Correct title Glutamateammonialigaseadenylyltransferase reason bracket enzyme Name glutamateammonialigaseadenylyltransferase EC number 2.7.7.42 CAS number 9077 66 1 IUBMB EC number 2 7 7 42 GO code 0008882 image width caption In enzymology , a glutamateammonialigaseadenylyltransferase EC number 2.7.7.42 is an enzyme that catalysis catalyzes the chemical reaction ATP L glutamateammonialigase ADP forming math rightleftharpoons math diphosphate adenylyl L glutamateammonialigase ADP forming Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and L glutamateammonialigase ADP forming , whereas its two product chemistry products are diphosphate and adenylyl L glutamateammonialigase ADP forming . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ATP L glutamateammonialigase ADP forming adenylyltransferase . Other names in common use include glutamine synthetase adenylyltransferase , ATP glutamine synthetase adenylyltransferase , and adenosine triphosphate glutamine synthetase adenylyltransferase . 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 1V4A . References reflist 1 cite journal author Ebner E, Wolf D, Gancedo C, Elsasser S, Holzer H date 1970 title ATP glutamine synthetase adenylyltransferase from Escherichia coli B. Purification and properties journal Eur. J. Biochem. volume 14 pages 535&ndash 44 pmid 4920894 doi 10.1111 j.1432 1033.1970.tb00320.x issue ... j.1432 1033.1972.tb01689.x issue 2 Category EC 2.7.7 Glutamateammonialigase Category Enzymes of known ... synthetase. 8. ATP glutamine synthetase adenylyltransferase, an enzyme that catalyzes alterations ... Inactivation, stabilization and some properties of ATP glutamine synthetase adenylyltransferase from ... more details
enzyme Name adenylylsulfate ammoniaadenylyltransferase EC number 2.7.7.51 CAS number 79121 94 1 IUBMB EC number 2 7 7 51 GO code 0047352 image width caption In enzymology , an adenylylsulfate ammoniaadenylyltransferase EC number 2.7.7.51 is an enzyme that catalysis catalyzes the chemical reaction adenylyl sulfate NH sub 3 sub math rightleftharpoons math adenosine 5 phosphoramidate sulfate. Thus, the two substrate biochemistry substrates of this enzyme are adenylyl sulfate and ammonia NH sub 3 sub , whereas its two product chemistry products are adenosine 5 phosphoramidate and sulfate . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is adenylyl sulfate ammoniaadenylyltransferase . Other names in common use include APSAT , and adenylylsulfate ammoniaadenylyltransferase . References reflist 1 cite journal author Fankhauser H, Garber L and Schiff JA date 1979 title Adenylyl sulfate APS ammonia adenylyl transferase APSAT forming adenosine 5 phosphoramidate APA from APS and ammonia journal Plant Physiol. volume 63S pages 162 cite journal author Fankhauser H and Schiff JA date 1980 title Further purification and properties of adenylyl sulfate APS ammonia adenylyl transferase APSAT from Chlorella journal Plant Physiol. volume 65S pages 17 enzyme stub Category EC 2.7.7 Category Enzymes of unknown structure ... more details
enzyme Name adenylyl glutamateammonialigase hydrolase EC number 3.1.4.15 CAS number 37288 22 5 IUBMB EC number 3 1 4 15 GO code 0047388 image width caption In enzymology , an adenylyl glutamateammonialigase hydrolase EC number 3.1.4.15 is an enzyme that catalysis catalyzes the chemical reaction adenylyl L glutamateammonialigase ADP forming H sub 2 sub O math rightleftharpoons math adenylate L glutamateammonialigase ADP forming Thus, the two substrate biochemistry substrates of this enzyme are adenylyl L glutamateammonialigase ADP forming and water H sub 2 sub O , whereas its two product chemistry products are adenylate and L glutamateammonialigase ADP forming . This enzyme belongs to the family of hydrolase s, specifically those acting on phosphoric ester diester bonds. The systematic name of this enzyme class is adenylyl L glutamateammonialigase ADP forming adenylylhydrolase . Other names in common use include adenylyl glutamine synthetase hydrolase , and adenylyl glutamine synthetase hydrolase . References reflist 1 cite journal author Heilmeyer L, Battig F and Holzer H date 1968 title Characterization of a glutamine synthetase b activating deadenylylating enzyme system in Escherichia coli journal Eur. J. Biochem. volume 9 pages 259&ndash 262 doi 