The Enzyme Database

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EC 2.6.1.1     
Accepted name: aspartate transaminase
Reaction: L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
For diagram of EC 2.6.1, click here
Other name(s): glutamic-oxaloacetic transaminase; glutamic-aspartic transaminase; transaminase A; AAT; AspT; 2-oxoglutarate-glutamate aminotransferase; aspartate α-ketoglutarate transaminase; aspartate aminotransferase; aspartate-2-oxoglutarate transaminase; aspartic acid aminotransferase; aspartic aminotransferase; aspartyl aminotransferase; AST; glutamate-oxalacetate aminotransferase; glutamate-oxalate transaminase; glutamic-aspartic aminotransferase; glutamic-oxalacetic transaminase; glutamic oxalic transaminase; GOT (enzyme) [ambiguous]; L-aspartate transaminase; L-aspartate-α-ketoglutarate transaminase; L-aspartate-2-ketoglutarate aminotransferase; L-aspartate-2-oxoglutarate aminotransferase; L-aspartate-2-oxoglutarate-transaminase; L-aspartic aminotransferase; oxaloacetate-aspartate aminotransferase; oxaloacetate transferase; aspartate:2-oxoglutarate aminotransferase; glutamate oxaloacetate transaminase
Systematic name: L-aspartate:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. Also acts on L-tyrosine, L-phenylalanine and L-tryptophan. Aspartate transaminase activity can be formed from the aromatic-amino-acid transaminase (EC 2.6.1.57) of Escherichia coli by controlled proteolysis [7], some EC 2.6.1.57 activity can be found in this enzyme from other sources [8]; indeed the enzymes are identical in Trichomonas vaginalis [6].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9000-97-9
References:
1.  Banks, B.E.C. and Vernon, C.A. Transamination. Part I. The isolation of the apoenzyme of glutamic-aspartic transaminase from pig heart muscle. J. Chem. Soc. (Lond.) (1961) 1698–1705.
2.  Bertland, L.H. and Kaplan, N.O. Chicken heart soluble aspartate aminotransferase. Purification and properties. Biochemistry 7 (1968) 134–142. [PMID: 5758538]
3.  Forest, J.C. and Wightman, F. Amino acid metabolism in plants. III. Purification and some properties of a multispecific aminotransferase isolated from bushbean seedlings (Phaseolus vulgaris L.). Can. J. Biochem. 50 (1973) 813–829.
4.  Henson, C.P. and Cleland, W.W. Kinetic studies of glutamic oxaloacetic transaminase isozymes. Biochemistry 3 (1964) 338–345. [PMID: 14155095]
5.  Jenkins, W.T., Yphantis, D.A. and Sizer, I.W. Glutamic aspartic transaminase. I. Assay, purification, and general properties. J. Biol. Chem. 234 (1959) 51–57. [PMID: 13610891]
6.  Lowe, P.N. and Rowe, A.F. Aspartate: 2-oxoglutarate aminotransferase from Trichomonas vaginalis. Identity of aspartate aminotransferase and aromatic amino acid aminotransferase. Biochem. J. 232 (1985) 689–695. [PMID: 3879173]
7.  Mavrides, C. and Orr, W. Multispecific aspartate and aromatic amino acid aminotransferases in Escherichia coli. J. Biol. Chem. 250 (1975) 4128–4133. [PMID: 236311]
8.  Schreiber, G., Eckstein, M., Oeser, A. and Holzer, H. [The concentration of aspartate aminotransferase from brewers’ yeast] Biochem. Z. 340 (1964) 13–20. [PMID: 14317947]
9.  Shrawder, E. and Martinez-Carrion, M. Evidence of phenylalanine transaminase activity in the isoenzymes of aspartate transaminase. J. Biol. Chem. 247 (1972) 2486–2492. [PMID: 4623131]
[EC 2.6.1.1 created 1961, modified 1976]
 
 
EC 2.6.1.2     
Accepted name: alanine transaminase
Reaction: L-alanine + 2-oxoglutarate = pyruvate + L-glutamate
For diagram of reaction, click here and for mechanism, click here
Other name(s): glutamic-pyruvic transaminase; glutamic-alanine transaminase; GPT (ambiguous); β-alanine aminotransferase; alanine aminotransferase; alanine-α-ketoglutarate aminotransferase; alanine-pyruvate aminotransferase; ALT; glutamic acid-pyruvic acid transaminase; glutamic-pyruvic aminotransferase; L-alanine aminotransferase; L-alanine transaminase; L-alanine-α-ketoglutarate aminotransferase; pyruvate transaminase; pyruvate-alanine aminotransferase; pyruvate-glutamate transaminase
Systematic name: L-alanine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. 2-Aminobutanoate can act slowly instead of alanine.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9000-86-6
References:
1.  Dumitru, I.F., Iordachescu, D. and Niculescu, S. Chromatographic purification, crystallization and study of vegetable L-alanine: 2-oxoglutarate-aminotransferase properties. Experientia 26 (1970) 837–838. [PMID: 5452003]
2.  Dumitru, I.F., Iordachescu, D. and Niculescu, S. L-Alanine: 2-oxoglutarate-aminotransferase chromatographic purification and crystallization of the enzyme from seeds of Glycine hispida var Cheepeura. Rev. Roum. Biochim. 7 (1970) 31–44.
3.  Green, D.E., Leloir, L.F. and Nocito, W. Transaminases. J. Biol. Chem. 161 (1945) 559–582. [PMID: 21006939]
4.  Iordachescu, D., Dumitru, I.F. and Corniciuc, M.-T. Comparative biochemical studies concerning L-alanine: 2-oxoglutarate-aminotransferase from the liver and the bile of swines. Rev. Roum. Biochim. 20 (1983) 173–179.
5.  Wilson, D.G., King, K.W. and Burris, R.H. Transaminase reactions in plants. J. Biol. Chem. 208 (1954) 863–874. [PMID: 13174595]
[EC 2.6.1.2 created 1961]
 
 
EC 2.6.1.3     
Accepted name: cysteine transaminase
Reaction: L-cysteine + 2-oxoglutarate = mercaptopyruvate + L-glutamate
For diagram of reaction, click here and for mechanism, click here
Other name(s): cysteine aminotransferase; L-cysteine aminotransferase; CGT
Systematic name: L-cysteine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9030-32-4
References:
1.  Chatagner, F. and Sauret-Ignazi, G. Role des transamination et du phosphate de pyridoxal dans la formation enzymatique de H2S a partir de la cystéine par le foie du rat en anaérobiose. Bull. Soc. Chim. Biol. 38 (1956) 415–428. [PMID: 13342749]
[EC 2.6.1.3 created 1961]
 
 
EC 2.6.1.4     
Accepted name: glycine transaminase
Reaction: glycine + 2-oxoglutarate = glyoxylate + L-glutamate
For diagram of reaction, click here and for mechanism, click here
Other name(s): glutamic-glyoxylic transaminase; glycine aminotransferase; glyoxylate-glutamic transaminase; L-glutamate:glyoxylate aminotransferase; glyoxylate-glutamate aminotransferase
Systematic name: glycine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9032-99-9
References:
1.  Nakada, H.I. Glutamic-glycine transaminase from rat liver. J. Biol. Chem. 239 (1964) 468–471. [PMID: 14169146]
2.  Thompson, J.S. and Richardson, K.E. Isolation and chracterization of a glutamate-glycine transaminase from human liver. Arch. Biochem. Biophys. 117 (1966) 599–603.
[EC 2.6.1.4 created 1961, modified 1982]
 
