enzyme Name imidazoleacetate phosphoribosyldiphosphate ligase EC number 6.3.4.8 CAS number 37318 65 3 IUBMB EC number 6 3 4 8 GO code 0047483 image width caption In enzymology , an imidazoleacetate phosphoribosyldiphosphate ligase EC number 6.3.4.8 is an enzyme that catalysis catalyzes the chemical reaction ATP imidazole 4 acetate 5 phosphoribosyl diphosphate math rightleftharpoons math ADP phosphate 1 5 phosphoribosyl imidazole 4 acetate diphosphate The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , imidazole 4 acetate , and 5 phosphoribosyl diphosphate , whereas its 4 product chemistry products are adenosine diphosphate ADP , phosphate , 1 5 phosphoribosyl imidazole 4 acetate , and diphosphate . This enzyme belongs to the family of ligase s, specifically those forming generic carbon nitrogen bonds. The systematic name of this enzyme class is imidazoleacetate 5 phosphoribosyl diphosphate ligase ADP and diphosphate forming . This enzyme is also called 5 phosphoribosylimidazoleacetate synthetase . This enzyme participates in histidine metabolism . References reflist 1 cite journal author CROWLEY GM date 1964 title THE ENZYMATIC SYNTHESIS OF 5 PHOSPHORIBOSYLIMIDAZOLEACETIC ACID journal J. Biol. Chem. volume 239 pages 2593&ndash 601 pmid 14235540 ligase stub Category EC 6.3.4 Category Enzymes of unknown structure ... more details
enzyme Name malate CoA ligase 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 CoA ligase 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 CoA ligase 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 CoA ligase 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 CoA ligase 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 CoA ligase 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 propionate CoA ligase 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 CoA ligase 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 CoA ligase 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 Journal of Dairy Science 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 ribose 5 phosphate ammonia ligase EC number 6.3.4.7 CAS number 9082 52 4 IUBMB EC number 6 3 4 7 GO code 0050260 image width caption In enzymology , a ribose 5 phosphate ammonia ligase EC number 6.3.4.7 is an enzyme that catalysis catalyzes the chemical reaction ATP ribose 5 phosphate NH sub 3 sub math rightleftharpoons math ADP phosphate 5 phosphoribosylamine The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , ribose 5 phosphate , and ammonia NH sub 3 sub , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and 5 phosphoribosylamine . This enzyme belongs to the family of ligase s, specifically those forming generic carbon nitrogen bonds. The systematic name of this enzyme class is ribose 5 phosphate ammonia ligase ADP forming . Other names in common use include 5 phosphoribosylamine synthetase , ribose 5 phosphate aminotransferase , and ammonia ribose 5 phosphate aminotransferase . This enzyme participates in purine metabolism . References reflist 1 cite journal author Reem GH date 1968 title Enzymatic synthesis of 5 phosphoribosylamine from ribose 5 phosphate and ammonia, an alternate first step in purine biosynthesis journal J. Biol. Chem. volume 243 pages 5695&ndash 701 pmid 5699059 issue 21 ligase stub Category EC 6.3.4 Category Enzymes of unknown structure ... more details
enzyme Name tubulin tyrosine ligase EC number 6.3.2.25 CAS number 60321 03 1 IUBMB EC number 6 3 2 25 GO code 0004835 image width caption In enzymology , a tubulin tyrosine ligase EC number 6.3.2.25 is an enzyme that catalysis catalyzes the chemical reaction ATP detyrosinated alpha tubulin L tyrosine math rightleftharpoons math alpha tubulin ADP phosphate The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , detyrosinated alpha tubulin , and L tyrosine , whereas its 3 product chemistry products are alpha tubulin , adenosine diphosphate ADP , and phosphate . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds as acid D amino acid ligases peptide synthases . The systematic name of this enzyme class is alpha tubulin L tyrosine ligase ADP forming . References reflist 1 cite journal author Wehland J, Schroder HC, Weber K date 1986 title Isolation and purification of tubulin tyrosine ligase journal Methods Enzymol. volume 134 pages 170&ndash 9 pmid 3821560 doi 10.1016 0076 6879 86 34086 2 cite journal author Rudiger M, Wehland J, Weber K date 1994 title The carboxy terminal peptide of detyrosinated alpha tubulin provides a minimal system to study the substrate specificity of tubulin tyrosine ligase journal Eur. J. Biochem. volume 220 pages 309&ndash 20 pmid 7510228 doi 10.1111 j.1432 1033.1994.tb18627.x issue 2 ligase stub Category EC 6.3.2 Category Enzymes of unknown structure ... more details
Orphan date November 2010 enzyme Name 4 chlorobenzoate CoA ligase 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 CoA ligase 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 CoA ligase . 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 benzoate CoA ligase 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 CoA ligase 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 CoA ligase 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 butyrate CoA ligase 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 CoA ligase 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 CoA ligase 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 CoA ligase , 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 CoA ligase 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 CoA ligase 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 CoA ligase ADP forming . Other names in common use include citryl CoA synthetase , citrate CoA ligase , 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 glutamine tRNA ligase EC number 6.1.1.18 CAS number 9075 59 6 IUBMB EC number 6 1 1 18 GO code 0004819 image width caption In enzymology , a glutamine tRNA ligase EC number 6.1.1.18 is an enzyme that catalysis catalyzes the chemical reaction ATP L glutamine tRNAGln math rightleftharpoons math AMP diphosphate L glutaminyl tRNAGln The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L glutamine , and tRNA Gln , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L glutaminyl tRNA Gln . This enzyme belongs to the family of ligase s, to be specific those forming carbon oxygen bonds in aminoacyl tRNA and related compounds. The systematic name of this enzyme class is L glutamine tRNAGln ligase AMP forming . Other names in common use include glutaminyl tRNA synthetase , glutaminyl transfer RNA synthetase , glutaminyl transfer ribonucleate synthetase , glutamine tRNA synthetase , glutamine translase , glutamate tRNA ligase , glutaminyl ribonucleic acid , and GlnRS . This enzyme participates in glutamate metabolism and aminoacyl trna biosynthesis . Structural studies As of late 2007, 15 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1EUQ , PDB link 1EUY , PDB link 1EXD , PDB link 1GSG , PDB link 1GTR , PDB link 1GTS , PDB link 1NYL , PDB link 1O0B , PDB link 1O0C , PDB link 1QRS , PDB link 1QRT , PDB link 1QRU , PDB link 1QTQ , PDB link 1ZJW , and PDB link 2HZ7 . References reflist 1 cite journal author Ravel JM, Wang S, Heinemeyer C and Shive W year 1965 title Glutamyl and glutaminyl ribonucleic acid synthetases of Escherichia coli W. Separation, properties, and stimulation of adenosine triphosphate pyrophosphate exchange by acceptor ribonucleic acid journal J. Biol. Chem. volume 240 pages 432&ndash 438 pmid 14253448 Ligases Category EC 6.1.1 Category Enzymes of known structure ligase stub ... more details
