enzyme Name aspartatetransaminase EC number 2.6.1.1 CAS number 9000 97 9 IUBMB EC number 2 6 1 1 GO code 0004069 image Aspartate transaminase.png width caption Aspartate aminotransferase from E. coli ... doi 10.1093 protein 7.3.405 url issn ref Aspartatetransaminase AST , also called aspartate aminotransferase AspAT ASAT AAT or serum glutamic oxaloacetic transaminase SGOT , is a pyridoxal phosphate PLP dependent transaminase enzyme EC number 2.6.1.1 . AST catalyzes the reversible transfer of an amino group between aspartate and glutamate and, as such, is an important enzyme in amino acid metabolism ... measured clinically as a marker for liver health. Function Aspartatetransaminase catalyzes the interconversion of aspartate and ketoglutarate to oxaloacetate and glutamate . Aspartate Asp ketoglutarate oxaloacetate glutamate Glu File Aspartate aminotransferase reaction.png thumb 450px Reaction catalyzed by aspartate aminotransferase As a prototypical transaminase, AST relies on PLP as a cofactor to transfer the amino group from aspartate or glutamate to the corresponding ... of aspartatetransaminase from chicken heart mitochondria X ray crystallography studies have been performed to determine the structure of aspartatetransaminase from various sources, including chicken ... Aspartatetransaminase, as with all transaminases, operates via dual substrate recognition that is, it is able ... 7801 year 1991 pmid 1868057 doi 10.1021 bi00245a019 External links MeshName AspartateTransaminase http ... AspartateTransaminase Category Liver function tests Category EC 2.6.1 de Aspartat Aminotransferase ... for the altered substrate specificity of the R292D active site mutant of aspartate aminotransferase .... ref name pmid6143829 cite journal author Kirsch JF title Mechanism of action of aspartate aminotransferase ... to form ammonium ions, which are excreted as urea . In the reverse reaction, aspartate may be synthesized ... FJ, Alvarez Ossorio MC, Relimpio AM title Purification and characterization of aspartate aminotransferase ... more details
enzyme Name aspartate phenylpyruvate transaminase EC number 2.6.1.70 CAS number 99533 45 6 IUBMB EC number 2 6 1 70 GO code 0047319 image width caption In enzymology , an aspartate phenylpyruvate transaminase EC number 2.6.1.70 is an enzyme that catalysis catalyzes the chemical reaction L aspartate phenylpyruvate math rightleftharpoons math oxaloacetate L phenylalanine Thus, the two substrate biochemistry substrates of this enzyme are L aspartate and phenylpyruvate , whereas its two product chemistry products are oxaloacetate and L phenylalanine . 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 aspartate phenylpyruvate aminotransferase . This enzyme is also called aspartate phenylpyruvate aminotransferase . References reflist 1 cite journal author Holger Z and Kula M R date 1985 title Isolation and characterization of a highly inducible L aspartate phenylpyruvate transaminase from Pseudomonas putida journal J. Biotechnol. volume 3 pages 19&ndash 31 doi 10.1016 0168 1656 85 90004 5 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
Image Aspartate transaminase.png thumb right 300px Aspartatetransaminase from E. coli with Pyridoxal 5 Phosphate cofactor In biochemistry , a transaminase or an aminotransferase is an enzyme that catalyze s a type of reaction between an amino acid and an alpha keto acid &alpha keto acid . To be specific, this reaction transamination involves removing the amino group from the amino acid, leaving behind an keto acid, and transferring it to the reactant keto acid and converting it into an amino acid. Some transamination activities of the ribosome have been found to be catalyzed by so called ribozymes RNA enzymes . Examples being the hammerhead ribozyme , the VS ribozyme and the hairpin ribozyme . The transaminase enzymes are important in the production of various amino acids, and measuring the concentration s of various transaminases in the blood is important in the diagnosing and tracking many disease s. Transaminases require the coenzyme pyridoxal phosphate , which is converted into pyridoxamine in the first phase of the reaction, when an amino acid is converted into a keto acid. Enzyme bound pyridoxamine in turn reacts with pyruvate , oxaloacetate , or alpha ketoglutarate , giving alanine , aspartic acid , or glutamic acid , respectively. Many