 
EC 2.6.1.5     
Accepted name: tyrosine transaminase
Reaction: L-tyrosine + 2-oxoglutarate = 4-hydroxyphenylpyruvate + L-glutamate
For diagram of reaction, click here, for mechanism, click here , for diagram of phenylalanine and tyrosine biosynthesis, click here and for diagram of the methionine-salvage pathway, click here
Other name(s): tyrosine aminotransferase; glutamic-hydroxyphenylpyruvic transaminase; glutamic phenylpyruvic aminotransferase; L-phenylalanine 2-oxoglutarate aminotransferase; L-tyrosine aminotransferase; phenylalanine aminotransferase; phenylalanine transaminase; phenylalanine-α-ketoglutarate transaminase; phenylpyruvate transaminase; phenylpyruvic acid transaminase; tyrosine-α-ketoglutarate aminotransferase; tyrosine-α-ketoglutarate transaminase; tyrosine-2-ketoglutarate aminotransferase; TyrAT
Systematic name: L-tyrosine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. L-Phenylalanine can act instead of L-tyrosine. The mitochondrial enzyme may be identical with EC 2.6.1.1 (aspartate transaminase). The three isoenzymic forms are interconverted by EC 3.4.22.32 (stem bromelain) and EC 3.4.22.33 (fruit bromelain). The enzyme can also catalyse the final step in the methionine-salvage pathway of Klebsiella pneumoniae [8].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 9014-55-5
References:
1.  Canellakis, Z.N. and Cohen, P.P. Purification studies of tyrosine-α-ketoglutaric acid transaminase. J. Biol. Chem. 222 (1956) 53–62. [PMID: 13366978]
2.  Canellakis, Z.N. and Cohen, P.P. Kinetic and substrate specificity study of tyrosine-α-ketoglutaric acid transaminase. J. Biol. Chem. 222 (1956) 63–71. [PMID: 13366979]
3.  Jacoby, G.A. and La Ru, B.N. Studies on the specificity of tyrosine-α-ketoglutarate transaminase. J. Biol. Chem. 239 (1964) 419–424. [PMID: 14171223]
4.  Kenney, F.T. Properties of partially purified tyrosine-α-ketoglutarate transaminase from rat liver. J. Biol. Chem. 234 (1959) 2707–2712. [PMID: 14408534]
5.  Miller, J.E. and Litwack, G. Purification, properties, and identity of liver mitochondrial tyrosine aminotransferase. J. Biol. Chem. 246 (1971) 3234–3240. [PMID: 4396841]
6.  Rowsell, E.V. Transaminations with L-glutamate and α-oxoglutarate in fresh extracts of animal tissues. Biochem. J. 64 (1956) 235–245. [PMID: 13363833]
7.  SentheShanmuganathan, S. The purification and properties of the tyrosine-2-oxoglutarate transaminase of Saccharomyces cerevisiae. Biochem. J. 77 (1960) 619–625. [PMID: 13750129]
8.  Heilbronn, J., Wilson, J. and Berger, B.J. Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumoniae. J. Bacteriol. 181 (1999) 1739–1747. [PMID: 10074065]
[EC 2.6.1.5 created 1961]
 
 
EC 2.6.1.6     
Accepted name: leucine transaminase
Reaction: L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate
For diagram of reaction, click here, for diagram of leucine biosynthesis, click here and for diagram of mechanism, click here
Other name(s): L-leucine aminotransferase; leucine 2-oxoglutarate transaminase; leucine aminotransferase; leucine-α-ketoglutarate transaminase
Systematic name: L-leucine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. This enzyme differs from EC 2.6.1.42, branched-chain-amino-acid transaminase, in that it does not act on L-valine or L-isoleucine, although it does act on L-methionine. The mitochondrial form from rat liver differs in physical characteristics from the cytoplasmic form.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9030-37-9
References:
1.  Aki, K., Ogawa, K. and Ichihara, A. Transaminases of branched chain amino acids. IV. Purification and properties of two enzymes from rat liver. Biochim. Biophys. Acta 159 (1968) 276–284. [DOI] [PMID: 4968655]
2.  Ikeda, T., Konishi, Y. and Ichihara, A. Transaminase of branched chain amino acids. XI. Leucine (methionine) transaminase of rat liver mitochondria. Biochim. Biophys. Acta 445 (1976) 622–631. [DOI] [PMID: 974100]
[EC 2.6.1.6 created 1961, modified 1982]
 
 
EC 2.6.1.7     
Accepted name: kynurenine—oxoglutarate transaminase
Reaction: L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate
For diagram of reaction, click here, of tryptophan catabolism, click here and for diagram of mechanism, click here
Other name(s): kynurenine transaminase (cyclizing); kynurenine 2-oxoglutarate transaminase; kynurenine aminotransferase; L-kynurenine aminotransferase
Systematic name: L-kynurenine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. Also acts on 3-hydroxykynurenine. The product 4-(2-aminophenyl)-2,4-dioxobutanoate is converted into kynurenate by a spontaneous reaction.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9030-38-0
References:
1.  Jakoby, W.B. and Bonner, D.M. Kynurenine transaminase from Neurospora. J. Biol. Chem. 221 (1956) 689–695. [PMID: 13357462]
2.  Mason, M. Kynurenine transaminase of rat kidney: a study of coenzyme dissociation. J. Biol. Chem. 227 (1957) 61–68. [PMID: 13449053]
[EC 2.6.1.7 created 1961, modified 1983]
 
 
EC 2.6.1.8     
Accepted name: 2,5-diaminovalerate transaminase
Reaction: 2,5-diaminopentanoate + 2-oxoglutarate = 5-amino-2-oxopentanoate + L-glutamate
For diagram of reaction, click here and for mechanism, click here
Other name(s): diamino-acid transaminase; diamino acid aminotransferase
Systematic name: 2,5-diaminopentanoate:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. 2,5-Diaminoglutarate can act instead of diaminopentanoate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9030-39-1
References:
1.  Roberts, E. Studies of transamination. Arch. Biochem. Biophys. 48 (1954) 395–401. [DOI] [PMID: 13125615]
[EC 2.6.1.8 created 1961, modified 1982]
 
 
EC 2.6.1.9     
Accepted name: histidinol-phosphate transaminase
Reaction: L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Other name(s): imidazolylacetolphosphate transaminase; glutamic-imidazoleacetol phosphate transaminase; histidinol phosphate aminotransferase; imidazoleacetol phosphate transaminase; L-histidinol phosphate aminotransferase; histidine:imidazoleacetol phosphate transaminase; IAP transaminase; imidazolylacetolphosphate aminotransferase
Systematic name: L-histidinol-phosphate:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9032-98-8
References:
1.  Ames, B.N. and Horecker, B.L. The biosynthesis of histidine: imidazoleacetol phosphate transaminase. J. Biol. Chem. 220 (1956) 113–128. [PMID: 13319331]
2.  Martin, R.G. and Goldberger, R.F. Imidazolylacetolphosphate:L-glutamate aminotransferase. Purification and properties. J. Biol. Chem. 242 (1963) 1168–1174. [PMID: 5337155]
[EC 2.6.1.9 created 1961]
 
 
EC 2.6.1.10      
Deleted entry:  D-aspartate transaminase. Now included with EC 2.6.1.21, D-amino-acid transaminase
[EC 2.6.1.10 created 1961, deleted 1972]
 
 
EC 2.6.1.11     
Accepted name: acetylornithine transaminase
Reaction: N2-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
For diagram of ornithine biosynthesis, click here
Other name(s): acetylornithine δ-transaminase; ACOAT; acetylornithine 5-aminotransferase; acetylornithine aminotransferase; N-acetylornithine aminotransferase; N-acetylornithine-δ-transaminase; N2-acetylornithine 5-transaminase; N2-acetyl-L-ornithine:2-oxoglutarate aminotransferase; succinylornithine aminotransferase; 2-N-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase
Systematic name: N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase
Comments: A pyridoxal-phosphate protein. Also acts on L-ornithine and N2-succinyl-L-ornithine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9030-40-4
References:
1.  Albrecht, A. and Vogel, H.J. Acetylornithine δ-transaminase. Partial purification and repression behavior. J. Biol. Chem. 239 (1964) 1872–1876. [PMID: 14213368]
2.  Vogel, H.J. Path of ornithine synthesis in Escherichia coli. Proc. Natl. Acad. Sci. USA 39 (1953) 578–583. [DOI] [PMID: 16589307]
3.  Vander Wauven, C. and Stalon, V. Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia. J. Bacteriol. 164 (1985) 882–886. [PMID: 2865249]
4.  Voellmy, R. and Leisinger, T. Dual role for N-2-acetylornithine 5-aminotransferase from Pseudomonas aeruginosa in arginine biosynthesis and arginine catabolism. J. Bacteriol. 122 (1975) 799–809. [PMID: 238949]
[EC 2.6.1.11 created 1961, modified 2004 (EC 2.6.1.69 created 1989, incorporated 2004)]
 