The ligase chain reaction LCR is a method of DNA amplification . While the better known PCR carries out the amplification by polymerizing nucleotides, LCR instead amplifies the nucleic acid used as the probe. For each of the two DNA strands, two partial probes are ligated to form the actual one thus, LCR uses two enzymes a DNA polymerase and a DNA ligase . Each cycle results in a doubling of the target nucleic acid molecule. A key advantage of LCR is greater specificity as compared to PCR. ref Wiedmann M, Wilson WJ, Czajka J, Luo J, Barany F, Batt CA. Ligase chain reaction LCR overview and applications. PCR Methods and Applications 1994 Feb 3 4 S51 64 PMID 8173509 ref Target conditions It has been widely used for the detection of Point mutation single base mutation s, as in genetic disease s. ref Barany F. Genetic disease detection and DNA amplification using cloned thermostable ligase. Proc Natl Acad Sci U S A. 1991 Jan 1 88 1 189 93. PMID 1986365 ref LCR and PCR may be used to detect gonorrhea and chlamydia infection chlamydia , and may be performed on first catch urine samples, providing easy collection and a large yield of organisms. Endogenous inhibitors limit the Sensitivity and specificity sensitivity , but if this effect could be eliminated, LCR and PCR would have clinical advantages over any other methods of diagnosing gonorrhea and chlamydia. ref http dx.doi.org 10.1016 S1068 607X 97 00044 9 New diagnostic tests for gonorrhea and chlamydia Gregory J. Locksmith MD. Department of Obstetrics and Gynecology, University of Florida College of Medicine, Gainesville, Florida, USA. Available online 13 February 1998. ref References reflist General reading Walker, J. M., & Rapley, R. 2005 . Medical biomethods handbook. Totowa, N.J. Humana Press. ISBN 9781592598700 DEFAULTSORT Ligase Chain Reaction Category DNA profiling techniques Category Amplifiers Category Molecular biology techniques de Ligase Kettenreaktion es Reaccion en cadena de la ligasa it Reazione a catena ... more details
enzyme Name D aspartate ligase EC number 6.3.1.12 CAS number IUBMB EC number 6 3 1 12 GO code image width caption Orphan date February 2009 In enzymology , a D aspartate ligase EC number 6.3.1.12 is an enzyme that catalysis catalyzes the chemical reaction ATP D aspartate beta GlcNAc 1 4 Mur sub 2 sub Ac oyl L Ala gamma D Glu L Lys D Ala D Ala n math rightleftharpoons math beta GlcNAc 1 4 Mur sub 2 sub Ac oyl L Ala gamma D Glu 6 N beta D Asp L Lys D Ala D Ala n ADP phosphate The 4 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , D aspartate , beta GlcNAc 1 4 Mur2Ac oyl L Ala gamma D Glu L Lys D Ala D , and Ala n , whereas its 4 product chemistry products are beta GlcNAc 1 4 Mur2Ac oyl L Ala gamma D Glu 6 N beta D Asp L , Lys D Ala D Ala n , adenosine diphosphate ADP , and phosphate . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds as acid D ammonia or amine ligases amide synthases . The systematic name of this enzyme class is D aspartate beta GlcNAc 1 4 Mur2Ac oyl L Ala gamma D Glu L Lys D Ala D Ala n ligase ADP forming . Other names in common use include Aslfm , UDP MurNAc pentapeptide D aspartate ligase , and D aspartic acid activating enzyme . References reflist 1 cite journal author Staudenbauer W, Strominger JL date 1972 title Activation of D aspartic acid for incorporation into peptidoglycan journal J. Biol. Chem. volume 247 pages 5095&ndash 102 pmid 4262567 issue 16 cite journal author Staudenbauer W, Willoughby E, Strominger JL date 1972 title Further studies of the D aspartic acid activating enzyme of Streptococcus faecalis and its attachment to the membrane journal J. Biol. Chem. volume ... title A diverse superfamily of enzymes with ATP dependent carboxylate amine thiol ligase activity ... Aslfm, the D aspartate ligase responsible for the addition of D aspartic acid onto the peptidoglycan ... 16510449 doi 10.1074 jbc.M600114200 issue 17 ligase stub Category EC 6.3.1 Category Enzymes of unknown ... more details
enzyme Name 6 carboxyhexanoate CoA ligase 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 CoA ligase 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 CoA ligase 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