transamination reactions occur in tissues, catalysed by transaminases specific for a particular amino keto acid pair. The reactions are readily reversible, the direction being determined by which of the reactants are in excess. The specific ... acid and pyruvic acid to make alpha ketoglutaric acid and alanine is called glutamic pyruvic transaminase or GPT for short. Tissue transaminase activities can be investigated by incubating a homogenate ... plays a key role in funneling nitrogen from amino acid metabolism to aspartate and glutamate for conversion ... GABA transaminase inhibitor References Ghany, Marc & Hoofnagle, Jay H. 2005 . Approach to the Patient ... fr Transaminase hr Transaminaze it Transaminasi ja pl Aminotransferazy pt Transaminase ... more details
enzyme Name dihydroxyphenylalanine transaminase EC number 2.6.1.49 CAS number 37277 98 8 IUBMB EC number 2 6 1 49 GO code 0047309 image width caption In enzymology , a dihydroxyphenylalanine transaminase EC number 2.6.1.49 is an enzyme that catalysis catalyzes the chemical reaction 3,4 dihydroxy L phenylalanine 2 oxoglutarate math rightleftharpoons math 3,4 dihydroxyphenylpyruvate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are 3,4 dihydroxy L phenylalanine and 2 oxoglutarate , whereas its two product chemistry products are 3,4 dihydroxyphenylpyruvate 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 3,4 dihydroxy L phenylalanine 2 oxoglutarate aminotransferase . Other names in common use include dopa transaminase , dihydroxyphenylalanine aminotransferase , aspartate DOPP transaminase ADT , L dopa transaminase , dopa aminotransferase , glutamate DOPP transaminase GDT , phenylalanine DOPP transaminase PDT , DOPA 2 oxoglutarate aminotransferase , and DOPAATS . This enzyme participates in tyrosine metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Fonnum F, Larsen K date 1965 title Purification and properties of dihydroxyphenylalanine transaminase from guinea pig brain journal J. Neurochem. volume 12 pages 589&ndash 98 pmid 5829872 doi 10.1111 j.1471 4159.1965.tb04251.x issue 7 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name aspartate 1 decarboxylase EC number 4.1.1.11 CAS number 9024 58 2 IUBMB EC number 4 1 1 11 GO code 0004068 image width caption In enzymology , an aspartate 1 decarboxylase EC number 4.1.1.11 is an enzyme that catalysis catalyzes the chemical reaction L aspartate math rightleftharpoons math beta alanine CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , L aspartate , and two product chemistry products , beta alanine and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of lyase s, specifically the carboxy lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is L aspartate 1 carboxy lyase beta alanine forming . Other names in common use include aspartate alpha decarboxylase , L aspartate alpha decarboxylase , aspartic alpha decarboxylase , and L aspartate 1 carboxy lyase . This enzyme participates in alanine and aspartate metabolism and beta alanine metabolism . Structural studies As of 2007 alt As of late 2007 , 12 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1AW8 , PDB link 1PPY , PDB link 1PQE , PDB link 1PQF , PDB link 1PQH , PDB link 1PT0 , PDB link 1PT1 , PDB link 1PYQ , PDB link 1PYU , PDB link 1UHD , PDB link 1UHE , and PDB link 2C45 . References reflist 1 cite journal author Williamson JM, Brown GM date 1979 title Purification and properties of L Aspartate alpha decarboxylase, an enzyme that catalyzes the formation of beta alanine in Escherichia coli journal J. Biol. Chem. volume 254 pages 8074&ndash 82 pmid 381298 issue 16 4.1 enzyme stub Category EC 4.1.1 Category Enzymes of known structure ... more details
enzyme Name aspartate racemase EC number 5.1.1.13 CAS number 37237 56 2 IUBMB EC number 5 1 1 13 GO code 0047689 image width caption In enzymology , an aspartate racemase EC number 5.1.1.13 is an enzyme that catalysis catalyzes the chemical reaction L aspartate math rightleftharpoons math D aspartate Hence, this enzyme has one substrate biochemistry substrate , aspartic acid L aspartate , and one product chemistry product , aspartic acid D aspartate . This enzyme belongs to the family of isomerase s, specifically those racemase s and epimerase s acting on amino acid s and derivatives. The systematic name of this enzyme class is aspartate racemase . Other names in common