 
EC 2.6.1.12     
Accepted name: alanine—oxo-acid transaminase
Reaction: L-alanine + a 2-oxo carboxylate = pyruvate + an L-amino acid
For diagram of reaction, click here and for mechanism, click here
Other name(s): L-alanine-α-keto acid aminotransferase; leucine-alanine transaminase; alanine-keto acid aminotransferase; alanine-oxo acid aminotransferase
Systematic name: L-alanine:2-oxo-acid aminotransferase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9030-41-5
References:
1.  Altenbern, R.A. and Housewright, R.D. Transaminases in smooth Brucella abortus, strain 19. J. Biol. Chem. 204 (1953) 159–167. [PMID: 13084587]
2.  Rowsell, E.V. Transaminations with pyruvate and other α-keto acids. Biochem. J. 64 (1956) 246–252. [PMID: 13363834]
3.  Sallach, H.J. Formation of serine from hydroxypyruvate and L-alanine. J. Biol. Chem. 223 (1956) 1101–1108. [PMID: 13385257]
4.  Wilson, D.G., King, K.W. and Burris, R.H. Transaminase reactions in plants. J. Biol. Chem. 208 (1954) 863–874. [PMID: 13174595]
[EC 2.6.1.12 created 1961]
 
 
EC 2.6.1.13     
Accepted name: ornithine aminotransferase
Reaction: L-ornithine + a 2-oxo carboxylate = L-glutamate 5-semialdehyde + an L-amino acid
Other name(s): ornithine δ-transaminase; L-ornithine:α-ketoglutarate δ-aminotransferase; OAT; L-ornithine 5-aminotransferase; L-ornithine aminotransferase; ornithine 5-aminotransferase; ornithine transaminase; ornithine-α-ketoglutarate aminotransferase; ornithine-2-oxoacid aminotransferase; ornithine-keto acid aminotransferase; ornithine-keto acid transaminase; ornithine-ketoglutarate aminotransferase; ornithine-oxo acid aminotransferase; ornithine:α-oxoglutarate transaminase; ornithine—oxo-acid transaminase
Systematic name: L-ornithine:2-oxo-acid aminotransferase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9030-42-6
References:
1.  Fincham, J.R.S. Ornithine transaminase in Neurospora and its relation to the biosynthesis of proline. Biochem. J. 53 (1953) 313–320. [PMID: 13032071]
2.  Katunuma, N., Matsuda, Y. and Tomino, I. Studies on ornithine-ketoacid transaminase. I. Purification and properties. J. Biochem. (Tokyo) 56 (1964) 499–503. [PMID: 14244051]
3.  Meister, A. Enzymatic transamination reactions involving arginine and ornithine. J. Biol. Chem. 206 (1954) 587–596. [PMID: 13143017]
4.  Peraino, C., Bunville, L.G. and Tahmisian, T.N. Chemical, physical, and morphological properties of ornithine aminotransferase from rat liver. J. Biol. Chem. 244 (1969) 2241–2249. [PMID: 5783831]
5.  Quastel, J.H. and Witty, R. Ornithine transaminase. Nature 167 (1951) 556. [PMID: 14826840]
6.  Strecker, H.J. Purification and properties of rat liver ornithine δ-transaminase. J. Biol. Chem. 240 (1965) 1225–1230. [PMID: 14284729]
[EC 2.6.1.13 created 1961]
 
 
EC 2.6.1.14     
Accepted name: asparagine—oxo-acid transaminase
Reaction: L-asparagine + a 2-oxo carboxylate = 2-oxosuccinamate + an amino acid
For diagram of reaction, click here and for mechanism, click here
Other name(s): asparagine-keto acid aminotransferase
Systematic name: L-asparagine:2-oxo-acid aminotransferase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9030-43-7
References:
1.  Meister, A. and Fraser, P.E. Enzymatic formation of L-asparagine by transamination. J. Biol. Chem. 210 (1954) 37–43. [PMID: 13201567]
[EC 2.6.1.14 created 1961]
 
 
EC 2.6.1.15     
Accepted name: glutamine—pyruvate transaminase
Reaction: L-glutamine + pyruvate = 2-oxoglutaramate + L-alanine
For diagram of EC 2.6.1, click here
Other name(s): glutaminase II; L-glutamine transaminase L; glutamine-oxo-acid transaminase
Systematic name: L-glutamine:pyruvate aminotransferase
Comments: A pyridoxal-phosphate protein. L-Methionine can act as donor; glyoxylate can act as acceptor.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9030-44-8
References:
1.  Cooper, A.J.L. and Meister, A. Isolation and properties of highly purified glutamine transaminase. Biochemistry 11 (1972) 661–671. [PMID: 5059882]
2.  Meister, A. Studies on the mechanism and specificity of the glutamine-α-keto acid transamination-deamidation reaction. J. Biol. Chem. 210 (1954) 17–35. [PMID: 13201566]
[EC 2.6.1.15 created 1961]
 
 
EC 2.6.1.16     
Accepted name: glutamine—fructose-6-phosphate transaminase (isomerizing)
Reaction: L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate
For diagram of the biosynthesis of UDP-N-acetylglucosamine, click here
Other name(s): hexosephosphate aminotransferase; glucosamine-6-phosphate isomerase (glutamine-forming); glutamine-fructose-6-phosphate transaminase (isomerizing); D-fructose-6-phosphate amidotransferase; glucosaminephosphate isomerase; glucosamine 6-phosphate synthase; GlcN6P synthase
Systematic name: L-glutamine:D-fructose-6-phosphate isomerase (deaminating)
Comments: Although the overall reaction is that of a transferase, the mechanism involves the formation of ketimine between fructose 6-phosphate and a 6-amino group from a lysine residue at the active site, which is subsequently displaced by ammonia (transamidination).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9030-45-9
References:
1.  Ghosh, S., Blumenthal, H.J., Davidson, E. and Roseman, S. Glucosamine metabolism. V. Enzymatic synthesis of glucosamine 6-phosphate. J. Biol. Chem. 235 (1960) 1265–1273. [PMID: 13827775]
2.  Gryder, R.M. and Pogell, B.M. Further studies on glucosamine 6-phosphate synthesis by rat liver enzymes. J. Biol. Chem. 235 (1960) 558–562. [PMID: 13829889]
3.  Leloir, L.F. and Cardini, C.E. The biosynthesis of glucosamine. Biochim. Biophys. Acta 12 (1953) 15–22. [DOI] [PMID: 13115409]
4.  Teplyakov, A., Obmolova, G., Badet-Denisot, M.A. and Badet, B. The mechanism of sugar phosphate isomerization by glucosamine 6-phosphate synthase. Protein Sci. 8 (1999) 596–602. [DOI] [PMID: 10091662]
[EC 2.6.1.16 created 1961, deleted 1972, reinstated 1984, modified 2000 (EC 5.3.1.19 created 1972, incorporated 1984)]
 
 
EC 2.6.1.17     
Accepted name: succinyldiaminopimelate transaminase
Reaction: N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate = N-succinyl-L-2-amino-6-oxoheptanedioate + L-glutamate
Other name(s): succinyldiaminopimelate aminotransferase; N-succinyl-L-diaminopimelic glutamic transaminase
Systematic name: N-succinyl-L-2,6-diaminoheptanedioate:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9030-46-0
References:
1.  Peterkofsky, B. and Gilvarg, C. N-Succinyl-L-diaminopimelic-glutamic transaminase. J. Biol. Chem. 236 (1961) 1432–1438. [PMID: 13734750]
[EC 2.6.1.17 created 1965]
 