10.1111 j.1432 1033.1969.tb00603.x pmid 4897098 cite journal author Shapiro BM date 1969 title The glutamine synthetase deadenylylating enzyme system from Escherichia coli. Resolution into two components, specific nucleotide stimulation, and cofactor requirements journal Biochemistry. volume 8 pages 659&ndash 70 pmid 4893578 doi 10.1021 bi00830a030 issue 2 cite journal author Shapiro BM, Stadtman ER date 1968 title 5 adenylyl O tyrosine. The novel phosphodiester residue of adenylylated glutamine synthetase from Escherichia coli journal J. Biol. Chem. volume 243 pages 3769&ndash 71 pmid 4298074 issue 13 hydrolase stub Category EC 3.1.4 Category Enzymes of unknown structure ... more details
enzyme Name anthranilate adenylyltransferase EC number 2.7.7.55 CAS number 70248 64 5 IUBMB EC number 2 7 7 55 GO code 0047671 image width caption In enzymology , an anthranilate adenylyltransferase EC number 2.7.7.55 is an enzyme that catalysis catalyzes the chemical reaction ATP anthranilate math rightleftharpoons math diphosphate N adenylylanthranilate Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and anthranilate , whereas its two product chemistry products are diphosphate and N adenylylanthranilate . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ATP anthranilate N adenylyltransferase . This enzyme is also called anthranilic acid adenylyltransferase . References reflist 1 cite journal author Lerbs W, Luckner M date 1985 title Cyclopeptine synthetase activity in surface cultures of Penicillium cyclopium journal J. Basic. Microbiol. volume 25 pages 387&ndash 91 pmid 2995633 doi 10.1002 jobm.3620250611 issue 6 enzyme stub Category EC 2.7.7 Category Enzymes of unknown structure ... more details
enzyme Name aldose 1 phosphate adenylyltransferase EC number 2.7.7.36 CAS number 37278 27 6 IUBMB EC number 2 7 7 36 GO code 0047346 image width caption In enzymology , an aldose 1 phosphate adenylyltransferase EC number 2.7.7.36 is an enzyme that catalysis catalyzes the chemical reaction ADP alpha D aldose 1 phosphate math rightleftharpoons math phosphate ADP aldose Thus, the two substrate biochemistry substrates of this enzyme are adenosine diphosphate ADP and alpha D aldose 1 phosphate , whereas its two product chemistry products are phosphate and ADP aldose . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ADP alpha D aldose 1 phosphate adenylyltransferase . Other names in common use include sugar 1 phosphate adenylyltransferase , ADPaldose phosphorylase , adenosine diphosphosugar phosphorylase , ADP sugar phosphorylase , adenosine diphosphate glucose orthophosphate adenylyltransferase , and ADP aldose 1 phosphate adenylyltransferase . References reflist 1 cite journal author Dankert M, Goncalves IRJ and Recondo E date 1964 title Adenosine diphosphate glucose orthophosphate adenylyltransferase in wheat germ journal Biochim. Biophys. Acta volume 81 issue 1 pages 78&ndash 85 doi 10.1016 0926 6569 64 90337 2 cite journal author Passeron S, Recondo E and Dankert M date 1964 title Biosynthesis of adenosine diphosphate D hexoses journal Biochim. Biophys. Acta volume 89 pages 372&ndash 374 pmid 14205499 enzyme stub Category EC 2.7.7 Category Enzymes of unknown structure ... more details
enzyme Name ATP adenylyltransferase EC number 2.7.7.53 CAS number 96697 71 1 IUBMB EC number 2 7 7 53 GO code 0003877 image width caption In enzymology , an ATP adenylyltransferase EC number 2.7.7.53 is an enzyme that catalysis catalyzes the chemical reaction ADP ATP math rightleftharpoons math phosphate P sub 1 sub ,P sub 4 sub bis 5 adenosyl tetraphosphate Thus, the two substrate biochemistry substrates of this enzyme are adenosine diphosphate ADP and adenosine triphosphate ATP , whereas its two product chemistry products are phosphate and P1,P4 bis 5 adenosyl tetraphosphate . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ADP ATP adenylyltransferase . Other names in common use include bis 5 nucleosyl tetraphosphate phosphorylase NDP forming , diadenosinetetraphosphate alphabeta phosphorylase , adenine triphosphate adenylyltransferase , diadenosine 5 ,5 P1,P4 tetraphosphate alphabeta phosphorylase , ADP forming , and dinucleoside oligophosphate alphabeta phosphorylase . This enzyme participates in purine metabolism . References reflist 1 cite journal author Guranowski A, Blanquet S date 1985 title Phosphorolytic cleavage of diadenosine 5 ,5 P1,P4 tetraphosphate Properties of homogeneous diadenosine 5 ,5 P1,P4 tetraphosphate alpha, beta phosphorylase from Saccharomyces cerevisiae journal J. Biol. Chem. volume 260 pages 3542&ndash 7 pmid 2982863 issue 6 enzyme stub Category EC 2.7.7 Category Enzymes of unknown structure ... more details
