IUBMB Enzyme Nomenclature


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; 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


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. [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. [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 created 1972 (EC created 1961, incorporated 1972), modified 2005]

Return to EC 2.6.1 home page
Return to EC 2.6 home page
Return to EC 2 home page
Return to Enzymes home page
Return to IUBMB Biochemical Nomenclature home page