enzyme Name asparagine tRNA ligase EC number 6.1.1.22 CAS number 37211 76 0 IUBMB EC number 6 1 1 22 GO code 0004816 image width caption In enzymology , an asparagine tRNA ligase EC number 6.1.1.22 is an enzyme that catalysis catalyzes the chemical reaction ATP L asparagine tRNAAsn math rightleftharpoons math AMP diphosphate L asparaginyl tRNAAsn The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L asparagine , and tRNA Asn , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L asparaginyl tRNA Asn . This enzyme belongs to the family of ligase s, to be specific those forming carbon oxygen bonds in aminoacyl tRNA and related compounds. The systematic name of this enzyme class is L asparagine tRNAAsn ligase AMP forming . Other names in common use include asparaginyl tRNA synthetase , asparaginyl transfer ribonucleate synthetase , asparaginyl transfer RNA synthetase , asparaginyl transfer ribonucleic acid synthetase , asparagyl transfer RNA synthetase , and asparagine translase . This enzyme participates in alanine and aspartate metabolism and aminoacyl trna biosynthesis . Structural studies As of late 2007, 3 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1X54 , PDB link 1X55 , and PDB link 1X56 . References reflist 1 cite journal author Davies MR, Marshall RD date 1972 title Partial purification of L asparaginyl tRNA synthetase from rabbit liver journal Biochem. Biophys. Res. Commun. volume 47 pages 1386&ndash 95 pmid 5040239 doi 10.1016 0006 291X 72 90226 4 issue 6 ligase stub Ligases Category EC 6.1.1 Category Enzymes of known structure ... more details
enzyme Name aspartate ammonia ligase EC number 6.3.1.1 CAS number 9023 69 2 IUBMB EC number 6 3 1 1 GO code 0004071 image width caption In enzymology , an aspartate ammonia ligase EC number 6.3.1.1 is an enzyme that catalysis catalyzes the chemical reaction ATP L aspartate NH sub 3 sub math rightleftharpoons math AMP diphosphate L asparagine The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L aspartate , and ammonia NH sub 3 sub , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L asparagine . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds as acid D ammonia or amine ligases amide synthases . The systematic name of this enzyme class is L aspartate ammonia ligase AMP forming . Other names in common use include asparagine synthetase , and L asparagine synthetase . This enzyme participates in 3 metabolism metabolic pathways alanine and aspartate metabolism , cyanoamino acid metabolism , and nitrogen metabolism . 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 11AS and PDB link 12AS . References reflist 1 cite journal author RAVEL JM, NORTON SJ, HUMPHREYS JS, SHIVE W date 1962 title Asparagine biosynthesis in Lactobacillus arabinosus and its control by asparagine through enzyme inhibition and repression journal J. Biol. Chem. volume 237 pages 2845&ndash 9 pmid 14490631 cite journal author Webster GC and Varner JE date 1955 title Aspartate metabolism and asparagine synthesis in plant systems journal J. Biol. Chem. volume 215 pages 91&ndash 99 pmid 14392145 ligase stub Category EC 6.3.1 Category Enzymes of known structure ... more details
enzyme Name aspartate tRNA Asn ligase EC number 6.1.1.23 CAS number 9027 32 1 IUBMB EC number 6 1 1 23 GO code 0050560 image width caption In enzymology , an aspartate tRNAAsn ligase EC number 6.1.1.23 is an enzyme that catalysis catalyzes the chemical reaction ATP L aspartate tRNAAsx math rightleftharpoons math AMP diphosphate aspartyl tRNAAsx The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L aspartate , and tRNAAsx , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and aspartyl tRNAAsx . This enzyme belongs to the family of ligase s, to be specific those forming carbon oxygen bonds in aminoacyl tRNA and related compounds. The systematic name of this enzyme class is L aspartate tRNAAsx ligase AMP forming . This enzyme is also called nondiscriminating aspartyl tRNA synthetase . This enzyme participates in alanine and aspartate metabolism . References reflist 1 cite journal author Ibba M, Soll D year 2000 title Aminoacyl tRNA synthesis journal Annu. Rev. Biochem. volume 69 pages 617&ndash 50 pmid 10966471 doi 10.1146 annurev.biochem.69.1.617 cite journal author Schmitt E, Moulinier L, Fujiwara S, Imanaka T, Thierry JC, Moras D year 1998 title Crystal structure of aspartyl tRNA synthetase from Pyrococcus kodakaraensis KOD archaeon specificity and catalytic mechanism of adenylate formation journal EMBO J. volume 17 pages 5227&ndash 37 pmid 9724658 doi 10.1093 emboj 17.17.5227 issue 17 pmc 1170850 cite journal author Becker HD, Kern D year 1998 title Thermus thermophilus a link in evolution of the tRNA dependent amino acid amidation pathways journal Proc. Natl. Acad. Sci. U. S. A. volume 95 pages 12832&ndash 7 pmid 9789000 doi 10.1073 pnas.95.22.12832 issue 22 pmc 23616 Ligases Category EC 6.1.1 Category Enzymes of unknown structure ligase stub ... more details