use include D aspartate racemase , and McyF . This enzyme participates in alanine and aspartate 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 1IU9 , PDB link 1JFL , and PDB link 2DX7 . References reflist 1 cite journal author Lamont HC, Staudenbauer WL, Strominger JL date 1972 title Partial purification and characterization of an aspartate racemase from Streptococcus faecalis journal J. Biol. Chem. volume 247 pages 5103&ndash 6 pmid 4626916 issue 16 cite journal author Yamauchi T, Choi SY, Okada H, Yohda M, Kumagai H, Esaki N, Soda K date 1992 title Properties of aspartate racemase, a pyridoxal 5 phosphate independent amino acid racemase journal J. Biol. Chem. volume 267 pages 18361&ndash 4 pmid 1526977 issue 26 cite journal author Liu L, Iwata K, Kita A, Kawarabayasi Y, Yohda M, Miki K date 2002 title Crystal structure of aspartate racemase from Pyrococcus horikoshii OT3 and its implications for molecular mechanism of PLP independent racemization journal J. Mol. Biol. volume 319 ... Microcystis aeruginosa encodes an aspartate racemase journal Biochem. J. volume 373 pages 909&ndash ... aspartate racemase from Bifidobacterium bifidum journal Eur. J. Biochem. volume 271 pages 4798&ndash ... more details
enzyme Name aspartate 4 decarboxylase EC number 4.1.1.12 CAS number 9024 57 1 IUBMB EC number 4 1 1 12 GO code 0047688 image width caption In enzymology , an aspartate 4 decarboxylase EC number 4.1.1.12 is an enzyme that catalysis catalyzes the chemical reaction L aspartate math rightleftharpoons math L alanine CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , L aspartate , and two product chemistry products , L alanine and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of lyase s, specifically the carboxy lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is L aspartate 4 carboxy lyase L alanine forming . Other names in common use include desulfinase , aminomalonic decarboxylase , aspartate beta decarboxylase , aspartate omega decarboxylase , aspartic omega decarboxylase , aspartic beta decarboxylase , L aspartate beta decarboxylase , cysteine sulfinic desulfinase , L cysteine sulfinate acid desulfinase , and L aspartate 4 carboxy lyase . This enzyme participates in alanine and aspartate metabolism and cysteine metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Kakimoto T, Kato J, Shibatani T, Nishimura N, Chibata I date 1969 title Crystalline L aspartate beta decarboxylase of Pseudomonas dacunhae I. Crystallization and some physiocochemical properties journal J. Biol. Chem. volume 244 pages 353&ndash 8 pmid 5773301 issue 2 cite journal author Novogrodsky A and Meister A date 1964 title Control of aspartate beta decarboxylase activity by transamination journal J. Biol. Chem. volume 239 pages 879&ndash 888 pmid 14154469 cite journal author Palekar AG, Tate SS, Meister A date 1970 title Inhibition of aspartate beta decarboxylase by aminomalonate Stereospecific decarboxylation of aminomalonate to glycine journal Biochemistry. volume ... EM and Kornberg HL date 1963 title Properties of crystalline l aspartate 4 carboxy lyase from Achromobacter ... more details
enzyme Name Aspartate dehydrogenase EC number 1.4.1.21 CAS number 37278 97 0 IUBMB EC number 1 4 1 21 GO code image width caption Aspartate dehydrogenase EC number 1.4.1.21 is an enzyme that catalysis catalyzes the chemical reaction L aspartate H sub 2 sub O NAD P math rightleftharpoons math oxaloacetate NH sub 3 sub NAD P H H sup sup The 4 substrate biochemistry substrates of this enzyme are L aspartic acid aspartate , water , nicotinamide adenine dinucleotide ion, and nicotinamide adenine dinucleotide phosphate ion, whereas its 5 product chemistry products are oxaloacetate , ammonia , nicotinamide adenine dinucleotide NADH , nicotinamide adenine dinucleotide phosphate , and hydrogen ion . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH NH2 group of donors with NAD or NADP as acceptor. The systematic name of this enzyme class is L aspartate NAD P oxidoreductase deaminating . Other names in common use include NAD dependent aspartate dehydrogenase , NADH2 dependent aspartate dehydrogenase , and NADP dependent aspartate dehydrogenase . This enzyme participates in nicotinate and nicotinamide metabolism. Structural studies As of late 2007, only one tertiary structure structure has been solved for this class of enzymes, with the Protein Data Bank PDB accession code PDB link 2DC1 . References reflist 1 cite journal author Tong L date 2003 title Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643 journal J. Biol. Chem. volume 278 pages 8804&ndash 8 pmid 12496312 doi 10.1074 jbc.M211892200 last2 Savchenko first2 A last3 Yakunin first3 A last4 Zhang first4 R last5 Edwards first5 A last6 Arrowsmith first6 C last7 Tong first7 L issue 10 cite journal author Okamura T, Noda H, Fukuda S, Ohsugi M date Tokyo title Aspartate dehydrogenase in vitamin B12 producing Klebsiella pneumoniae IFO 13541 journal J. Nutr. Sci. volume Vitaminol. pages 483&ndash 90 pmid 9819709 issue 4 cite journal author ... more details
infobox enzyme Name Aspartate carbamoyltransferase EC number 2.1.3.2 CAS number 9012 49 1 IUBMB EC number 2 1 3 2 GO code 0004070 image Apartate carbamoyltransferase pdb 2ATC.png width caption Aspartate ... phosphate synthetase 2, aspartate transcarbamoylase, dihydroorotase caption image width HGNCid 1424 ... Chromosome 2 Arm p Band 22 LocusSupplementaryData p21 Aspartate carbamoyltransferase also known as aspartate transcarbamoylase or ATCase catalyze s the first step in the pyrimidine biosynthetic ... in Escherichia coli aspartate transcarbamoylase journal Nature Structural Biology volume 8 issue ... S, Braus GH title Allosteric regulation of catalytic activity Escherichia coli aspartate transcarbamoylase ... of aspartate and carbamyl phosphate to form N carbamyl L aspartate and inorganic phosphate . ATCase ... activity. Image ATCase reaction.jpg Reaction of aspartate transcarbamylase. Structure Image Aspartate ... of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6 resolution journal Proceedings ..., which have different roles. ref name pmid8154326 cite journal author Lipscomb WN title Aspartate ... ref The catalytic subunits catalyze the carbamylation of the amino group of aspartate but do not have ... domains is composed of two structural domains, the aspartate domain, which contains most of the residues responsible for binding aspartate , and the carbamoyl phosphate domain, which contains ... aspartate transcarbamylase the relation between structure and function journal Science volume 241 ... by the binding of a bisubstrate analogue, N phosphonoacetyl L aspartate PALA . ref name pmid3586030 cite journal author Krause KL, Volz KW, Lipscomb WN title 2.5 structure of aspartate carbamoyltransferase complexed with the bisubstrate analog N phosphonacetyl L aspartate journal Journal of molecular ... in aspartate transcarbamoylase journal Proceedings of the National Academy of Sciences of the United ... of carbamoyl phosphate and succinate bound to aspartate carbamoyltransferase journal Proceedings of the National ... more details
Drugbox verifiedrevid 428769099 IUPAC name magnesium 2S 2 amino 4 hydroxy 4 oxobutanoate image magnesium aspartate.png Clinical data tradename Drugs.com drugs.com CDI magnesium aspartate pregnancy AU A B1 B2 B3 C D X pregnancy US A B C D X pregnancy category legal AU Unscheduled S2 S3 S4 S5 S6 S7 S8 S9 legal CA Schedule I, II, III, IV, V, VI, VII, VIII legal UK GSL P POM CD Class A, B, C legal US OTC Rx only Schedule I, II, III, IV, V legal status routes of administration Pharmacokinetic data bioavailability protein bound metabolism elimination half life excretion Identifiers CAS number ATC prefix A12 ATC suffix CC05 PubChem 16211203 DrugBank Ref drugbankcite correct drugbank DrugBank Chemical data chemical formula C sub 8 sub H sub 12 sub MgN sub 2 sub O sub 8 sub molecular weight 288.494 g mol Magnesium aspartate , the magnesium salt chemistry salt of aspartic acid , is a Dietary mineral mineral supplement . Mineral supplements Category Magnesium compounds Category Salts and esters of carboxylic acids gastrointestinal drug stub ... more details
