enzyme Name 2,5 diaminovalerate transaminase EC number 2.6.1.8 CAS number 9030 39 1 IUBMB EC number 2 6 1 8 GO code 0047531 image width caption In enzymology , a 2,5 diaminovalerate transaminase EC number 2.6.1.8 is an enzyme that catalysis catalyzes the chemical reaction 2,5 diaminopentanoate 2 oxoglutarate math rightleftharpoons math 5 amino 2 oxopentanoate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are 2,5 diaminopentanoate and 2 oxoglutarate , whereas its two product chemistry products are 5 amino 2 oxopentanoate and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is 2,5 diaminopentanoate 2 oxoglutarate aminotransferase . Other names in common use include diamino acid transaminase , and diamino acid aminotransferase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author ROBERTS E date 1954 title Studies of transamination journal Arch. Biochem. Biophys. volume 48 pages 395&ndash 401 pmid 13125615 doi 10.1016 0003 9861 54 90355 0 issue 2 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name 2 aminohexanoate transaminase EC number 2.6.1.67 CAS number 111310 35 1 IUBMB EC number 2 6 1 67 GO code 0047537 image width caption In enzymology , a 2 aminohexanoate transaminase EC number 2.6.1.67 is an enzyme that catalysis catalyzes the chemical reaction L 2 aminohexanoate 2 oxoglutarate math rightleftharpoons math 2 oxohexanoate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are L 2 aminohexanoate and 2 oxoglutarate , whereas its two product chemistry products are 2 oxohexanoate and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L 2 aminohexanoate 2 oxoglutarate aminotransferase . Other names in common use include norleucine transaminase , norleucine leucine aminotransferase , and leucine L norleucine 2 oxoglutarate aminotransferase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Der Garabedian PA, Vermeersch JJ date 1987 title Candida L norleucine,leucine 2 oxoglutarate aminotransferase Purification and properties journal Eur. J. Biochem. volume 167 pages 141&ndash 7 pmid 3622507 doi 10.1111 j.1432 1033.1987.tb13315.x issue 1 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name 4 hydroxyglutamate transaminase EC number 2.6.1.23 CAS number 37277 86 4 IUBMB EC number 2 6 1 23 GO code 0047578 image width caption In enzymology , a 4 hydroxyglutamate transaminase EC number 2.6.1.23 is an enzyme that catalysis catalyzes the chemical reaction 4 hydroxy L glutamate 2 oxoglutarate math rightleftharpoons math 4 hydroxy 2 oxoglutarate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are 4 hydroxy L glutamate and 2 oxoglutarate , whereas its two product chemistry products are 4 hydroxy 2 oxoglutarate and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is 4 hydroxy L glutamate 2 oxoglutarate aminotransferase . This enzyme is also called 4 hydroxyglutamate aminotransferase . This enzyme participates in arginine and proline metabolism . References reflist 1 cite journal author GOLDSTONE A, ADAMS E date 1962 title Metabolism of gamma hydroxyglutamic acid. I. Conversion to alpha hydroxy gamma ketoglutarate by purified glutamic aspartic transaminase to rat liver journal J. Biol. Chem. volume 237 pages 3476&ndash 85 pmid 13948827 cite journal author KURATOMI K, FUKUNAGA K, KOBAYASHI Y date 1963 title THE METABOLISM OF GAMMA HYDROXYGLUTAMATE IN RAT LIVER. II. A TRANSAMINASE CONCERNED IN GAMMA HYDROXYGLUTAMATE METABOLISM journal Biochim. Biophys. Acta. volume 78 pages 629&ndash 36 pmid 14089443 doi 10.1016 0006 3002 63 91028 X issue 4 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