enzyme Name cysteine tRNA ligase EC number 6.1.1.16 CAS number 37318 56 2 IUBMB EC number 6 1 1 16 GO code 0004817 image width caption In enzymology , a cysteine tRNA ligase EC number 6.1.1.16 is an enzyme that catalysis catalyzes the chemical reaction ATP L cysteine tRNACys math rightleftharpoons math AMP diphosphate L cysteinyl tRNACys The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L cysteine , and tRNA Cys , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L cysteinyl tRNA Cys . This enzyme belongs to the family of ligase s, to be specific those forming carbon oxygen bonds in aminoacyl tRNA and related compounds. The systematic name of this enzyme class is L cysteine tRNACys ligase AMP forming . Other names in common use include cysteinyl tRNA synthetase , cysteinyl transferRNA synthetase , cysteinyl transfer ribonucleate synthetase , and cysteine translase . This enzyme participates in cysteine metabolism and aminoacyl trna biosynthesis . Structural studies As of late 2007, 3 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1LI5 , PDB link 1LI7 , and PDB link 1U0B . References reflist 1 cite journal author McCorquodale DJ year 1964 title The separation and partial purification of aminoacyl RNA synthetases from Escherichia coli journal Biochim. Biophys. Acta volume 91 pages 541&ndash 548 pmid 14262440 Ligases Category EC 6.1.1 Category Enzymes of known structure ligase stub ... more details
enzyme Name diphthine ammonia ligase EC number 6.3.2.22 CAS number 114514 33 9 IUBMB EC number 6 3 2 22 GO code 0017178 image width caption In enzymology , a diphthine ammonia ligase EC number 6.3.2.22 is an enzyme that catalysis catalyzes the chemical reaction ATP diphthine NH sub 3 sub math rightleftharpoons math ADP phosphate diphthamide The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , diphthine , and ammonia NH sub 3 sub , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and diphthamide . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds as acid D amino acid ligases peptide synthases . The systematic name of this enzyme class is diphthine ammonia ligase ADP forming . Other names in common use include diphthamide synthase , and diphthamide synthetase . References reflist 1 cite journal author Moehring JM, Moehring TJ date 1988 title The post translational trimethylation of diphthamide studied in vitro journal J. Biol. Chem. volume 263 pages 3840&ndash 4 pmid 3346227 issue 8 cite journal author Moehring TJ and Moehring JM date 1987 title Mutant cultured cells used to study the synthesis of diphthamide journal UCLA Symp. Mol. Cell. Biol. New Ser. volume 45 pages 53&ndash 63 ligase stub Category EC 6.3.2 Category Enzymes of unknown structure ... more details
enzyme Name glutamate ethylamine ligase EC number 6.3.1.6 CAS number 62213 31 4 IUBMB EC number 6 3 1 6 GO code 0047942 image width caption In enzymology , a glutamate ethylamine ligase EC number 6.3.1.6 is an enzyme that catalysis catalyzes the chemical reaction ATP L glutamate ethylamine math rightleftharpoons math ADP phosphate N sub 5 sub ethyl L glutamine The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L glutamate , and ethylamine , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and N5 ethyl L glutamine . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds as acid D ammonia or amine ligases amide synthases . The systematic name of this enzyme class is L glutamate ethylamine ligase ADP forming . Other names in common use include N5 ethyl L glutamine synthetase , theanine synthetase , and N5 ethylglutamine synthetase . References reflist 1 cite journal author Sasaoka K and Kito M date 1964 title Synthesis of theanine by tea seedling homogenate journal Agric. Biol. Chem. volume 28 pages 313&ndash 317 cite journal author Sasaoka K, Kito M and Inagaki H date 1963 title Studies on the biosynthesis of theanine in tea seedlings. Synthesis of theanine by the homogenate of tea seedlings journal Agric. Biol. Chem. volume 27 pages 467&ndash 468 cite journal author Sasaoka K, Kito M and Onishi Y date 1965 title Some properties of the theanine synthesizing enzyme in tea seedlings journal Agric. Biol. Chem. volume 29 pages 984&ndash 988 ligase stub Category EC 6.3.1 Category Enzymes of unknown structure ... more details