ref See also Aspartatetransaminase Liver function tests References reflist External links MeshName Alanine transaminase http www.nlm.nih.gov medlineplus ency article 003473.htm ALT MedlinePlus ...protein Name glutamic pyruvate transaminase caption image width HGNCid 4552 Symbol GPT AltSymbols EntrezGene 2875 OMIM 138200 RefSeq NM 005309 UniProt P24298 PDB ECnumber 2.6.1.2 Chromosome 8 Arm q Band 24.2 LocusSupplementaryData qter infobox enzyme Name Alanine transaminase EC number 2.6.1.2 CAS number 9000 86 6 IUBMB EC number 2 6 1 2 GO code 0004021 image width caption Alanine transaminase or ALT is a transaminase enzyme EC number 2.6.1.2 . It is also called serum glutamic pyruvic transaminase SGPT or alanine aminotransferase ALAT . ALT is found in blood plasma serum and in various bodily tissues, but is most commonly associated with the liver . It catalyzes the two parts of the alanine cycle . Function It catalyzes the transfer of an amino group from alanine to Alpha Ketoglutaric acid ketoglutarate , the products of this reversible transamination reaction being pyruvate and glutamate . glutamate pyruvate unicode & 8652 alpha ketoglutaric acid ketoglutarate alanine Image Alanine amino transf rase.png thumb none 600px Alanine transaminase Clinical significance It is commonly measured clinically as a part of a diagnostic evaluation of Liver function tests hepatocellular injury , to determine liver health. When used in diagnostics, it is almost always measured in international units liter U L . ref name Wang2012 cite journal last1 Wang first1 CS year 2012 title Impact of increasing ... transaminase shows a marked diurnal variation . Elevated levels class wikitable Patient type ... Liver Transaminase Levels in the Asymptomatic Patient , American Family Physician . ref When elevated ... DEFAULTSORT Alanine Transaminase Category Biomarkers Category Liver function tests Category Enzymes ... amino transf rase hr Alanin transaminaza id Alanina transaminase it Alanina transaminasi nl Alanine ... more details
of protease enzymes that use an aspartate residue for catalysis of their peptide substrates. In general, they have two highly conserved aspartate s in the active site and are optimally active at acidic ... coordination of a water molecule between the two highly conserved aspartate residues. ref name pmid3313384 ... 1 pages 5 14 year 2003 pmid 12929379 doi 10.1039 b208248a ref One aspartate activates the water by abstracting ... Pepstatin is an inhibitor of aspartate proteases. External links The MEROPS online database for peptidases ... acid proteases InterPro content IPR000036 DEFAULTSORT Aspartate Protease Category Protein domains ... more details
enzyme Name aminolevulinate transaminase EC number 2.6.1.43 CAS number 9012 46 8 IUBMB EC number 2 6 1 43 GO code 0047665 image width caption In enzymology , an aminolevulinate transaminase EC number 2.6.1.43 is an enzyme that catalysis catalyzes the chemical reaction 5 aminolevulinate pyruvate math rightleftharpoons math 4,5 dioxopentanoate L alanine Thus, the two substrate biochemistry substrates of this enzyme are 5 aminolevulinate and pyruvate , whereas its two product chemistry products are 4,5 dioxopentanoate 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 5 aminolevulinate pyruvate aminotransferase . Other names in common use include aminolevulinate aminotransferase, gamma,delta dioxovalerate , aminotransferase , gamma,delta dioxovaleric acid transaminase , 4,5 dioxovalerate aminotransferase , 4,5 dioxovaleric acid transaminase , 4,5 dioxovaleric transaminase , 5 aminolevulinic acid transaminase , alanine gamma,delta dioxovalerate aminotransferase , alanine dioxovalerate aminotransferase , alanine 4,5 dioxovalerate aminotransferase , aminolevulinic acid transaminase , dioxovalerate transaminase , L alanine 4,5 dioxovalerate aminotransferase , L alanine 4,5 dioxovaleric acid transaminase , L alanine dioxovalerate transaminase , DOVA transaminase , and 4,5 dioxovaleric acid aminotransferase . This enzyme participates in porphyrin and chlorophyll metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Gibson KD, Matthew M and Neuberger A date 1961 title Biosynthesis of porphyrins and chlorophylls journal Nature volume 192 issue 4799 pages 204&ndash 208 doi 10.1038 192204a0 pmid 13898421 cite journal author NEUBERGER A, TURNER JM date 1963 title gamma,delta Dioxovalerate aminotransferase activity in Rhodopseudomonas spheroides journal Biochim. Biophys. Acta. volume 67 ... more details