 
EC 2.6.1.18     
Accepted name: β-alanine—pyruvate transaminase
Reaction: L-alanine + 3-oxopropanoate = pyruvate + β-alanine
Other name(s): β-alanine-pyruvate aminotransferase; β-alanine-α-alanine transaminase
Systematic name: L-alanine:3-oxopropanoate aminotransferase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 61461-61-8
References:
1.  Hayaishi, O., Nishizuka, Y., Tatibana, M., Takeshita, M. and Kuno, S. Enzymatic studies on the metabolism of β-alanine. J. Biol. Chem. 236 (1961) 781–790. [PMID: 13712439]
2.  Stinson, R.A. and Spencer, M.S. β-Aalanine aminotransferase(s) from a plant source. Biochem. Biophys. Res. Commun. 34 (1969) 120–127. [DOI] [PMID: 5762452]
[EC 2.6.1.18 created 1965]
 
 
EC 2.6.1.19     
Accepted name: 4-aminobutyrate—2-oxoglutarate transaminase
Reaction: 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate
For diagram of arginine catabolism, click here
Glossary: 4-aminobutanoate = γ-aminobutyrate = GABA
Other name(s): β-alanine-oxoglutarate transaminase; aminobutyrate aminotransferase (ambiguous); β-alanine aminotransferase; β-alanine-oxoglutarate aminotransferase; γ-aminobutyrate aminotransaminase (ambiguous); γ-aminobutyrate transaminase (ambiguous); γ-aminobutyrate-α-ketoglutarate aminotransferase; γ-aminobutyrate-α-ketoglutarate transaminase; γ-aminobutyrate:α-oxoglutarate aminotransferase; γ-aminobutyric acid aminotransferase (ambiguous); γ-aminobutyric acid transaminase (ambiguous); γ-aminobutyric acid-α-ketoglutarate transaminase; γ-aminobutyric acid-α-ketoglutaric acid aminotransferase; γ-aminobutyric acid-2-oxoglutarate transaminase; γ-aminobutyric transaminase (ambiguous); 4-aminobutyrate aminotransferase (ambiguous); 4-aminobutyrate-2-ketoglutarate aminotransferase; 4-aminobutyrate-2-oxoglutarate aminotransferase; 4-aminobutyrate-2-oxoglutarate transaminase; 4-aminobutyric acid 2-ketoglutaric acid aminotransferase; 4-aminobutyric acid aminotransferase (ambiguous); aminobutyrate transaminase (ambiguous); GABA aminotransferase (ambiguous); GABA transaminase (ambiguous); GABA transferase; GABA-α-ketoglutarate aminotransferase; GABA-α-ketoglutarate transaminase; GABA-α-ketoglutaric acid transaminase; GABA-α-oxoglutarate aminotransferase; GABA-2-oxoglutarate aminotransferase; GABA-2-oxoglutarate transaminase; GABA-oxoglutarate aminotransferase; GABA-oxoglutarate transaminase; glutamate-succinic semialdehyde transaminase; GabT
Systematic name: 4-aminobutanoate:2-oxoglutarate aminotransferase
Comments: Requires pyridoxal phosphate. Some preparations also act on β-alanine, 5-aminopentanoate and (R,S)-3-amino-2-methylpropanoate.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9037-67-6
References:
1.  Scott, E.M. and Jakoby, W.B. Soluble γ-aminobutyric-glutamic transaminase from Pseudomonas fluorescens. J. Biol. Chem. 234 (1959) 932–936. [PMID: 13654294]
2.  Aurich, H. Über die β-Alanin-α-Ketoglutarat-Transaminase aus Neurospora crassa. Hoppe-Seyler's Z. Physiol. Chem. 326 (1961) 25–33. [PMID: 13863304]
3.  Schausboe, A., Wu, J.-Y. and Roberts, E. Purification and characterization of the 4-aminobutyrate-2-ketoglutarate transaminase from mouse brain. Biochemistry 12 (1973) 2868–2873. [PMID: 4719123]
4.  Bartsch, K., von Johnn-Marteville, A. and Schulz, A. Molecular analysis of two genes of the Escherichia coli gab cluster: nucleotide sequence of the glutamate:succinic semialdehyde transaminase gene (gabT) and characterization of the succinic semialdehyde dehydrogenase gene (gabD). J. Bacteriol. 172 (1990) 7035–7042. [DOI] [PMID: 2254272]
[EC 2.6.1.19 created 1965, modified 1982, modified 2012]
 
 
EC 2.6.1.20      
Deleted entry:  tyrosine—pyruvate transaminase
[EC 2.6.1.20 created 1965, deleted 1972]
 
 
EC 2.6.1.21     
Accepted name: D-amino-acid transaminase
Reaction: D-alanine + 2-oxoglutarate = pyruvate + D-glutamate
Other name(s): D-aspartate transaminase; D-alanine aminotransferase; D-aspartic aminotransferase; D-alanine-D-glutamate transaminase; D-alanine transaminase; D-amino acid aminotransferase
Systematic name: D-alanine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. The enzyme from thermophilic Bacillus species acts on many D-amino acids with D-alanine and D-2-aminobutyrate as the best amino donors. It can similarly use any of several 2-oxo acids as amino acceptor, with 2-oxoglutarate and 2-oxobutyrate among the best. The enzyme from some other sources has a broader specificity [6].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 37277-85-3
References:
1.  Thorne, C.B., Gómez, C.G. and Housewright, R.D. Transamination of D-amino acids by Bacillus subtilis. J. Bacteriol. 69 (1955) 357–362. [PMID: 14367287]
2.  Thorne, C.B. and Molnar, D.M. D-Amino acid transamination in Bacillus anthracis. J. Bacteriol. 70 (1955) 420–426. [PMID: 13263311]
3.  Martinez-Carrion, M. and Jenkins, W.T. D-Alanine-D-glutamate transaminase. I. Purification and characterization. J. Biol. Chem. 240 (1965) 3538–3546. [PMID: 4953710]
4.  Ozawa, T., Fukuda, M. and Sasaoka, K. Occurrence of D-amino acid aminotransferase in pea seedlings. Biochem. Biophys. Res. Commun. 52 (1973) 998–1002. [DOI] [PMID: 4710577]
5.  Yonaha, K., Misono, H., Yamamoto, T. and Soda, K. D-Amino acid aminotransferase of Bacillus sphaericus. Enzymologic and spectrometric properties. J. Biol. Chem. 250 (1975) 6983–6989. [PMID: 1158891]
6.  Tanizawa, K., Masu, Y., Asano, S., Tanaka, H. and Soda, K. Thermostable D-amino acid aminotransferase from a thermophilic Bacillus species. Purification, characterization, and active site sequence determination. J. Biol. Chem. 264 (1989) 2445–2449. [PMID: 2914916]
7.  Fotheringham, I.G., Bledig, S.A. and Taylor, P.P. Characterization of the genes encoding D-amino acid transaminase and glutamate racemase, two D-glutamate biosynthetic enzymes of Bacillus sphaericus ATCC 10208. J. Bacteriol. 180 (1998) 4319–4323. [PMID: 9696787]
8.  van Ophem, P.W., Erickson, S.D., Martinez del Pozo, A., Haller, I., Chait, B.T., Yoshimura, T., Soda, K., Ringe, D., Petsko, G. and Manning, J.M. Substrate inhibition of D-amino acid transaminase and protection by salts and by reduced nicotinamide adenine dinucleotide: isolation and initial characterization of a pyridoxo intermediate related to inactivation. Biochemistry 37 (1998) 2879–2888. [DOI] [PMID: 9485439]
9.  Sugio, S., Petsko, G.A., Manning, J.M., Soda, K. and Ringe, D. Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity. Biochemistry 34 (1995) 9661–9669. [PMID: 7626635]
[EC 2.6.1.21 created 1972 (EC 2.6.1.10 created 1961, incorporated 1972), modified 2005]
 