enzyme Name phenylalanine adenylyltransferase EC number 2.7.7.54 CAS number 98285 55 3 IUBMB EC number 2 7 7 54 GO code 0050173 image width caption In enzymology , a phenylalanine adenylyltransferase EC number 2.7.7.54 is an enzyme that catalysis catalyzes the chemical reaction ATP L phenylalanine math rightleftharpoons math diphosphate N adenylyl L phenylalanine Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and L phenylalanine , whereas its two product chemistry products are diphosphate and N adenylyl L phenylalanine . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ATP L phenylalanine adenylyltransferase . This enzyme is also called L phenylalanine adenylyltransferase . References reflist 1 cite journal author Lerbs W, Luckner M date 1985 title Cyclopeptine synthetase activity in surface cultures of Penicillium cyclopium journal J. Basic. Microbiol. volume 25 pages 387&ndash 91 pmid 2995633 doi 10.1002 jobm.3620250611 issue 6 enzyme stub Category EC 2.7.7 Category Enzymes of unknown structure ... more details
enzyme Name ribose 5 phosphate adenylyltransferase EC number 2.7.7.35 CAS number 9054 55 1 IUBMB EC number 2 7 7 35 GO code 0047345 image width caption In enzymology , a ribose 5 phosphate adenylyltransferase EC number 2.7.7.35 is an enzyme that catalysis catalyzes the chemical reaction ADP D ribose 5 phosphate math rightleftharpoons math phosphate ADP ribose Thus, the two substrate biochemistry substrates of this enzyme are adenosine diphosphate ADP and D ribose 5 phosphate , whereas its two product chemistry products are phosphate and ADP ribose . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ADP D ribose 5 phosphate adenylyltransferase . Other names in common use include ADP ribose phosphorylase , and adenosine diphosphoribose phosphorylase . References reflist 1 cite journal author Evans WR, San Pietro A date 1966 title Phosphorolysis of adenosine diphosphoribose journal Arch. Biochem. Biophys. volume 113 pages 236&ndash 44 pmid 4287446 doi 10.1016 0003 9861 66 90178 0 issue 1 cite journal author Stern AI, Avron M date 1966 title An adenosine 5 diphosphate ribose orthophosphate adenylyltransferase from Euglena gracilis journal Biochim. Biophys. Acta. volume 118 pages 577&ndash 91 pmid 5970863 issue 3 enzyme stub Category EC 2.7.7 Category Enzymes of unknown structure ... more details
enzyme Name glucose 1 phosphate adenylyltransferase EC number 2.7.7.27 CAS number 9027 71 8 IUBMB EC number 2 7 7 27 GO code 0008878 image width caption In enzymology , a glucose 1 phosphate adenylyltransferase EC number 2.7.7.27 is an enzyme that catalysis catalyzes the chemical reaction ATP alpha D glucose 1 phosphate math rightleftharpoons math diphosphate ADP glucose Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and alpha D glucose 1 phosphate , whereas its two product chemistry products are diphosphate and ADP glucose . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ATP alpha D glucose 1 phosphate adenylyltransferase . Other names in common use include ADP glucose pyrophosphorylase , glucose 1 phosphate adenylyltransferase , adenosine diphosphate glucose pyrophosphorylase , adenosine diphosphoglucose pyrophosphorylase , ADP glucose pyrophosphorylase , ADP glucose synthase , ADP glucose synthetase , ADPG pyrophosphorylase , ADP alpha D glucose 1 phosphate adenylyltransferase and AGPase . This enzyme participates in starch and sucrose metabolism . 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 1YP2 , PDB link 1YP3 , and PDB link 1YP4 . References reflist 1 cite journal author Ghosh HP, Preiss J date 1966 title Adenosine diphosphate glucose pyrophosphorylase. A regulatory enzyme in the biosynthesis of starch in spinach leaf chloroplasts journal J. Biol. Chem. volume 241 pages 4491&ndash 504 pmid 5922972 issue 19 cite journal author Shen L and Preiss J date 1965 title Biosynthesis of bacterial glycogen. I. Purification and properties of the adenosine diphosphoglucose pyrophosphorylase of Arthrobacter species NRRL B1973 journal J. Biol. Chem. volume 240 pages ... more details