enzyme Name glutamate tRNA Gln ligase EC number 6.1.1.24 CAS number 9068 76 2 IUBMB EC number 6 1 1 24 GO code 0050561 image width caption In enzymology , a glutamate tRNAGln ligase EC number 6.1.1.24 is an enzyme that catalysis catalyzes the chemical reaction ATP L glutamate tRNAGlx math rightleftharpoons math AMP diphosphate glutamyl tRNAGlx The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L glutamate , and tRNAGlx , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and glutamyl tRNAGlx . This enzyme belongs to the family of ligase s, to be specific those forming carbon oxygen bonds in aminoacyl tRNA and related compounds. The systematic name of this enzyme class is L glutamate tRNAGlx ligase AMP forming . This enzyme is also called glutamyl tRNA synthetase . This enzyme participates in glutamate metabolism . References reflist 1 cite journal author Ibba M, Soll D year 2000 title Aminoacyl tRNA synthesis journal Annu. Rev. Biochem. volume 69 pages 617&ndash 50 pmid 10966471 doi 10.1146 annurev.biochem.69.1.617 cite journal author Schmitt E, Moulinier L, Fujiwara S, Imanaka T, Thierry JC, Moras D year 1998 title Crystal structure of aspartyl tRNA synthetase from Pyrococcus kodakaraensis KOD archaeon specificity and catalytic mechanism of adenylate formation journal EMBO J. volume 17 pages 5227&ndash 37 pmid 9724658 doi 10.1093 emboj 17.17.5227 issue 17 pmc 1170850 cite journal author Kim SI, Soll D year 1998 title Major identity element of glutamine tRNAs from Bacillus subtilis and Escherichia coli in the reaction with B. subtilis glutamyl tRNA synthetase journal Mol. Cells. volume 8 pages 459&ndash 65 pmid 9749534 issue 4 Ligases Category EC 6.1.1 Category Enzymes of unknown structure ligase stub ... more details
enzyme Name histidine tRNA ligase EC number 6.1.1.21 CAS number 9068 78 4 IUBMB EC number 6 1 1 21 GO code 0004821 image width caption In enzymology , a histidine tRNA ligase EC number 6.1.1.21 is an enzyme that catalysis catalyzes the chemical reaction ATP L histidine tRNAHis math rightleftharpoons math AMP diphosphate L histidyl tRNAHis The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L histidine , and tRNA His , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L histidyl tRNA His . This enzyme belongs to the family of ligase s, to be specific those forming carbon oxygen bonds in aminoacyl tRNA and related compounds. The systematic name of this enzyme class is L histidine tRNAHis ligase AMP forming . Other names in common use include histidyl tRNA synthetase , histidyl transfer ribonucleate synthetase , and histidine translase . This enzyme participates in histidine metabolism and aminoacyl trna biosynthesis . Structural studies As of late 2007, 9 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1ADJ , PDB link 1ADY , PDB link 1H4V , PDB link 1HTT , PDB link 1KMM , PDB link 1KMN , PDB link 1QE0 , PDB link 1WU7 , and PDB link 1X59 . See also Anti Jo1 References reflist 1 cite journal author von Tigerstrom M, Tener GM date 1967 title Histidyl transfer ribonucleic acid synthetase from bakers yeast journal Can. J. Biochem. volume 45 pages 1067&ndash 74 pmid 6035970 issue 7 ligase stub Ligases CO CS and CN Category EC 6.1.1 Category Enzymes of known structure ... more details
