP forming ligase AMP forming . Other names in common use include biotin acetyl CoA carboxylase synthetase , biotin acetyl coenzyme A carboxylase synthetase , acetyl coenzyme A holocarboxylase synthetase , acetyl CoA holocarboxylase synthetase , biotin apocarboxylase ligase , Biotin holoenzyme synthetase , and HCS . This enzyme participates in biotin metabolism . Structural studies As of late 2007, 29 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1BIA , PDB link 1BIB , PDB link 1HXD , PDB link 1WNL , PDB link 1WPY , PDB link 1WQ7 , PDB link 1WQW , PDB link 1X01 , PDB link 2CGH , PDB link 2DEQ , PDB link 2DJZ , PDB link 2DKG , PDB link 2DTH , PDB link 2DTI , PDB link 2DTO , PDB link 2DVE , PDB link 2DXT , PDB link 2DXU , PDB link 2DZ9 , PDB link 2DZC , PDB link 2E10 , PDB link 2E3Y , PDB link 2E41 , PDB link 2E64 , PDB link 2E65 , PDB link 2EAY , PDB link 2EWN , PDB link 2FYK , and PDB link ... 145 pages 545&ndash 8 pmid 239688 issue 3 pmc 1165255 ligase stub Category EC 6.3.4 Category ... more details
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