enzyme Name acetylornithine transaminase EC number 2.6.1.11 CAS number 9030 40 4 IUBMB EC number 2 6 1 11 GO code 0003992 image width caption In enzymology , an acetylornithine transaminase EC number 2.6.1.11 is an enzyme that catalysis catalyzes the chemical reaction N sub 2 sub acetyl L ornithine 2 oxoglutarate math rightleftharpoons math N acetyl L glutamate 5 semialdehyde L glutamate Thus, the two substrate biochemistry substrates of this enzyme are N2 acetyl L ornithine and 2 oxoglutarate , whereas its two product chemistry products are N acetyl L glutamate 5 semialdehyde and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is N2 acetyl L ornithine 2 oxoglutarate 5 aminotransferase . Other names in common use include acetylornithine delta transaminase , ACOAT , acetylornithine 5 aminotransferase , acetylornithine aminotransferase , N acetylornithine aminotransferase , N acetylornithine delta transaminase , N2 acetylornithine 5 transaminase , N2 acetyl L ornithine 2 oxoglutarate aminotransferase , succinylornithine aminotransferase , and 2 N acetyl L ornithine 2 oxoglutarate 5 aminotransferase . This enzyme participates in urea cycle and metabolism of amino groups . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . 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 1VEF , PDB link 1WKG , PDB link 1WKH , PDB link 2E54 , PDB link 2EH6 , and PDB link 2ORD . References reflist 1 cite journal author ALBRECHT AM, VOGEL HJ date 1964 title ACETYLORNITHINE DELTA TRANSAMINASE. PARTIAL PURIFICATION AND REPRESSION BEHAVIOR journal J. Biol. Chem. volume 239 pages 1872&ndash 6 pmid 14213368 cite journal author Vogel HJ date 1953 title Path of Ornithine Synthesis in Escherichia Coli journal Proc. Natl. Acad. Sci. U. S. A. volume ... more details
enzyme Name histidine transaminase EC number 2.6.1.38 CAS number 37277 92 2 IUBMB EC number 2 6 1 38 GO code 0008110 image width caption In enzymology , a histidine transaminase EC number 2.6.1.38 is an enzyme that catalysis catalyzes the chemical reaction L histidine 2 oxoglutarate math rightleftharpoons math imidazol 5 yl pyruvate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are L histidine and 2 oxoglutarate , whereas its two product chemistry products are imidazol 5 yl pyruvate and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L histidine 2 oxoglutarate aminotransferase . Other names in common use include histidine aminotransferase , and histidine 2 oxoglutarate aminotransferase . This enzyme participates in histidine metabolism . References reflist 1 cite journal author Coote JG, Hassall H date 1969 title The role of imidazol 5 yl lactate nicotinamide adenine dinucleotide phosphate oxidoreductase and histidine 2 oxoglutarate aminotransferase in the degradation of imidazol 5 yl lactate by Pseudomonas acidovorans journal Biochem. J. volume 111 pages 237&ndash 9 pmid 4303364 issue 2 pmc 1187811 cite journal author Wickremasinghe R, Hedegaard J and Roche J date 1967 title Degradation de la L histidine chez Escherichia coli B formation de l acide imidazolepyruvique par une histidine transaminase journal C.R. Soc. Biol. volume 161 pages 1891&ndash 1896 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
enzyme Name cysteine transaminase EC number 2.6.1.3 CAS number 9030 32 4 IUBMB EC number 2 6 1 3 GO code 0047801 image width caption In enzymology , a cysteine transaminase EC number 2.6.1.3 is an enzyme that catalysis catalyzes the chemical reaction L cysteine 2 oxoglutarate math rightleftharpoons math mercaptopyruvate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are L cysteine and 2 oxoglutarate , whereas its two product chemistry products are mercaptopyruvate and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L cysteine 2 oxoglutarate aminotransferase . Other names in common use include cysteine aminotransferase , L cysteine aminotransferase , and CGT . This enzyme participates in cysteine metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author CHATAGNER F, SAURET IGNAZI G date Paris title Role of transamination and pyridoxal phosphate in the enzymatic formation of hydrogen sulfide from cysteine by the rat liver under anaerobiosis. journal Bull. Soc. Chim. volume Biol. pages 415&ndash 28 pmid 13342749 issue 2 3 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ja ... more details