 
EC 2.6.1.22     
Accepted name: (S)-3-amino-2-methylpropionate transaminase
Reaction: (S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate
For diagram of reaction, click here
Other name(s): L-3-aminoisobutyrate transaminase; β-aminobutyric transaminase; L-3-aminoisobutyric aminotransferase; β-aminoisobutyrate-α-ketoglutarate transaminase
Systematic name: (S)-3-amino-2-methylpropanoate:2-oxoglutarate aminotransferase
Comments: Also acts on β-alanine and other ω-amino acids having carbon chains between 2 and 5. The two enantiomers of the 2-methyl-3-oxopropanoate formed by the enzyme interconvert by enolization, so that this enzyme, together with EC 2.6.1.40, (R)-3-amino-2-methylpropionate—pyruvate transaminase, provide a route for interconversion of the enantiomers of 3-amino-2-methylpropanoate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9031-95-2
References:
1.  Kakimoto, Y., Kanazawa, A., Taniguchi, K. and Sano, I. β-Aminoisobutyrate-α-ketoglutarate transaminase in relation to β-aminoisobutyric aciduria. Biochim. Biophys. Acta 156 (1968) 374–380. [DOI] [PMID: 5641913]
2.  Tamaki, N., Sakata, S.F. and Matsuda, K. Purification, properties, and sequencing of aminoisobutyrate aminotransferases from rat liver. Methods Enzymol. 324 (2000) 376–389. [DOI] [PMID: 10989446]
[EC 2.6.1.22 created 1972, modified 1982, modified 2004]
 
 
EC 2.6.1.23     
Accepted name: 4-hydroxyglutamate transaminase
Reaction: 4-hydroxy-L-glutamate + 2-oxoglutarate = 4-hydroxy-2-oxoglutarate + L-glutamate
For diagram of reaction, click here and for mechanism, click here
Other name(s): 4-hydroxyglutamate aminotransferase
Systematic name: 4-hydroxy-L-glutamate:2-oxoglutarate aminotransferase
Comments: Oxaloacetate can replace 2-oxoglutarate. This enzyme may be identical with EC 2.6.1.1 aspartate transaminase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-86-4
References:
1.  Goldstone, A. and Adams, E. Metabolism of γ-hydroxyglutamic acid. I. Conversion to α-hydroxy-γ-ketoglutarate by purified glutamic-aspartic transaminase to rat liver. J. Biol. Chem. 237 (1962) 3476–3485. [PMID: 13948827]
2.  Kuratomi, K., Fukunaga, K. and Kobayashi, Y. The metabolism of γ-hydroxyglutamate in rat liver. II. A transaminase concerned in γ-hydroxyglutamate metabolism. Biochim. Biophys. Acta 78 (1963) 629–636. [DOI] [PMID: 14089443]
[EC 2.6.1.23 created 1972, modified 1982]
 
 
EC 2.6.1.24     
Accepted name: diiodotyrosine transaminase
Reaction: 3,5-diiodo-L-tyrosine + 2-oxoglutarate = 4-hydroxy-3,5-diiodophenylpyruvate + L-glutamate
For diagram of reaction, click here and for reaction mechanism, click here
Other name(s): diiodotyrosine aminotransferase; halogenated tyrosine aminotransferase; halogenated tyrosine transaminase
Systematic name: 3,5-diiodo-L-tyrosine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. Also acts on 3,5-dichloro-, 3,5-dibromo- and 3-iodo-L-tyrosine, thyroxine and triiodothyronine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9033-18-5
References:
1.  Nakano, M. Purification and properties of halogenated tyrosine and thyroid hormone transaminase from rat kidney mitochondria. J. Biol. Chem. 242 (1967) 73–81. [PMID: 4381052]
2.  Nakano, M. and Danowski, T.S. Thyroid-hormone transaminase and oxidase in rat-kidney mitochondria. Biochim. Biophys. Acta 85 (1964) 18–28. [PMID: 14159298]
[EC 2.6.1.24 created 1972 (EC 2.6.1.25 created 1972, incorporated 1972)]
 
 
EC 2.6.1.25      
Deleted entry:  thyroxine transaminase. Now included with EC 2.6.1.24 diiodotyrosine transaminase
[EC 2.6.1.25 created 1972, deleted 1984]
 
 
EC 2.6.1.26     
Accepted name: thyroid-hormone transaminase
Reaction: L-3,5,3′-triiodothyronine + 2-oxoglutarate = 3-[4-(4-hydroxy-3-iodophenoxy)-3,5-diiodophenyl]-2-oxopropanoate + L-glutamate
For diagram of reaction, click here and for mechanism, click here
Other name(s): 3,5-dinitrotyrosine transaminase; thyroid hormone aminotransferase
Systematic name: L-3,5,3′-triiodothyronine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. Acts on monoiodotyrosine, diiodotyrosine, triiodothyronine, thyroxine and dinitrotyrosine (unlike EC 2.6.1.24 diiodotyrosine transaminase, which does not act on dinitrotyrosine). Pyruvate or oxaloacetate can act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 51004-29-6
References:
1.  Soffer, R.L., Hechtman, P. and Savage, M. L-Triiodothyronine aminotransferase. J. Biol. Chem. 248 (1973) 1224–1230. [PMID: 4686924]
[EC 2.6.1.26 created 1972]
 
 
EC 2.6.1.27     
Accepted name: tryptophan transaminase
Reaction: L-tryptophan + 2-oxoglutarate = (indol-3-yl)pyruvate + L-glutamate
For diagram of reaction, click here and for mechanism, click here
Other name(s): L-phenylalanine-2-oxoglutarate aminotransferase; tryptophan aminotransferase; 5-hydroxytryptophan-ketoglutaric transaminase; hydroxytryptophan aminotransferase; L-tryptophan aminotransferase; L-tryptophan transaminase
Systematic name: L-tryptophan:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. Also acts on 5-hydroxytryptophan and, to a lesser extent, on the phenyl amino acids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9022-98-4
References:
1.  George, H. and Gabay, S. Brain aromatic aminotransferase. I. Purification and some properties of pig brain L-phenylalanine-2-oxoglutarate aminotransferase. Biochim. Biophys. Acta 167 (1968) 555–566. [DOI] [PMID: 5722279]
2.  O'Neil, S.R. and DeMoss, R.D. Tryptophan transaminase from Clostridium sporogenes. Arch. Biochem. Biophys. 127 (1968) 361–368. [DOI] [PMID: 5697992]
3.  Tangen, O., Fonnum, F. and Haavaldsen, R. Separation and purification of aromatic amino acid transaminases from rat brain. Biochim. Biophys. Acta 96 (1965) 82–90. [DOI] [PMID: 14285270]
[EC 2.6.1.27 created 1972]
 
 
EC 2.6.1.28     
Accepted name: tryptophan—phenylpyruvate transaminase
Reaction: L-tryptophan + phenylpyruvate = (indol-3-yl)pyruvate + L-phenylalanine
For diagram of reaction, click here and for mechanism, click here
Other name(s): L-tryptophan-α-ketoisocaproate aminotransferase
Systematic name: L-tryptophan:phenylpyruvate aminotransferase
Comments: Valine, leucine and isoleucine can replace tryptophan as amino donor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-87-5
References:
1.  Koide, Y., Honma, M. and Shimomura, T. L-Tryptophan-α-ketoisocaproate aminotransferase from Pseudomonas sp. Agric. Biol. Chem. 44 (1980) 2013–2019.
2.  Sukanya, N.K. and Vaidyanathan, C.S. Aminotransferases of Agrobacterium tumefaciens. Transamination between tryptophan and phenylpyruvate. Biochem. J. 92 (1964) 594–598. [PMID: 5837443]
[EC 2.6.1.28 created 1972]
 
 
EC 2.6.1.29     
Accepted name: diamine transaminase
Reaction: an α,ω-diamine + 2-oxoglutarate = an ω-aminoaldehyde + L-glutamate
Other name(s): amine transaminase; amine-ketoacid transaminase; diamine aminotransferase; diamine-ketoglutaric transaminase
Systematic name: diamine:2-oxoglutarate aminotransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9031-83-8
References:
1.  Kim, K. Purification and properties of a diamine α-ketoglutarate transaminase from Escherichia coli. J. Biol. Chem. 239 (1964) 783–786. [PMID: 14154456]
[EC 2.6.1.29 created 1972]
 
 
EC 2.6.1.30     
Accepted name: pyridoxamine—pyruvate transaminase
Reaction: pyridoxamine + pyruvate = pyridoxal + L-alanine
Other name(s): pyridoxamine-pyruvic transaminase
Systematic name: pyridoxamine:pyruvate aminotransferase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 9023-38-5
References:
1.  Wada, H. and Snell, E.E. Enzymatic transamination of pyridoxamine. II. Crystalline pyridoxamine-pyruvate transaminase. J. Biol. Chem. 237 (1962) 133–137. [PMID: 14004227]
[EC 2.6.1.30 created 1972]
 