enzyme Name FMN adenylyltransferase EC number 2.7.7.2 CAS number 9026 37 3 IUBMB EC number 2 7 7 2 GO code 0003919 image width caption In enzymology , a FMN adenylyltransferase EC number 2.7.7.2 is an enzyme that catalysis catalyzes the chemical reaction ATP FMN math rightleftharpoons math diphosphate FAD Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and flavin mononucleotide FMN , whereas its two product chemistry products are diphosphate and FAD . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ATP FMN adenylyltransferase . This enzyme participates in riboflavin metabolism . Other names Other names in common use include FAD pyrophosphorylase riboflavin mononucleotide adenylyltransferase adenosine triphosphate riboflavin mononucleotide transadenylase adenosine triphosphate riboflavine mononucleotide transadenylase FAD synthetase riboflavin adenine dinucleotide pyrophosphorylase riboflavine References reflist 1 cite journal author GIRI KV, RAO NA, CAMA HR, KUMAR SA year 1960 title Studies on flavinadenine dinucleotide synthesizing enzyme in plants journal Biochem. J. volume 75 pages 381&ndash 6 pmid 13828163 pmc 1204435 cite journal author Schrecker AW and Kornberg A year 1950 title Reversible enzymatic synthesis of flavin adenine dinucleotide journal J. Biol. Chem. volume 182 pages 795&ndash 803 pmid 19994476 issue 2 Category EC 2.7.7 Category Enzymes of unknown structure enzyme stub de FAD Synthetase ... more details
enzyme Name polynucleotide adenylyltransferase EC number 2.7.7.19 CAS number 9026 30 6 IUBMB EC number 2 7 7 19 GO code 0004652 image width caption In enzymology , a polynucleotide adenylyltransferase EC number 2.7.7.19 is an enzyme that catalysis catalyzes the chemical reaction ATP RNAn math rightleftharpoons math diphosphate RNAn sup sup 1 Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and RNA , whereas its two product chemistry products are diphosphate and RNA with an extra adenosine nucleotide at its 3 end. Naming This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ATP polynucleotide adenylyltransferase . Other names in common use include NTP polymerase RNA adenylating enzyme AMP polynucleotidylexotransferase ATP polynucleotide adenylyltransferase ATP polynucleotidylexotransferase Poly A polymerase Poly A synthetase Polyadenylate nucleotidyltransferase Polyadenylate polymerase Polyadenylate synthetase Polyadenylic acid polymerase Polyadenylic polymerase Terminal riboadenylate transferase Poly A hydrolase RNA formation factors PF1 Adenosine triphosphate ribonucleic acid adenylyltransferase Function This enzyme is responsible for the addition of the 3 polyadenylation polyadenine tail to a newly synthesized pre messenger RNA pre mRNA molecule during the process of transcription genetics gene transcription . The protein is the final addition to a large protein complex that also contains smaller assemblies known as the cleavage and polyadenylation specificity factor CPSF and cleavage stimulatory factor CtSF and its binding is a necessary prerequisite to the cleavage of the 3 end of the pre mRNA. After cleavage of the 3 signaling region that directs the assembly of the complex, PAP adds the polyadenine tail to the new 3 end. The rate at which PAP adds adenine nucleotide s is dependent ... more details
enzyme Name sulfate adenylyltransferase ATP EC number 2.7.7.4 CAS number 9012 39 9 IUBMB EC number 2 7 7 4 GO code 0004781 image width caption Infobox protein family Symbol ATP sulfurylase Name ATP sulfurylase image PDB 1v47 EBI.jpg width caption crystal structure of atp sulfurylase from thermus thermophillus hb8 in complex with aps Pfam PF01747 Pfam clan InterPro IPR002650 SMART PROSITE MEROPS SCOP 1i2d TCDB OPM family OPM protein CAZy CDD In enzymology , a sulfate adenylyltransferase EC number 2.7.7.4 is an enzyme that catalysis catalyzes the chemical reaction ATP sulfate math rightleftharpoons math diphosphate adenylyl sulfate Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and sulfate , whereas its two product chemistry products are diphosphate and adenylyl sulfate . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ATP sulfate adenylyltransferase . Other names in common use include ATP sulfurylase , adenosine 5 triphosphate sulfurylase , adenosinetriphosphate sulfurylase , adenylylsulfate pyrophosphorylase , ATP sulfurylase , ATP sulfurylase , and sulfurylase . This enzyme participates in 3 metabolism metabolic pathways purine metabolism , selenoamino acid metabolism , and sulfur metabolism . Some sulphate adenylyltransferases are part of a bifunctional polypeptide polymer chain associated with adenosyl phosphosulphate kinase adenosyl phosphosulphate APS kinase . Both enzyme s are required for PAPS phosphoadenosine phosphosulphate synthesis from inorganic sulphate. ref name pmid8522184 cite journal author Rosenthal E, Leustek T title A multifunctional Urechis caupo protein, PAPS synthetase, has both ATP sulfurylase and APS kinase activities journal Gene volume 165 issue 2 pages 243 8 year 1995 month November pmid 8522184 doi 10.1016 0378 1119 95 00450 K url ref ref name pmid9671738 ... more details
enzyme Name 4 methyleneglutamate ammonialigase EC number 6.3.1.7 CAS number 85537 85 5 IUBMB EC number 6 3 1 7 GO code 0047581 image width caption In enzymology , a 4 methyleneglutamate ammonialigase EC number 6.3.1.7 is an enzyme that catalysis catalyzes the chemical reaction ATP 4 methylene L glutamate NH sub 3 sub math rightleftharpoons math AMP diphosphate 4 methylene L glutamine The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , 4 methylene L glutamate , and ammonia NH sub 3 sub , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and 4 methylene 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 4 methylene L glutamateammonialigase AMP forming . This enzyme is also called 4 methyleneglutamine synthetase . This enzyme participates in c5 branched dibasic acid metabolism . References reflist 1 cite journal author Winter HC, Su TZ, Dekker EE date 1983 title 4 methyleneglutamine synthetase a new amide synthetase present in germinating peanuts journal Biochem. Biophys. Res. Commun. volume 111 pages 484&ndash 9 pmid 6838571 doi 10.1016 0006 291X 83 90332 7 issue 2 ligase stub Category EC 6.3.1 Category Enzymes of unknown structure ... more details
enzyme Name Glutamate putrescine ligase EC number 6.3.1.11 CAS number 914090 78 1 IUBMB EC number 6 3 1 11 GO code image width caption In enzymology , a glutamate putrescine ligase EC number 6.3.1.11 is an enzyme that catalysis catalyzes the chemical reaction ATP L glutamate putrescine math rightleftharpoons math ADP phosphate gamma L glutamylputrescine The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L glutamate , and putrescine , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and gamma L glutamylputrescine . 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 putrescine ligase ADP forming . Other names in common use include gamma glutamylputrescine synthetase , and YcjK . This enzyme participates in urea cycle and metabolism of amino groups . References reflist 1 cite journal author Kurihara S, Oda S, Kato K, Kim HG, Koyanagi T, Kumagai H, Suzuki H date 2005 title A novel putrescine utilization pathway involves gamma glutamylated intermediates of Escherichia coli K 12 journal J. Biol. Chem. volume 280 pages 4602&ndash 8 pmid 15590624 doi 10.1074 jbc.M411114200 issue 6 ligase stub Category EC 6.3.1 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 ribose 5 phosphate ammonialigase 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 ammonialigase 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 ammonialigase 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 glutamate methylamine ligase EC number 6.3.4.12 CAS number 37318 69 7 IUBMB EC number 6 3 4 12 GO code 0047943 image width caption In enzymology , a glutamate methylamine ligase EC number 6.3.4.12 is an enzyme that catalysis catalyzes the chemical reaction ATP L glutamate methylamine math rightleftharpoons math ADP phosphate N sub 5 sub methyl L glutamine The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L glutamate , and methylamine , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and N5 methyl L glutamine . This enzyme belongs to the family of ligase s, specifically those forming generic carbon nitrogen bonds. The systematic name of this enzyme class is L glutamate methylamine ligase ADP forming . This enzyme is also called gamma glutamylmethylamide synthetase . References reflist 1 cite journal author Kung HF, Wagner C date 1969 title Gamma glutamylmethylamide. A new intermediate in the metabolism of methylamine journal J. Biol. Chem. volume 244 pages 4136&ndash 40 pmid 5800436 issue 15 ligase stub Category EC 6.3.4 Category Enzymes of unknown structure ... more details