enzyme Name D 4 hydroxyphenylglycine transaminase EC number 2.6.1.72 CAS number 117444 05 0 IUBMB EC number 2 6 1 72 GO code 0047320 image width caption In enzymology , a D 4 hydroxyphenylglycine transaminase EC number 2.6.1.72 is an enzyme that catalysis catalyzes the chemical reaction D 4 hydroxyphenylglycine 2 oxoglutarate math rightleftharpoons math 4 hydroxyphenylglyoxylate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are D 4 hydroxyphenylglycine and 2 oxoglutarate , whereas its two product chemistry products are 4 hydroxyphenylglyoxylate and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is D 4 hydroxyphenylglycine 2 oxoglutarate aminotransferase . This enzyme is also called D hydroxyphenylglycine aminotransferase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Probst C, Grotz M, Krettek C, Pape HC date 2005 title Impact of hypothermia on the immunologic response after trauma and elective surgery journal Surg. Technol. Int. volume 14 pages 41&ndash 50 pmid 16525953 cite journal author Probst C, Grotz M, Krettek C, Pape HC date 2005 title Impact of hypothermia on the immunologic response after trauma and elective surgery journal Surg. Technol. Int. volume 14 pages 41&ndash 50 pmid 16525953 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name UDP 2 acetamido 4 amino 2,4,6 trideoxyglucose transaminase EC number 2.6.1.34 CAS number 37277 89 7 IUBMB EC number 2 6 1 34 GO code 0047302 image width caption In enzymology , an UDP 2 acetamido 4 amino 2,4,6 trideoxyglucose transaminase EC number 2.6.1.34 is an enzyme that catalysis catalyzes the chemical reaction UDP 2 acetamido 4 amino 2,4,6 trideoxyglucose 2 oxoglutarate math rightleftharpoons math UDP 2 acetamido 4 dehydro 2,6 dideoxyglucose L glutamate Thus, the two substrate biochemistry substrates of this enzyme are UDP 2 acetamido 4 amino 2,4,6 trideoxyglucose and 2 oxoglutarate , whereas its two product chemistry products are UDP 2 acetamido 4 dehydro 2,6 dideoxyglucose and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is UDP 2 acetamido 4 amino 2,4,6 trideoxyglucose 2 oxoglutarate aminotransferase . Other names in common use include uridine diphospho 4 amino 2 acetamido 2,4,6 trideoxyglucose , and aminotransferase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Distler J, Kaufman B, Roseman S date 1966 title Enzymic synthesis of a diamino sugar nucleotide by extracts of type XIV Diplococcus pneumoniae journal Arch. Biochem. Biophys. volume 116 pages 466&ndash 78 pmid 4381351 doi 10.1016 0003 9861 66 90054 3 issue 1 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
Image Malate aspartate shuttle.png right thumb 300px Diagram Illustrating the Malate Asparate Shuttle Pathway The malate aspartate shuttle sometimes also the malate shuttle is a biochemical system for translocating electrons produced during glycolysis across the semipermeable inner membrane of the mitochondrion for oxidative phosphorylation in eukaryote s. These electrons enter the electron transport chain of the mitochondria via Reducing equivalent reduction equivalents to generate adenosine triphosphate ATP . The shuttle system is required because the mitochondrial inner membrane is impermeable ... of four protein parts malate dehydrogenase in the mitochondrial matrix and intermembrane space. Aspartatetransaminaseaspartate aminotransferase in the mitochondrial matrix and intermembrane space. malate alpha Ketoglutaric acid alpha ketoglutarate antiporter in the inner membrane. Glutamate aspartate transporter glutamate aspartate antiporter in the inner membrane. Mechanism The primary enzyme in the malate aspartate shuttle is malate dehydrogenase . Malate dehydrogenase is present in two forms ... electrons to form NADH and an H sup sup is released. Oxaloacetate is then transformed into aspartate since oxaloacetate cannot be transported into the cytosol by mitochondrial aspartate aminotransferase. Since aspartate is an amino acid, an amino radical needs to be added to the oxaloacetate. This is supplied ... enzyme. The second antiporter the glutamate aspartate antiporter imports glutamate from the cytosol into the matrix and exports aspartate from the matrix to the cytosol. Once in the cytosol, aspartate is converted by cytosolic aspartate aminotransferase to oxaloacetate. The net effect of the malate aspartate shuttle is purely redox NADH in the cytosol is oxidized to NAD sup sup , and NAD sup sup ... chain so that ATP can be synthesized. Since the malate aspartate shuttle regenerates NADH inside ... Aspartate Shuttle Category Cellular respiration ca Llan adora malat aspartat de Malat Aspartat Shuttle ... more details
