B6db activities : 2_6_1

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	2.6.1.21
Description	D-alanine aminotransferase.
Alternative names	D-aspartate aminotransferase. D-amino acid aminotransferase. D-amino acid transaminase.
Catalyzed reaction	D-alanine + 2-oxoglutarate = pyruvate + D-glutamate.
Cofactor	Pyridoxal-phosphate.
Comments	-!- Acts on the D-isomers of leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. -!- Formerly EC 2.6.1.10.
Prosite	PROSITE; PDOC00618;
PDB	3DAA; 2DAA; 1G2W;
Organisms	-Bacteria -Plants
Family	2.6.1.21 (17)

Links	Enzyme (activities) 2.6.1.21 BRENDA (activities) 2.6.1.21 KEGG (pathways) 2.6.1.21 PLPMDB (PLP mutants) 2.6.1.21

References	Lee, S.G.; Hong, S.P.; Song, J.J.; Kim, S.J.; Kwak, M.S.; Sung, M.H. (2006) Functional and Structural Characterization of Thermostable D-Amino Acid Aminotransferases from Geobacillus spp Appl. Envir. Microbiol. 72 1588- 94. Berger, B.J.; English, S.; Chan, G.; Knodel, M.H. (2003) Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis J Bacteriol 185 2418-31. Pucci, M.J.; Thanassi, J.A.; Ho, H.T.; Falk, P.J.; Dougherty, T.J. (1995) Staphylococcus haemolyticus contains two D-glutamic acid biosynthetic activities, a glutamate racemase and a D-amino acid transaminase J Bacteriol 177 336-42. Sugio, S.; Petsko, G. A.; Manning, J. M.; Soda, K.; Ringe, D. (1995) Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity Biochemistry 34 9661-9661. Tanizawa K, Asano S, Masu Y, Kuramitsu S, Kagamiyama H, Tanaka H, Soda K. (1989) The primary structure of thermostable D-amino acid aminotransferase from a thermophilic Bacillus species and its correlation with L-amino acid aminotransferases J Biol Chem 264 2450-4. Articles on 2.6.1.21

last changed	2007/09/20 18:44

Family