enzyme Name diamine transaminase EC number 2.6.1.29 CAS number 9031 83 8 IUBMB EC number 2 6 1 29 GO code 0019161 image width caption In enzymology , a diamine transaminase EC number 2.6.1.29 is an enzyme that catalysis catalyzes the chemical reaction an alpha,omega diamine 2 oxoglutarate math rightleftharpoons math an omega aminoaldehyde L glutamate Thus, the two substrate biochemistry substrates of this enzyme are alpha,omega diamine and 2 oxoglutarate , whereas its two product chemistry products are omega aminoaldehyde 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 diamine 2 oxoglutarate aminotransferase . Other names in common use include amine transaminase , amine ketoacid transaminase , diamine aminotransferase , and diamine ketoglutaric transaminase . This enzyme participates in urea cycle and metabolism of amino groups . References reflist 1 cite journal author Kim K date 1964 title Purification and properties of a diamine alpha ketoglutarate transaminase from Escherichia coli journal J. Biol. Chem. volume 239 pages 783&ndash 786 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
enzyme Name 2 aminoadipate transaminase EC number 2.6.1.39 CAS number 9033 00 5 IUBMB EC number 2 6 1 39 GO code 0047536 image width caption In enzymology , a 2 aminoadipate transaminase EC number 2.6.1.39 is an enzyme that catalysis catalyzes the chemical reaction L 2 aminoadipate 2 oxoglutarate math rightleftharpoons math 2 oxoadipate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are L 2 aminoadipate and 2 oxoglutarate , whereas its two product chemistry products are 2 oxoadipate 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 aminoadipate 2 oxoglutarate aminotransferase . Other names in common use include alpha aminoadipate aminotransferase , 2 aminoadipate aminotransferase , 2 aminoadipic aminotransferase , glutamic ketoadipic transaminase , and glutamate alpha ketoadipate transaminase . This enzyme participates in lysine biosynthesis and lysine degradation . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . 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 2DTV . References reflist 1 cite journal author Matsuda M, Ogur M date 1969 title Separation and specificity of the yeast glutamate alpha ketoadipate transaminase journal J. Biol. Chem. volume 244 pages 3352&ndash 8 pmid 5792664 issue 12 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of known structure ... more details
enzyme Name glycine transaminase EC number 2.6.1.4 CAS number 9032 99 9 IUBMB EC number 2 6 1 4 GO code 0047958 image width caption In enzymology , a glycine transaminase EC number 2.6.1.4 is an enzyme that catalysis catalyzes the chemical reaction glycine 2 oxoglutarate math rightleftharpoons math glyoxylate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are glycine and 2 oxoglutarate , whereas its two product chemistry products are glyoxylate 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 glycine 2 oxoglutarate aminotransferase . Other names in common use include glutamic glyoxylic transaminase , glycine aminotransferase , glyoxylate glutamic transaminase , L glutamate glyoxylate aminotransferase , and glyoxylate glutamate aminotransferase . This enzyme participates in glycine, serine and threonine metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Nakada HI year 1964 title Glutamic glycine transaminase from rat liver journal J. Biol. Chem. volume 239 pages 468&ndash 471 pmid 14169146 cite journal author Thompson JS and Richardson KE year 1966 title Isolation and chracterization of a glutamate glycine transaminase from human liver journal Arch. Biochem. Biophys. volume 117 issue 3 pages 599&ndash 603 doi 10.1016 0003 9861 66 90101 9 Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure transferase stub ... more details
enzyme Name leucine transaminase EC number 2.6.1.6 CAS number 9030 37 9 IUBMB EC number 2 6 1 6 GO code 0050048 image width caption In enzymology , a leucine transaminase EC number 2.6.1.6 is an enzyme that catalysis catalyzes the chemical reaction L leucine 2 oxoglutarate math rightleftharpoons math 4 methyl 2 oxopentanoate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are L leucine and 2 oxoglutarate , whereas its two product chemistry products are 4 methyl 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 L leucine 2 oxoglutarate aminotransferase . Other names in common use include L leucine aminotransferase , leucine 2 oxoglutarate transaminase , leucine aminotransferase , and leucine alpha ketoglutarate transaminase . This enzyme participates in 3 metabolism metabolic pathways valine, leucine and isoleucine degradation , valine, leucine and isoleucine biosynthesis , and pantothenate and coa biosynthesis . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Aki K, Ogawa K, Ichihara A date 1968 title Transaminases of branched chain amino acids. IV. Purification and properties of two enzymes from rat liver journal Biochim. Biophys. Acta. volume 159 pages 276&ndash 84 pmid 4968655 issue 2 cite journal author Ikeda T, Konishi Y, Ichihara A date 1976 title Transaminase of branched chain amino acids. XI. Leucine methionine transaminase of rat liver mitochondria journal Biochim. Biophys. Acta. volume 445 pages 622&ndash 31 pmid 974100 issue 3 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name S 3 amino 2 methylpropionate transaminase EC number 2.6.1.22 CAS number 9031 95 2 IUBMB EC number 2 6 1 22 GO code 0047298 image width caption In enzymology , a S 3 amino 2 methylpropionate transaminase EC number 2.6.1.22 is an enzyme that catalysis catalyzes the chemical reaction S 3 amino 2 methylpropanoate 2 oxoglutarate math rightleftharpoons math 2 methyl 3 oxopropanoate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are S 3 amino 2 methylpropanoate and 2 oxoglutarate , whereas its two product chemistry products are 2 methyl 3 oxopropanoate 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 S 3 amino 2 methylpropanoate 2 oxoglutarate aminotransferase . Other names in common use include L 3 aminoisobutyrate transaminase , beta aminobutyric transaminase , L 3 aminoisobutyric aminotransferase , and beta aminoisobutyrate alpha ketoglutarate transaminase . This enzyme participates in valine, leucine and isoleucine degradation . References reflist 1 cite journal author Kakimoto Y, Kanazawa A, Taniguchi K, Sano I date 1968 title Beta aminoisobutyrate alpha ketoglutarate transaminase in relation to beta aminoisobutyric aciduria journal Biochim. Biophys. Acta. volume 156 pages 374&ndash 80 pmid 5641913 issue 2 cite journal author Tamaki N, Sakata SF, Matsuda K date 2000 title Purification, properties, and sequencing of aminoisobutyrate aminotransferases from rat liver journal Methods Enzymol. volume 324 pages 376&ndash 89 pmid 10989446 doi 10.1016 S0076 6879 00 24247 X series Methods in Enzymology isbn 9780121822255 Category EC 2.6.1 Category Enzymes of unknown structure transferase stub ... more details
enzyme Name Aspartate prephenate aminotransferase EC number 2.6.1.78 CAS number IUBMB EC number 2 6 1 78 GO code image width caption In enzymology , an aspartate prephenate aminotransferase EC number 2.6.1.78 is an enzyme that catalysis catalyzes the chemical reaction L arogenate oxaloacetate math rightleftharpoons math prephenate L aspartate Thus, the two substrate biochemistry substrates of this enzyme are L arogenate and oxaloacetate , whereas its two product chemistry products are prephenate 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 L arogenate oxaloacetate aminotransferase . Other names in common use include prephenate transaminase ambiguous , PAT ambiguous , prephenate aspartate aminotransferase , and L aspartate prephenate aminotransferase . References reflist 1 cite journal author De Eknamkul W, Ellis BE date 1988 title Purification and characterization of prephenate aminotransferase from Anchusa officinalis cell cultures journal Arch. Biochem. Biophys. volume 267 pages 87&ndash 94 pmid 3196038 doi 10.1016 0003 9861 88 90011 2 issue 1 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
enzyme Name 5 aminovalerate transaminase EC number 2.6.1.48 CAS number 37277 97 7 IUBMB EC number 2 6 1 48 GO code 0047589 image width caption In enzymology , a 5 aminovalerate transaminase EC number 2.6.1.48 is an enzyme that catalysis catalyzes the chemical reaction 5 aminopentanoate 2 oxoglutarate math rightleftharpoons math 5 oxopentanoate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are 5 aminopentanoate and 2 oxoglutarate , whereas its two product chemistry products are 5 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 5 aminopentanoate 2 oxoglutarate aminotransferase . Other names in common use include 5 aminovalerate aminotransferase , delta aminovalerate aminotransferase , and delta aminovalerate transaminase . This enzyme participates in lysine degradation . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Ichihara A, Ichihara EA and Suda M date Tokyo title Metabolism of L lysine by bacterial enzymes. IV. delta Aminovaleric acid glutamic acid transaminase journal J. volume Biochem. pages 412&ndash 420 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name succinyldiaminopimelate transaminase EC number 2.6.1.17 CAS number 9030 46 0 IUBMB EC number 2 6 1 17 GO code 0009016 image width caption In enzymology , a succinyldiaminopimelate transaminase EC number 2.6.1.17 is an enzyme that catalysis catalyzes the chemical reaction N succinyl L 2,6 diaminoheptanedioate 2 oxoglutarate math rightleftharpoons math N succinyl L 2 amino 6 oxoheptanedioate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are N succinyl L 2,6 diaminoheptanedioate and 2 oxoglutarate , whereas its two product chemistry products are N succinyl L 2 amino 6 oxoheptanedioate 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 N succinyl L 2,6 diaminoheptanedioate 2 oxoglutarate aminotransferase . Other names in common use include succinyldiaminopimelate aminotransferase , and N succinyl L diaminopimelic glutamic transaminase . This enzyme participates in lysine biosynthesis . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Peterkofsky B and Gilvarg C date 1961 title N Succinyl L diaminopimelic glutamic transaminase journal J. Biol. Chem. volume 236 pages 1432&ndash 1438 pmid 13734750 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name diiodotyrosine transaminase EC number 2.6.1.24 CAS number 9033 18 5 IUBMB EC number 2 6 1 24 GO code 0047861 image width caption In enzymology , a diiodotyrosine transaminase EC number 2.6.1.24 is an enzyme that catalysis catalyzes the chemical reaction 3,5 diiodo L tyrosine 2 oxoglutarate math rightleftharpoons math 4 hydroxy 3,5 diiodophenylpyruvate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are 3,5 diiodo L tyrosine and 2 oxoglutarate , whereas its two product chemistry products are 4 hydroxy 3,5 diiodophenylpyruvate 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 3,5 diiodo L tyrosine 2 oxoglutarate aminotransferase . Other names in common use include diiodotyrosine aminotransferase , halogenated tyrosine aminotransferase , and halogenated tyrosine transaminase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Nakano M year 1967 title Purification and properties of halogenated tyrosine and thyroid hormone transaminase from rat kidney mitochondria journal J. Biol. Chem. volume 242 pages 73&ndash 81 pmid 4381052 issue 1 cite journal author Nakano M and Danowski TS year 1964 title Thyroid hormone transaminase and oxidase in rat kidney mitochondria journal Biochim. Biophys. Acta volume 85 pages 18&ndash 28 pmid 14159298 Transaminases Thyroid hormone metabolism enzymes and transporters Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure transferase stub ja ... more details
enzyme Name tryptophan transaminase EC number 2.6.1.27 CAS number 9022 98 4 IUBMB EC number 2 6 1 27 GO code 0050362 image width caption In enzymology , a tryptophan transaminase EC number 2.6.1.27 is an enzyme that catalysis catalyzes the chemical reaction L tryptophan 2 oxoglutarate math rightleftharpoons math indol 3 yl pyruvate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are L tryptophan and 2 oxoglutarate , whereas its two product chemistry products are indol 3 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 tryptophan 2 oxoglutarate aminotransferase . Other names in common use include L phenylalanine 2 oxoglutarate aminotransferase , tryptophan aminotransferase , 5 hydroxytryptophan ketoglutaric transaminase , hydroxytryptophan aminotransferase , L tryptophan aminotransferase , and L tryptophan transaminase . This enzyme participates in tryptophan metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author George H, Gabay S year 1968 title Brain aromatic aminotransferase. I. Purification and some properties of pig brain L phenylalanine 2 oxoglutarate aminotransferase journal Biochim. Biophys. Acta. volume 167 pages 555&ndash 66 pmid 5722279 issue 3 cite journal author O Neil SR, DeMoss RD year 1968 title Tryptophan transaminase from Clostridium sporogenes journal Arch. Biochem. Biophys. volume 127 pages 361&ndash 9 pmid 5697992 doi 10.1016 0003 9861 68 90237 3 issue 1 cite journal author Tangen O, Fonnum F and Haavaldsen R year 1965 title Separation and purification of aromatic amino acid transaminases from rat brain journal Biochim. Biophys. Acta volume 96 pages 82&ndash 90 pmid 14285270 Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure transferase stub ... more details
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