enzyme Name succinylornithine transaminase EC number 2.6.1.81 CAS number IUBMB EC number 2 6 1 81 GO code 0043825 image width caption Orphan date February 2009 In enzymology , a succinylornithine transaminase EC number 2.6.1.81 is an enzyme that catalysis catalyzes the chemical reaction N sub 2 sub succinyl L ornithine 2 oxoglutarate math rightleftharpoons math N succinyl L glutamate 5 semialdehyde L glutamate Thus, the two substrate biochemistry substrates of this enzyme are N2 succinyl L ornithine and 2 oxoglutarate , whereas its two product chemistry products are N succinyl L glutamate 5 semialdehyde and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is N2 succinyl L ornithine 2 oxoglutarate 5 aminotransferase . Other names in common use include succinylornithine aminotransferase , N2 succinylornithine 5 aminotransferase , AstC , SOAT , and 2 N succinyl L ornithine 2 oxoglutarate 5 aminotransferase . This enzyme participates in arginine and proline metabolism . References reflist 1 cite journal author Vander Wauven C, Stalon V date 1985 title Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia journal J. Bacteriol. volume 164 pages 882&ndash 6 pmid 2865249 issue 2 pmc 214334 cite journal author Schneider BL, Kiupakis AK, Reitzer LJ date 1998 title Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli journal J. Bacteriol. volume 180 pages 4278&ndash 86 pmid 9696779 issue 16 pmc 107427 cite journal author Cunin R, Glansdorff N, Pierard A, Stalon V date 1986 title Biosynthesis and metabolism of arginine in bacteria journal Microbiol. Rev. volume 50 pages 314&ndash 52 pmid 3534538 issue 3 pmc 373073 cite journal author Itoh Y date 1997 title Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa ... more details
enzyme Name glycine oxaloacetate transaminase EC number 2.6.1.35 CAS number 37277 90 0 IUBMB EC number 2 6 1 35 GO code 0047303 image width caption In enzymology , a glycine oxaloacetate transaminase EC number 2.6.1.35 is an enzyme that catalysis catalyzes the chemical reaction glycine oxaloacetate math rightleftharpoons math glyoxylate L aspartate Thus, the two substrate biochemistry substrates of this enzyme are glycine and oxaloacetate , whereas its two product chemistry products are glyoxylate and L aspartate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is glycine oxaloacetate aminotransferase . This enzyme is also called glycine oxaloacetate aminotransferase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Gibbs RG and Morris JG date 1966 title Formation of glycine from glyoxylate in Micrococcus denitrificans journal Biochem. J. volume 99 pages 27 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name diaminobutyrate pyruvate transaminase EC number 2.6.1.46 CAS number 37277 95 5 IUBMB EC number 2 6 1 46 GO code 0047307 image width caption In enzymology , a diaminobutyrate pyruvate transaminase EC number 2.6.1.46 is an enzyme that catalysis catalyzes the chemical reaction L 2,4 diaminobutanoate pyruvate math rightleftharpoons math L aspartate 4 semialdehyde L alanine Thus, the two substrate biochemistry substrates of this enzyme are L 2,4 diaminobutanoate and pyruvate , whereas its two product chemistry products are L aspartate 4 semialdehyde and L alanine . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L 2,4 diaminobutanoate pyruvate aminotransferase . Other names in common use include diaminobutyrate pyruvate aminotransferase , and L diaminobutyric acid transaminase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Rao DR, Hariharan K, Vijayalakshmi KR date 1969 title A study of the metabolism of L alpha gamma diaminobutyric acid in a Xanthomonas species journal Biochem. J. volume 114 pages 107&ndash 15 pmid 4390206 issue 1 pmc 1184802 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name pyridoxamine oxaloacetate transaminase EC number 2.6.1.31 CAS number 37277 88 6 IUBMB EC number 2 6 1 31 GO code 0019162 image width caption In enzymology , a pyridoxamine oxaloacetate transaminase EC number 2.6.1.31 is an enzyme that catalysis catalyzes the chemical reaction pyridoxamine oxaloacetate math rightleftharpoons math pyridoxal L aspartate Thus, the two substrate biochemistry substrates of this enzyme are pyridoxamine and oxaloacetate , whereas its two product chemistry products are pyridoxal and L aspartate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is pyridoxamine oxaloacetate aminotransferase . This enzyme participates in vitamin B6 vitamin B sub 6 sub metabolism . References reflist 1 cite journal author Wada H and Snell EE date 1962 title Enzymatic transamination of pyridoxamine. I. With oxaloacetate and alpha ketoglutarate journal J. Biol. Chem. volume 237 pages 127&ndash 132 pmid 14004226 cite journal author Wu, HLC and Mason M date 1964 title Pyridoxamine oxaloacetic transaminase of rat kidney journal J. Biol. Chem. volume 239 pages 1492&ndash 1497 pmid 14189882 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
enzyme Name aspartate N acetyltransferase EC number 2.3.1.17 CAS number 9029 99 6 IUBMB EC number 2 3 1 17 GO code 0017188 image width caption In enzymology , an aspartate N acetyltransferase EC number 2.3.1.17 is an enzyme that catalysis catalyzes the chemical reaction acetyl CoA L aspartate math rightleftharpoons math CoA N acetyl L aspartate Thus, the two substrate biochemistry substrates of this enzyme are acetyl CoA and L aspartate , whereas its two product chemistry products are coenzyme A CoA and N acetyl L aspartate . This enzyme belongs to the family of transferase s, specifically those acyltransferase s transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl CoA L aspartate N acetyltransferase . Other names in common use include aspartate acetyltransferase , and L aspartate N acetyltransferase . References reflist 1 cite journal author Goldstein FB date 1959 title Biosynthesis of N acetyl L aspartic acid journal J. Biol. Chem. volume 234 pages 2702&ndash 2706 cite journal author Knizley H Jr date 1967 title The enzymatic synthesis of N acetyl L aspartic acid by a water insoluble preparation of a cat brain acetone powder journal J. Biol. Chem. volume 242 pages 4619&ndash 22 pmid 6061408 issue 20 transferase stub Category EC 2.3.1 Category Enzymes of unknown structure it Aspartato N acetiltransferasi ... more details
Orphan date April 2011 DISPLAYTITLE Zinc small L small aspartate chembox verifiedrevid 410070772 Name Zinc small L small aspartate ImageFile Zinc L aspartate skeletal.svg ImageSize 200px ImageName Zinc aspartate IUPACName Zinc 2 S 2 amino 4 hydroxy 4 oxobutanoate OtherNames Zinc aspartate Section1 Chembox Identifiers ChemSpiderID Ref chemspidercite correct chemspider ChemSpiderID InChI SMILES InChIKey Section2 Chembox Properties Formula C sub 8 sub H sub 12 sub N sub 2 sub O sub 8 sub Zn MolarMass 329.59848 g mol Appearance White crystalline powder Odor Characteristic Density Solid Solubility SolubilityProduct MeltingPt pKb Section3 Chembox Hazards ExternalMSDS http www.chemcas.com msds cas msds142 36393 20 1.asp MSDS MainHazards FlashPt Autoignition Zinc small L small aspartate , often simply called zinc aspartate , is a chelated zinc supplement. Zinc aspartate is a salt of zinc with the amino acid aspartic acid . Chemical properties Zinc aspartate is a white crystalline powder. It is soluble in dilute hydrochloric acid and insoluble in water. ref Technical dossier, 2005f clarify date