 
EC 2.6.1.31     
Accepted name: pyridoxamine—oxaloacetate transaminase
Reaction: pyridoxamine + oxaloacetate = pyridoxal + L-aspartate
Systematic name: pyridoxamine:oxaloacetate aminotransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-88-6
References:
1.  Wada, H. and Snell, E.E. Enzymatic transamination of pyridoxamine. I. With oxaloacetate and α-ketoglutarate. J. Biol. Chem. 237 (1962) 127–132. [PMID: 14004226]
2.  Wu, H.L.C. and Mason, M. Pyridoxamine-oxaloacetic transaminase of rat kidney. J. Biol. Chem. 239 (1964) 1492–1497. [PMID: 14189882]
[EC 2.6.1.31 created 1972]
 
 
EC 2.6.1.32     
Accepted name: valine—3-methyl-2-oxovalerate transaminase
Reaction: L-valine + (S)-3-methyl-2-oxopentanoate = 3-methyl-2-oxobutanoate + L-isoleucine
For diagram of EC 2.6.1, click here
Other name(s): valine—isoleucine transaminase; valine-3-methyl-2-oxovalerate aminotransferase; alanine-valine transaminase; valine-2-keto-methylvalerate aminotransferase; valine-isoleucine aminotransferase
Systematic name: L-valine:(S)-3-methyl-2-oxopentanoate aminotransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9023-14-7
References:
1.  Kagan, Z.S., Dronov, A.S. and Kretovich, V.L. [Some properties of valine-isoleucine- and valine-glutamate-aminotransferases of pea sprouts.] Dokl. Akad. Nauk S.S.S.R. 179 (1968) 1236–1239. (in Russian)
[EC 2.6.1.32 created 1972, modified 1976]
 
 
EC 2.6.1.33     
Accepted name: dTDP-4-amino-4,6-dideoxy-D-glucose transaminase
Reaction: dTDP-4-amino-4,6-dideoxy-α-D-glucose + 2-oxoglutarate = dTDP-4-dehydro-6-deoxy-α-D-glucose + L-glutamate
For diagram of dTDP-D-desosamine biosynthesis, click here
Other name(s): thymidine diphospho-4-amino-4,6-dideoxyglucose aminotransferase; thymidine diphospho-4-amino-6-deoxyglucose aminotransferase; thymidine diphospho-4-keto-6-deoxy-D-glucose transaminase; thymidine diphospho-4-keto-6-deoxy-D-glucose-glutamic transaminase; TDP-4-keto-6-deoxy-D-glucose transaminase; VioA; dTDP-4-amino-4,6-dideoxy-D-glucose:2-oxoglutarate aminotransferase
Systematic name: dTDP-4-amino-4,6-dideoxy-α-D-glucose:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9023-19-2
References:
1.  Matsuhashi, M. and Strominger, J.L. Thymidine diphosphate 4-acetamido-2,6-dideoxyhexoses. 3. Purification and properties of thymidine diphosphate 4-keto-6-deoxy-D-glucose transaminase from Escherichia coli strain B. J. Biol. Chem. 241 (1966) 4738–4744. [PMID: 5332731]
2.  Wang, Y., Xu, Y., Perepelov, A.V., Qi, Y., Knirel, Y.A., Wang, L. and Feng, L. Biochemical characterization of dTDP-D-Qui4N and dTDP-D-Qui4NAc biosynthetic pathways in Shigella dysenteriae type 7 and Escherichia coli O7. J. Bacteriol. 189 (2007) 8626–8635. [DOI] [PMID: 17905981]
[EC 2.6.1.33 created 1972]
 
 
EC 2.6.1.34     
Accepted name: UDP-N-acetylbacillosamine transaminase
Reaction: UDP-N-acetylbacillosamine + 2-oxoglutarate = UDP-2-acetamido-2,6-dideoxy-α-D-xylo-hex-4-ulose + L-glutamate
For diagram of legionaminic acid biosynthesis, click here
Glossary: UDP-N-acetylbacillosamine = UDP-2-acetamido-4-amino-2,4,6-trideoxy-α-D-glucose = UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine
Other name(s): uridine diphospho-4-amino-2-acetamido-2,4,6-trideoxyglucose aminotransferase; UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine transaminase; UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose transaminase; pglE (gene name); UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose:2-oxoglutarate aminotransferase
Systematic name: UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. The enzyme is involved in biosynthesis of UDP-N,N′-diacetylbacillosamine, an intermediate in protein glycosylation pathways in several bacterial species, including N-linked glycosylation of certain L-asparagine residues in Campylobacter species [2-4] and O-linked glycosylation of certain L-serine residues in Neisseria species [5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-89-7
References:
1.  Distler, J., Kaufman, B. and Roseman, S. Enzymic synthesis of a diamino sugar nucleotide by extracts of type XIV Diplococcus pneumoniae. Arch. Biochem. Biophys. 116 (1966) 466–478. [DOI] [PMID: 4381351]
2.  Olivier, N.B., Chen, M.M., Behr, J.R. and Imperiali, B. In vitro biosynthesis of UDP-N,N′-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system. Biochemistry 45 (2006) 13659–13669. [DOI] [PMID: 17087520]
3.  Schoenhofen, I.C., McNally, D.J., Vinogradov, E., Whitfield, D., Young, N.M., Dick, S., Wakarchuk, W.W., Brisson, J.R. and Logan, S.M. Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways. J. Biol. Chem. 281 (2006) 723–732. [DOI] [PMID: 16286454]
4.  Rangarajan, E.S., Ruane, K.M., Sulea, T., Watson, D.C., Proteau, A., Leclerc, S., Cygler, M., Matte, A. and Young, N.M. Structure and active site residues of PglD, an N-acetyltransferase from the bacillosamine synthetic pathway required for N-glycan synthesis in Campylobacter jejuni. Biochemistry 47 (2008) 1827–1836. [DOI] [PMID: 18198901]
5.  Hartley, M.D., Morrison, M.J., Aas, F.E., Borud, B., Koomey, M. and Imperiali, B. Biochemical characterization of the O-linked glycosylation pathway in Neisseria gonorrhoeae responsible for biosynthesis of protein glycans containing N,N′-diacetylbacillosamine. Biochemistry 50 (2011) 4936–4948. [DOI] [PMID: 21542610]
[EC 2.6.1.34 created 1972, modified 2013]
 
 
EC 2.6.1.35     
Accepted name: glycine—oxaloacetate transaminase
Reaction: glycine + oxaloacetate = glyoxylate + L-aspartate
For diagram of reaction, click here and for mechanism, click here
Other name(s): glycine-oxalacetate aminotransferase
Systematic name: glycine:oxaloacetate aminotransferase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 37277-90-0
References:
1.  Gibbs, R.G. and Morris, J.G. Formation of glycine from glyoxylate in Micrococcus denitrificans. Biochem. J. 99 (1966) 27.
[EC 2.6.1.35 created 1972]
 
 
EC 2.6.1.36     
Accepted name: L-lysine 6-transaminase
Reaction: L-lysine + 2-oxoglutarate = (S)-2-amino-6-oxohexanoate + L-glutamate
Glossary: (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine
L-1-piperideine 6-carboxylate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate = (S)-1,6-didehydropiperidine-2-carboxylate
Other name(s): lysine 6-aminotransferase; lysine ε-aminotransferase; lysine ε-transaminase; lysine:2-ketoglutarate 6-aminotransferase; L-lysine-α-ketoglutarate aminotransferase; L-lysine-α-ketoglutarate 6-aminotransferase
Systematic name: L-lysine:2-oxoglutarate 6-aminotransferase
Comments: A pyridoxal-phosphate protein. The product (L-allysine) is converted into the intramolecularly dehydrated form, (S)-2,3,4,5-tetrahydropyridine-2-carboxylate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9054-68-6
References:
1.  Soda, K., Misono, H. and Yamamoto, T. L-Lysine:α-ketoglutarate aminotransferase. I. Identification of a product, δ-1-piperideine-6-carboxylic acid. Biochemistry 7 (1968) 4102–4109. [PMID: 5722275]
2.  Soda, K. and Misono, H. L-Lysine: α-ketoglutarate aminotransferase. II. Purification, crystallization, and properties. Biochemistry 7 (1968) 4110–4119. [PMID: 5722276]
[EC 2.6.1.36 created 1972, modified 2011]
 