enzyme Name aspartate ammonialigase 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 ammonialigase 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 ammonialigase 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 diphthine ammonialigase 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 ammonialigase 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 ammonialigase 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 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 streptomycin 3 adenylyltransferase EC number 2.7.7.47 CAS number 52660 23 8 IUBMB EC number 2 7 7 47 GO code 0009012 image width caption In enzymology , a streptomycin 3 adenylyltransferase EC number 2.7.7.47 is an enzyme that catalysis catalyzes the chemical reaction ATP streptomycin math rightleftharpoons math diphosphate 3 adenylylstreptomycin Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and streptomycin , whereas its two product chemistry products are diphosphate and 3 adenylylstreptomycin . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ATP streptomycin 3 adenylyltransferase . Other names in common use include streptomycin adenylate synthetase , streptomycin adenyltransferase , streptomycin adenylylase , streptomycin adenylyltransferase , streptomycin spectinomycin adenylyltransferase , AAD 3 , and aminoglycoside 3 adenylyltransferase . References reflist 1 cite journal author Harwood JH, Smith DH date 1969 title Resistance factor mediated streptomycin resistance journal J. Bacteriol. volume 97 pages 1262&ndash 71 pmid 4887506 issue 3 pmc 249843 enzyme stub Category EC 2.7.7 Category Enzymes of unknown structure ... more details
enzyme Name glutamate tRNA ligase EC number 6.1.1.17 CAS number 9068 76 2 IUBMB EC number 6 1 1 17 GO code 0004818 image width caption In enzymology , a glutamate tRNA ligase EC number 6.1.1.17 is an enzyme that catalysis catalyzes the chemical reaction ATP L glutamate tRNAGlu math rightleftharpoons math AMP diphosphate L glutamyl tRNAGlu The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L glutamate , and tRNA Glu , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L glutamyl tRNA Glu . 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 tRNAGlu ligase AMP forming . Other names in common use include glutamyl tRNA synthetase , glutamyl transfer ribonucleate synthetase , glutamyl transfer RNA synthetase , glutamyl transfer ribonucleic acid synthetase , glutamate tRNA synthetase , and glutamic acid translase . This enzyme participates in 3 metabolism metabolic pathways glutamate metabolism , porphyrin and chlorophyll metabolism , and aminoacyl trna biosynthesis . Structural studies As of late 2007, 16 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1FYJ , PDB link 1G59 , PDB link 1J09 , PDB link 1N75 , PDB link 1N77 , PDB link 1N78 , PDB link 2CFO , PDB link 2CUZ , PDB link 2CV0 , PDB link 2CV1 , PDB link 2CV2 , PDB link 2DXI , PDB link 2HRA , PDB link 2HRK , PDB link 2HSM , and PDB link 2O5R . 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 ... Category Enzymes of known structure ligase stub ... more details
enzyme Name glutamate cysteine ligase EC number 6.3.2.2 CAS number 9023 64 7 IUBMB EC number 6 3 2 2 GO code 0004357 image width caption In enzymology , a glutamate cysteine ligase EC number 6.3.2.2 is an enzyme that catalysis catalyzes the chemical reaction ATP L glutamate L cysteine math rightleftharpoons math ADP phosphate gamma L glutamyl L cysteine The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L glutamate , and L cysteine , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and gamma L glutamyl L cysteine . 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 glutamate L cysteine gamma ligase ADP forming . Other names in common use include gamma glutamylcysteine synthetase , gamma glutamyl L cysteine synthetase , and gamma glutamylcysteinyl synthetase . This enzyme participates in glutamate metabolism and glutathione metabolism . At least one compound, S Butyl DL homocysteine S,R sulfoximine is known to enzyme inhibitor inhibit this enzyme . 