January 2011 details about what document this is referring to are needed ref Bioavailability There are no specific bioavailability studies that were made available on this dietary mineral. It is assumed that the reported solubility of zinc aspartate in diluted hydrochloric acid will allow its dissociation and absorption in the stomach. However, it was not clear if further absorption could take place in the intestine considering its reported insolubility in water. ref cite journal year 2008 month November title SCIENTIFIC OPINION. Magnesium aspartate, potassium aspartate, magnesium potassium aspartate, calcium aspartate, zinc aspartate, and copper aspartate as sources for magnesium, potassium ... EFSA Scientific Opinion ans ej883 Magnesium Aspartate op en,3.pdf?ssbinary true accessdate ... zinc aspartate is inhaled, it can cause lung irriation. It is also slightly hazardous in case of ingestion ... more details
enzyme Name asparagine oxo acid transaminase EC number 2.6.1.14 CAS number 9030 43 7 IUBMB EC number 2 6 1 14 GO code 0047297 image width caption In enzymology , an asparagine oxo acid transaminase EC number 2.6.1.14 is an enzyme that catalysis catalyzes the chemical reaction L asparagine a 2 oxo acid math rightleftharpoons math 2 oxosuccinamate an amino acid Thus, the two substrate biochemistry substrates of this enzyme are L asparagine and 2 oxo acid , whereas its two product chemistry products are 2 oxosuccinamate and amino acid . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L asparagine 2 oxo acid aminotransferase . This enzyme is also called asparagine keto acid aminotransferase . This enzyme participates in alanine and aspartate metabolism and tetracycline biosynthesis . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author MEISTER A, FRASER PE date 1954 title Enzymatic formation of L asparagine by transamination journal J. Biol. Chem. volume 210 pages 37&ndash 43 pmid 13201567 issue 1 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name beta alanine pyruvate transaminase EC number 2.6.1.18 CAS number 9030 47 1 IUBMB EC number 2 6 1 18 GO code 0016223 image width caption In enzymology , a beta alanine pyruvate transaminase EC number 2.6.1.18 is an enzyme that catalysis catalyzes the chemical reaction L alanine 3 oxopropanoate math rightleftharpoons math pyruvate beta alanine Thus, the two substrate biochemistry substrates of this enzyme are L alanine and 3 oxopropanoate , whereas its two product chemistry products are pyruvate and beta alanine . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L alanine 3 oxopropanoate aminotransferase . Other names in common use include beta alanine pyruvate aminotransferase , and beta alanine alpha alanine transaminase . This enzyme participates in 4 metabolism metabolic pathways alanine and aspartate metabolism , valine, leucine and isoleucine degradation , beta alanine metabolism , and propanoate metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author HAYAISHI O, NISHIZUKA Y, TATIBANA M, TAKESHITA M, KUNO S date 1961 title Enzymatic studies on the metabolism of beta alanine journal J. Biol. Chem. volume 236 pages 781&ndash 90 pmid 13712439 cite journal author Stinson RA, Spencer MS date 1969 title Beta alanine aminotransferase s from a plant source journal Biochem. Biophys. Res. Commun. volume 34 pages 120&ndash 7 pmid 5762452 doi 10.1016 0006 291X 69 90537 3 issue 1 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name L aspartate oxidase EC number 1.4.3.16 CAS number 69106 47 4 IUBMB EC number 1 4 3 16 GO code 0008734 image width caption In enzymology , a L aspartate oxidase EC number 1.4.3.16 is an enzyme that catalysis catalyzes the chemical reaction L aspartate H sub 2 sub O O sub 2 sub math rightleftharpoons math oxaloacetate NH sub 3 sub H sub 2 sub O sub 2 sub The 3 substrate biochemistry substrates of this enzyme are L aspartate , water H sub 2 sub O , and oxygen O sub 2 sub , whereas its 3 product chemistry products are oxaloacetate , ammonia NH sub 3 sub , and hydrogen peroxide H sub 2 sub O sub 2 sub . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is L aspartate oxygen oxidoreductase deaminating . This enzyme participates in alanine and aspartate metabolism and nicotinate and nicotinamide metabolism . It employs one cofactor biochemistry cofactor , FAD . 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 1J5P , PDB link 1KNP , and PDB link 1KNR . References reflist 1 cite journal author Nasu S, Wicks FD, Gholson RK date 1982 title L Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase journal J. Biol. Chem. volume 257 pages 626&ndash 32 pmid 7033218 issue 2 1.4 enzyme stub Category EC 1.4.3 Category Flavin enzymes Category Enzymes of known structure it L aspartato ossidasi ja L ... more details
enzyme Name aspartate ammonia lyase EC number 4.3.1.1 CAS number 9027 30 9 IUBMB EC number 4 3 1 1 GO code 0008797 image width caption In enzymology , an aspartate ammonia lyase EC number 4.3.1.1 is an enzyme that catalysis catalyzes the chemical reaction L aspartate math rightleftharpoons math fumarate NH sub 3 sub Hence, this enzyme has one substrate biochemistry substrate , L aspartate , and two product chemistry products , fumarate and ammonia NH sub 3 sub . This enzyme belongs to the family of lyase s, specifically ammonia lyases, which cleave carbon nitrogen bonds. The systematic name of this enzyme class is L aspartate ammonia lyase fumarate forming . Other names in common use include aspartase , fumaric aminase , L aspartase , and L aspartate ammonia lyase . This enzyme participates in alanine and aspartate 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 1J3U and PDB link 1JSW . References reflist 1 cite journal author Ellfolk N date 1953 title Studies on aspartase. 1. Quantitative separation of aspartase from bacterial cells, and its partial purification journal Acta Chem. Scand. volume 7 pages 824 830 doi 10.3891 acta.chem.scand.07 0824 last2 Kj rg rd first2 T. last3 B nhidi first3 Z. G. last4 Virtanen first4 Artturi I. last5 S rensen first5 Nils Andreas lyase stub Category EC 4.3.1 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 aspartate semialdehyde dehydrogenase EC number 1.2.1.11 CAS number 9000 98 0 IUBMB EC number 1 2 1 11 GO code 0004073 image width caption In enzymology , an aspartate semialdehyde dehydrogenase EC number 1.2.1.11 is an enzyme that is very important in the biosynthesis of amino acids in prokaryotes, fungi, and some higher plants. It forms an early branch point in the metabolic pathway forming lysine, methionine, leucine and isoleucine from aspartate. This pathway also produces diaminopimelate which plays an essential role in bacterial cell wall formation. There is particular interest in ASADH as disabling this enzyme proves fatal to the organism giving rise to the possibility of a new class of antibiotics, fungicides, and herbicides aimed at inhibiting it. The enzyme catalysis catalyzes the reversible chemical reaction L aspartate 4 semialdehyde phosphate NADP sup sup math rightleftharpoons math L 4 aspartyl phosphate NADPH H sup sup The 3 substrate biochemistry substrates of this enzyme are L aspartate 4 semialdehyde , phosphate , and nicotinamide adenine dinucleotide phosphate NADP sup sup , whereas its 3 product chemistry products are L 4 aspartyl phosphate , nicotinamide adenine dinucleotide phosphate NADPH , and hydrogen ion H sup sup . In physiological conditions however, the reaction runs in the opposite direction. This enzyme belongs to the family of oxidoreductase s, specifically those acting on the aldehyde or oxo group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is L aspartate 4 semialdehyde NADP oxidoreductase phosphorylating . Other names in common use include aspartate semialdehyde dehydrogenase , aspartic semialdehyde dehydrogenase , L aspartate beta semialdehyde NADP oxidoreductase , phosphorylating , aspartic beta semialdehyde dehydrogenase , and ASA dehydrogenase . This enzyme participates in glycine, serine and threonine metabolism and lysine biosynthesis . Aspartate semialdehyde dehydrogenase may be cis ... more details