 
EC 2.6.1.37     
Accepted name: 2-aminoethylphosphonate—pyruvate transaminase
Reaction: (2-aminoethyl)phosphonate + pyruvate = 2-phosphonoacetaldehyde + L-alanine
Other name(s): (2-aminoethyl)phosphonate transaminase; (2-aminoethyl)phosphonate aminotransferase; (2-aminoethyl)phosphonic acid aminotransferase; 2-aminoethylphosphonate-pyruvate aminotransferase; 2-aminoethylphosphonate aminotransferase; 2-aminoethylphosphonate transaminase; AEP transaminase; AEPT
Systematic name: (2-aminoethyl)phosphonate:pyruvate aminotransferase
Comments: A pyridoxal-phosphate protein. 2-Aminoethylarsonate can replace 2-aminoethylphosphonate as a substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37277-91-1
References:
1.  La Nauze, J.M. and Rosenberg, H. The identification of 2-phosphonoacetaldehyde as an intermediate in the degradation of 2-aminoethylphosphonate by Bacillus cereus. Biochim. Biophys. Acta 165 (1968) 438–447. [DOI] [PMID: 4982500]
2.  Dumora, C., Lacoste, A.-M. and Cassaigne, A. Purification and properties of 2-aminoethylphosphonate:pyruvate aminotransferase from Pseudomonas aeruginosa. Eur. J. Biochem. 133 (1983) 119–125. [DOI] [PMID: 6406228]
3.  Lacoste, A.-M., Dumora, C., Balas, L., Hammerschmidt, F. and Vercauteren, J. Stereochemistry of the reaction catalysed by 2-aminoethylphosphonate aminotransferase. A 1H-NMR study. Eur. J. Biochem. 215 (1993) 841–844. [DOI] [PMID: 8394813]
4.  Lacoste, A.-M., Dumora, C., Ali, B.R.S., Neuzil, E. and Dixon, H.B.F. Utilization of 2-aminoethylarsonic acid in Pseudomonas aeruginosa. J. Gen. Microbiol. 138 (1992) 1283–1287. [DOI] [PMID: 1527499]
[EC 2.6.1.37 created 1972, modified 1982, modified 2001]
 
 
EC 2.6.1.38     
Accepted name: histidine transaminase
Reaction: L-histidine + 2-oxoglutarate = (imidazol-5-yl)pyruvate + L-glutamate
For diagram of reaction, click here and for mechanism, click here
Other name(s): histidine aminotransferase; histidine-2-oxoglutarate aminotransferase
Systematic name: L-histidine:2-oxoglutarate aminotransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-92-2
References:
1.  Coote, J.G. and Hassall, H. 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. Biochem. J. 111 (1969) 237–239. [PMID: 4303364]
2.  Wickremasinghe, R., Hedegaard, J. and Roche, J. Dégradation de la L-histidine chez Escherichia coli B: formation de l’acide imidazolepyruvique par une histidine-transaminase. C.R. Soc. Biol. 161 (1967) 1891–1896.
[EC 2.6.1.38 created 1972]
 
 
EC 2.6.1.39     
Accepted name: 2-aminoadipate transaminase
Reaction: L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate
Other name(s): α-aminoadipate aminotransferase; 2-aminoadipate aminotransferase; 2-aminoadipic aminotransferase; glutamic-ketoadipic transaminase; glutamate-α-ketoadipate transaminase
Systematic name: L-2-aminoadipate:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9033-00-5
References:
1.  Matsuda, M. and Ogur, M. Separation and specificity of the yeast glutamate-α-ketoadipate transaminase. J. Biol. Chem. 244 (1969) 3352–3358. [PMID: 5792664]
[EC 2.6.1.39 created 1972]
 
 
EC 2.6.1.40     
Accepted name: (R)-3-amino-2-methylpropionate—pyruvate transaminase
Reaction: (R)-3-amino-2-methylpropanoate + pyruvate = 2-methyl-3-oxopropanoate + L-alanine
For diagram of reaction, click here
Other name(s): D-3-aminoisobutyrate—pyruvate transaminase; β-aminoisobutyrate-pyruvate aminotransferase; D-3-aminoisobutyrate-pyruvate aminotransferase; D-3-aminoisobutyrate-pyruvate transaminase; (R)-3-amino-2-methylpropionate transaminase; D-β-aminoisobutyrate:pyruvate aminotransferase
Systematic name: (R)-3-amino-2-methylpropanoate:pyruvate aminotransferase
Comments: The two enantiomers of the 2-methyl-3-oxopropanoate formed by the enzyme interconvert by enolization, so that this enzyme, together with EC 2.6.1.22, (S)-3-amino-2-methylpropionate transaminase, provide a route for interconversion of the enantiomers of 3-amino-2-methylpropanoate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37279-00-8
References:
1.  Kakimoto, Y., Taniguchi, K. and Sano, I. D-β-Aminoisobutyrate:pyruvate aminotransferase in mammalian liver and excretion of β-aminoisobutyrate by man. J. Biol. Chem. 244 (1969) 335–340. [PMID: 5773299]
2.  Tamaki, N., Sakata, S.F. and Matsuda, K. Purification, properties, and sequencing of aminoisobutyrate aminotransferases from rat liver. Methods Enzymol. 324 (2000) 376–389. [DOI] [PMID: 10989446]
[EC 2.6.1.40 created 1972 (EC 2.6.1.61 created 1982, incorporated 2004) modified 2004]
 
 
EC 2.6.1.41     
Accepted name: D-methionine—pyruvate transaminase
Reaction: D-methionine + pyruvate = 4-(methylsulfanyl)-2-oxobutanoate + L-alanine
Other name(s): D-methionine transaminase; D-methionine aminotransferase
Systematic name: D-methionine:pyruvate aminotransferase
Comments: Oxaloacetate can replace pyruvate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-93-3
References:
1.  Mapson, L.W., March, J.F. and Wardale, D.A. Biosynthesis of ethylene. 4-Methylmercapto-2-oxobutyric acid: an intermediate in the formation from methionine. Biochem. J. 115 (1969) 653–661. [PMID: 5357015]
[EC 2.6.1.41 created 1972, modified 1982]
 
 
EC 2.6.1.42     
Accepted name: branched-chain-amino-acid transaminase
Reaction: L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate
For diagram of reaction, click here, of leucine biosynthesis click here, of isoleucine and valine biosynthesis, click here, of coenzyme-A biosynthesis, click here and for diagram of mechanism, click here
Other name(s): transaminase B; branched-chain amino acid aminotransferase; branched-chain amino acid-glutamate transaminase; branched-chain aminotransferase; L-branched chain amino acid aminotransferase; glutamate-branched-chain amino acid transaminase
Systematic name: branched-chain-amino-acid:2-oxoglutarate aminotransferase
Comments: Also acts on L-isoleucine and L-valine, and thereby differs from EC 2.6.1.6, leucine transaminase, which does not. It also differs from EC 2.6.1.66, valine—pyruvate transaminase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9054-65-3
References:
1.  Aki, K., Ogawa, K. and Ichihara, A. Transaminases of branched chain amino acids. IV. Purification and properties of two enzymes from rat liver. Biochim. Biophys. Acta 159 (1968) 276–284. [DOI] [PMID: 4968655]
2.  Aki, K., Yokojima, A. and Ichihara, A. Transaminase of branched chain amino acids. VI. Purification and properties of the hog brain enzyme. J. Biochem. (Tokyo) 65 (1969) 539–544. [PMID: 4979711]
3.  Ichihara, A. and Koyama, E. Transaminase of branched chain amino acids. I. Branched chain amino acids-α-ketoglutarate transaminase. J. Biochem. (Tokyo) 59 (1966) 160–169. [PMID: 5943594]
4.  Taylor, R.T. and Jenkins, W.T. Leucine aminotransferase. II. Purification and characterization. J. Biol. Chem. 241 (1966) 4396–4405. [PMID: 5922965]
5.  Rudman, D. and Meister, A. Transamination in Escherichia coli. J. Biol. Chem. 200 (1953) 591–604. [PMID: 13034817]
[EC 2.6.1.42 created 1972]
 