enzyme Name lysine tRNA Pyl ligase EC number 6.1.1.25 CAS number 782472 12 2 IUBMB EC number 6 1 1 25 GO code 0050562 image width caption In enzymology , a lysine tRNAPyl ligase EC number 6.1.1.25 is an enzyme that catalysis catalyzes the chemical reaction ATP L lysine tRNAPyl math rightleftharpoons math AMP diphosphate L lysyl tRNAPyl The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L lysine , and tRNA Pyl , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L lysyl tRNA Pyl . This enzyme belongs to the family of ligase s, to be specific those forming carbon oxygen bonds in aminoacyl tRNA and related compounds. The systematic name of this enzyme class is L lysine tRNAPyl ligase AMP forming . References reflist 1 cite journal author Srinivasan G, James CM, Krzycki JA date 2002 title Pyrrolysine encoded by UAG in Archaea charging of a UAG decoding specialized tRNA journal Science. volume 296 pages 1459&ndash 62 pmid 12029131 doi 10.1126 science.1069588 issue 5572 cite journal author Hao B, Gong W, Ferguson TK, James CM, Krzycki JA, Chan MK date 2002 title A new UAG encoded residue in the structure of a methanogen methyltransferase journal Science. volume 296 pages 1462&ndash 6 pmid 12029132 doi 10.1126 science.1069556 issue 5572 ligase stub Ligases Category EC 6.1.1 Category Enzymes of unknown structure ... more details
enzyme Name tyrosine arginine ligase EC number 6.3.2.24 CAS number 116036 78 3 IUBMB EC number 6 3 2 24 GO code 0050367 image width caption In enzymology , a tyrosine arginine ligase EC number 6.3.2.24 is an enzyme that catalysis catalyzes the chemical reaction ATP L tyrosine L arginine math rightleftharpoons math AMP diphosphate L tyrosyl L arginine The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L tyrosine , and L arginine , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L tyrosyl L arginine . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds as acid D amino acid ligases peptide synthases . The systematic name of this enzyme class is L tyrosine L arginine ligase AMP forming . Other names in common use include tyrosyl arginine synthase , kyotorphin synthase , kyotorphin synthesizing enzyme , and kyotorphin synthetase . References reflist 1 cite journal author Ueda H, Yoshihara Y, Fukushima N, Shiomi H, Nakamura A, Takagi H date 1987 title Kyotorphin tyrosine arginine synthetase in rat brain synaptosomes journal J. Biol. Chem. volume 262 pages 8165&ndash 73 pmid 3597366 month Jun first1 H first2 Y first3 N first4 H first5 A first6 H issue 17 issn 0021 9258 url http www.jbc.org cgi pmidlookup?view long&pmid 3597366 format Free full text ligase stub Category EC 6.3.2 Category Enzymes of unknown structure ... more details
Orphan date November 2010 enzyme Name ubiquitin calmodulin ligase EC number 6.3.2.21 CAS number 119632 60 9 IUBMB EC number 6 3 2 21 GO code 0050372 image width caption In enzymology , an ubiquitin calmodulin ligase EC number 6.3.2.21 is an enzyme that catalysis catalyzes the chemical reaction n ATP calmodulin n ubiquitin math rightleftharpoons math n AMP n diphosphate ubiquitin n calmodulin The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , calmodulin , and ubiquitin , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and ubiquitin n calmodulin . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds as acid D amino acid ligases peptide synthases . The systematic name of this enzyme class is calmodulin ubiquitin ligase AMP forming . Other names in common use include ubiquityl calmodulin synthase , ubiquitin calmodulin synthetase , ubiquityl calmodulin synthetase , and uCaM synthetase . References reflist 1 cite journal doi 10.1515 bchm3.1988.369.2.1325 author Jennissen HP, Laub M year 1988 title Ubiquitin calmodulin conjugating activity from cardiac muscle journal Biol. Chem. Hoppe Seyler volume 369 pages 1325&ndash 30 pmid 2853950 issue 12 cite journal doi 10.1515 bchm3.1988.369.2.1317 author Ziegenhagen R, Jennissen HP year 1988 title Multiple ubiquitination of vertebrate calmodulin by reticulocyte lysate and inhibition of calmodulin conjugation by phosphorylase kinase journal Biol. Chem. Hoppe Seyler volume 369 pages 1317&ndash 24 pmid 2853949 issue 12 Category EC 6.3.2 Category Enzymes of unknown structure ligase stub ... more details
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