enzyme Name peptide aspartate beta dioxygenase EC number 1.14.11.16 CAS number 122544 66 5 IUBMB EC number 1 14 11 16 GO code 0004597 image width caption In enzymology , a peptide aspartate beta dioxygenase EC number 1.14.11.16 is an enzyme that catalysis catalyzes the chemical reaction peptide L aspartate 2 oxoglutarate O sub 2 sub math rightleftharpoons math peptide 3 hydroxy L aspartate succinate CO sub 2 sub The 3 substrate biochemistry substrates of this enzyme are peptide L aspartate , 2 oxoglutarate , and oxygen O sub 2 sub , whereas its 3 product chemistry products are peptide 3 hydroxy L aspartate , succinate , and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of oxidoreductase s, specifically those acting on paired donors, with O sub 2 sub as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O sub 2 sub with 2 oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is peptide L aspartate,2 oxoglutarate oxygen oxidoreductase 3 hydroxylating . Other names in common use include aspartate beta hydroxylase , and aspartylpeptide beta dioxygenase . It employs one cofactor biochemistry cofactor , iron . Structural studies As of late 2007, 4 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1YCI , PDB link 2CGN , PDB link 2CGO , and PDB link 2ILM . References reflist 1 cite journal author Friedman PA date 1990 title Partial purification and characterization of bovine liver aspartyl beta hydroxylase journal J. Biol. Chem. volume 265 pages 8558&ndash 65 pmid 2187868 last2 Welsch first2 DJ last3 Vandusen first3 WJ last4 Garsky first4 VM last5 Sardana first5 MK last6 Stern first6 AM last7 Friedman first7 PA issue 15 1.14 enzyme stub Category Human 2OG oxygenases Category EC 1.14.11 Category Iron enzymes Category Enzymes of known structure it Peptide aspartato beta ... more details
enzyme Name D aspartate oxidase EC number 1.4.3.1 CAS number 9029 20 3 IUBMB EC number 1 4 3 1 GO code 0008445 image width caption In enzymology , a D aspartate oxidase EC number 1.4.3.1 is an enzyme that catalysis catalyzes the chemical reaction D aspartate H sub 2 sub O O sub 2 sub math rightleftharpoons math oxaloacetate NH sub 3 sub H sub 2 sub O sub 2 sub The 3 substrate biochemistry substrates of this enzyme are D aspartate , water H sub 2 sub O , and oxygen O sub 2 sub , whereas its 3 product chemistry products are oxaloacetate , ammonia NH sub 3 sub , and hydrogen peroxide H sub 2 sub O sub 2 sub . This enzyme belongs to the FAD dependent oxidoreductase family , specifically those acting on the CH NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is D aspartate oxygen oxidoreductase deaminating . Other names in common use include aspartic oxidase , and D aspartic oxidase . This enzyme participates in alanine and aspartate metabolism . It employs one cofactor biochemistry cofactor , FAD . The enzyme is encoded by DDO gene DDO gene. References reflist 1 cite journal author Dixon M, Kenworthy P date 1967 title D aspartate oxidase of kidney journal Biochim. Biophys. Acta. volume 146 pages 54&ndash 76 pmid 6060479 issue 1 cite journal author Still JL, Buell MV, Knox WE and Green DE date 1949 title Studies on the cyclophorase system. VII. D Aspartic oxidase journal J. Biol. Chem. volume 179 pages 831&ndash 837 cite journal author Still JL and Sperling E date 1950 title On the prosthetic group of the D aspartic oxidase journal J. Biol. Chem. volume 182 pages 585&ndash 589 CH NH2 oxidoreductases 1.4 enzyme stub Category EC 1.4.3 Category Flavin enzymes Category Enzymes of unknown structure it D aspartato ossidasi ja D ... 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 247 pages 5289&ndash 96 pmid 4626717 issue 17 cite journal author Galperin MY, Koonin EV date 1997 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 ... more details
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