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 1V4G , PDB link 1VA6 , PDB link 2D32 , PDB link 2D33 , PDB link 2GWC , and PDB link 2GWD . References reflist 1 cite journal author Mackinnon CM, Carter PE, Smyth SJ, Dunbar B, Fothergill JE date 1987 title Molecular cloning of cDNA for human complement component C1s. The complete amino acid sequence journal Eur. J. Biochem. volume 169 pages 547&ndash 53 pmid 3500856 doi 10.1111 j.1432 1033.1987.tb13644.x issue 3 cite journal author SNOKE JE, YANARI S, BLOCH K date 1953 title Synthesis of glutathione from gamma glutamylcysteine journal J. Biol. Chem. volume ... pmid 14381401 issue 2 ligase stub Category EC 6.3.2 Category Enzymes of known structure ... more details
enzyme Name nicotinamide nucleotide adenylyltransferase EC number 2.7.7.1 CAS number 9032 70 6 IUBMB EC number 2 7 7 1 GO code 0000309 image width caption In enzymology , a nicotinamide nucleotide adenylyltransferase EC number 2.7.7.1 is an enzyme that catalysis catalyzes the chemical reaction ATP nicotinamide ribonucleotide math rightleftharpoons math diphosphate NAD sup sup Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and nicotinamide ribonucleotide , whereas its two product chemistry products are diphosphate and nicotinamide adenine dinucleotide NAD sup sup . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ATP nicotinamide nucleotide adenylyltransferase . Other names in common use include NAD pyrophosphorylase , adenosine triphosphate nicotinamide mononucleotide transadenylase , ATP NMN adenylyltransferase , diphosphopyridine nucleotide pyrophosphorylase , nicotinamide adenine dinucleotide pyrophosphorylase , nicotinamide mononucleotide adenylyltransferase , and NMN adenylyltransferase . This enzyme participates in nicotinate and nicotinamide metabolism . The human version of this protein is NMNAT1 . Structural studies As of late 2007, 11 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1EJ2 , PDB link 1GZU , PDB link 1HYB , PDB link 1KKU , PDB link 1KQN , PDB link 1KQO , PDB link 1KR2 , PDB link 1M8F , PDB link 1M8G , PDB link 1M8J , and PDB link 1M8K . References reflist 1 cite journal author ATKINSON MR, JACKSON JF, MORTON RK date 1961 title Nicotinamide mononucleotide adenylyltransferase of pig liver nuclei. The effects of nicotinamide mononucleotide concentration and pH on dinucleotide synthesis ... de Nicotinamidnukleotid Adenylyltransferase ... more details
enzyme Name pantetheine phosphate adenylyltransferase EC number 2.7.7.3 CAS number 9026 99 7 IUBMB EC number 2 7 7 3 GO code 0004595 image 1vlh.png width caption Phosphopantetheine adenylyltransferase from Thermotoga maritima . 4 Phosphopantetheine shown as spheres. Protein Data Bank PDB PDBe 1vlh In enzymology , a pantetheine phosphate adenylyltransferase EC number 2.7.7.3 is an enzyme that catalysis catalyzes the chemical reaction ATP 4 Phosphopantetheine math rightleftharpoons math diphosphate 3 dephospho CoA Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and Phosphopantetheine 4 Phosphopantetheine , whereas its two product chemistry products are diphosphate and 3 dephospho CoA . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ATP pantetheine 4 phosphate adenylyltransferase . Other names in common use include dephospho CoA pyrophosphorylase , pantetheine phosphate adenylyltransferase , dephospho coenzyme A pyrophosphorylase , and 3 dephospho CoA pyrophosphorylase . This enzyme participates in pantothenate and coa biosynthesis . Structural studies As of late 2007, 8 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1B6T , PDB link 1GN8 , PDB link 1H1T , PDB link 1O6B , PDB link 1OD6 , PDB link 1QJC , PDB link 1TFU , and PDB link 1VLH . References reflist 1 cite journal author HOAGLAND MB, NOVELLI GD date 1954 title Biosynthesis of coenzyme A from phospho pantetheine and of pantetheine from pantothenate journal ... of pantetheine phosphate adenylyltransferase journal Biochem. Biophys. Res. Commun. volume ... A, Lewendon A, Shaw WV date 1999 title Purification and characterization of phosphopantetheine adenylyltransferase ... JJ date Pt 6 title Cubic crystals of phosphopantetheine adenylyltransferase from Escherichia coli ... more details
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