| EC |
2.6.1.1 |
| Accepted name: |
aspartate transaminase |
| Reaction: |
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate |
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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 (ambiguous); 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] |
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| [EC 2.6.1.1 created 1961, modified 1976] |
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