 
EC 2.6.1.43     
Accepted name: aminolevulinate transaminase
Reaction: 5-aminolevulinate + pyruvate = 4,5-dioxopentanoate + L-alanine
Other name(s): aminolevulinate aminotransferase, γ,δ-dioxovalerate aminotransferase; γ,δ-dioxovaleric acid transaminase; 4,5-dioxovalerate aminotransferase; 4,5-dioxovaleric acid transaminase; 4,5-dioxovaleric transaminase; 5-aminolevulinic acid transaminase; alanine-γ,δ-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; 4,5-dioxovaleric acid aminotransferase
Systematic name: 5-aminolevulinate:pyruvate aminotransferase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9012-46-8
References:
1.  Gibson, K.D., Matthew, M. and Neuberger, A. Biosynthesis of porphyrins and chlorophylls. Nature 192 (1961) 204–208. [PMID: 13898421]
2.  Neuberger, A. and Turner, J.M. -Dioxovalerate aminotransferase activity in Rhodopseudomonas spheroides. Biochim. Biophys. Acta 67 (1963) 342–345. [PMID: 13938132]
[EC 2.6.1.43 created 1972]
 
 
EC 2.6.1.44     
Accepted name: alanine—glyoxylate transaminase
Reaction: L-alanine + glyoxylate = pyruvate + glycine
For diagram of reaction, click here and for mechanism, click here
Other name(s): AGT; alanine-glyoxylate aminotransferase; alanine-glyoxylic aminotransferase; L-alanine-glycine transaminase
Systematic name: L-alanine:glyoxylate aminotransferase
Comments: A pyridoxal-phosphate protein. With one component of the animal enzyme, 2-oxobutanoate can replace glyoxylate. A second component also catalyses the reaction of EC 2.6.1.51 serine—pyruvate transaminase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9015-67-2
References:
1.  Noguchi, T., Okuno, E., Takada, Y., Minatogawa, Y., Okai, K. and Kido, R. Characteristics of hepatic alanine-glyoxylate aminotransferase in different mammalian species. Biochem. J. 169 (1978) 113–122. [PMID: 629740]
2.  Okuno, E., Minatogawa, Y. and Kido, R. Co-purification of alanine-glyoxylate aminotransferase with 2-aminobutyrate aminotransferase in rat kidney. Biochim. Biophys. Acta 715 (1982) 97–104. [DOI] [PMID: 6803844]
3.  Thompson, J.S. and Richardson, K.E. Isolation and characterization of an L-alanine: glyoxylate aminotransferase from human liver. J. Biol. Chem. 242 (1967) 3614–3619. [PMID: 6038488]
[EC 2.6.1.44 created 1972, modified 1982]
 
 
EC 2.6.1.45     
Accepted name: serine—glyoxylate transaminase
Reaction: L-serine + glyoxylate = 3-hydroxypyruvate + glycine
For diagram of reaction, click here and for mechanism, click here
Systematic name: L-serine:glyoxylate aminotransferase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37259-57-7
References:
1.  Ireland, R.J. and Joy, K.W. Purification and properties of an asparagine aminotransferase from Pisum sativum leaves. Arch. Biochem. Biophys. 223 (1983) 291–296. [DOI] [PMID: 6407397]
2.  King, J. and Waygood, E.R. Glyoxylate aminotranferases from wheat leaves. Can. J. Biochem. 46 (1968) 771–779. [PMID: 5672858]
3.  Smith, I.K. Purification and characterization of serine:glyoxylate aminotransferase from kidney bean (Phaseolus vulgaris). Biochim. Biophys. Acta 321 (1973) 156–164. [DOI] [PMID: 4750762]
[EC 2.6.1.45 created 1972]
 
 
EC 2.6.1.46     
Accepted name: diaminobutyrate—pyruvate transaminase
Reaction: L-2,4-diaminobutanoate + pyruvate = L-aspartate 4-semialdehyde + L-alanine
Other name(s): diaminobutyrate-pyruvate aminotransferase; L-diaminobutyric acid transaminase
Systematic name: L-2,4-diaminobutanoate:pyruvate aminotransferase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-95-5
References:
1.  Rao, D.R., Hariharan, K. and Vijayalakshmi, K.R. A study of the metabolism of L-αγ-diaminobutyric acid in a Xanthomonas species. Biochem. J. 114 (1969) 107–115. [PMID: 4390206]
[EC 2.6.1.46 created 1972]
 
 
EC 2.6.1.47     
Accepted name: alanine—oxomalonate transaminase
Reaction: L-alanine + oxomalonate = pyruvate + aminomalonate
For diagram of reaction, click here and for mechanism, click here
Other name(s): alanine-oxomalonate aminotransferase; L-alanine-ketomalonate transaminase; alanine-ketomalonate (mesoxalate) transaminase
Systematic name: L-alanine:oxomalonate aminotransferase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-96-6
References:
1.  Nagayama, H., Muramatsu, M. and Shimura, K. Enzymatic formation of aminomalonic acid from ketomalonic acid. Nature 181 (1958) 417–418. [PMID: 13504217]
[EC 2.6.1.47 created 1972]
 
 
EC 2.6.1.48     
Accepted name: 5-aminovalerate transaminase
Reaction: 5-aminopentanoate + 2-oxoglutarate = 5-oxopentanoate + L-glutamate
Other name(s): 5-aminovalerate aminotransferase; δ-aminovalerate aminotransferase; δ-aminovalerate transaminase
Systematic name: 5-aminopentanoate:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-97-7
References:
1.  Ichihara, A., Ichihara, E.A. and Suda, M. Metabolism of L-lysine by bacterial enzymes. IV. δ-Aminovaleric acid-glutamic acid transaminase. J. Biochem. (Tokyo) 48 (1960) 412–420.
[EC 2.6.1.48 created 1972]
 
 
EC 2.6.1.49     
Accepted name: dihydroxyphenylalanine transaminase
Reaction: L-dopa + 2-oxoglutarate = 3,4-dihydroxyphenylpyruvate + L-glutamate
For diagram of reaction, click here and for mechanism, click here
Glossary: L-dopa = 3,4-dihydroxy-L-phenylalanine
Other name(s): 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; DOPAATS
Systematic name: 3,4-dihydroxy-L-phenylalanine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-98-8
References:
1.  Fonnum, F. and Larsen, K. Purification and properties of dihydroxyphenylalanine transaminase from guinea pig brain. J. Neurochem. 12 (1965) 589–598. [DOI] [PMID: 5829872]
2.  Ranjith, N.K., Sasikala, Ch. and Ramana, Ch.V. Catabolism of L-phenylalanine and L-tyrosine by Rhodobacter sphaeroides OU5 occurs through 3,4-dihydroxyphenylalanine. Res. Microbiol. 158 (2007) 506–511. [DOI] [PMID: 17616348]
[EC 2.6.1.49 created 1972]
 
 
EC 2.6.1.50     
Accepted name: glutamine—scyllo-inositol transaminase
Reaction: L-glutamine + 2,4,6/3,5-pentahydroxycyclohexanone = 2-oxoglutaramate + 1-amino-1-deoxy-scyllo-inositol
Other name(s): glutamine scyllo-inosose aminotransferase; L-glutamine-keto-scyllo-inositol aminotransferase; glutamine-scyllo-inosose transaminase; L-glutamine-scyllo-inosose transaminase
Systematic name: L-glutamine:2,4,6/3,5-pentahydroxycyclohexanone aminotransferase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9033-03-8
References:
1.  Walker, J.B. and Walker, M.S. Streptomycin biosynthesis. Transamination reactions involving inosamines and inosadiamines. Biochemistry 8 (1969) 763–770. [PMID: 5781017]
[EC 2.6.1.50 created 1972]
 
 


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