D-alanine + 2-oxoglutarate $rightleftharpoons$ pyruvate + D-glutamate

Thus, the two substrates of this enzyme are D-alanine and 2-oxoglutarate, whereas its two products are pyruvate and D-glutamate.

This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is D-alanine:2-oxoglutarate aminotransferase. Other names in common use include D-aspartate transaminase, D-alanine aminotransferase, D-aspartic aminotransferase, D-alanine-D-glutamate transaminase, D-alanine transaminase, and D-amino acid aminotransferase. This enzyme participates in 6 metabolic pathways: lysine degradation, arginine and proline metabolism, phenylalanine metabolism, d-arginine and d-ornithine metabolism, d-alanine metabolism, and peptidoglycan biosynthesis. It employs one cofactor, pyridoxal phosphate.

Structural studies

As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , and .

References

• THORNE CB, GOMEZ CG, HOUSEWRIGHT RD "Transamination of D-amino acids by Bacillus subtilis". J. Bacteriol. 69 357–62.
• THORNE CB, MOLNAR DM "D-Amino acid transamination in bacillus anthracis". J. Bacteriol. 70 420–6.
• Martinez-Carrion M, Jenkins WT "D-Alanine-D-glutamate transaminase. I. Purification and characterization". J. Biol. Chem. 240 3538–46.
• Ogawa T, Fukuda M, Sasaoka K "Occurrence of D-amino acid aminotransferase in pea seedlings". Biochem. Biophys. Res. Commun. 52 998–1002.
• Yonaha K, Misono H, Yamamoto T, Soda K "D-amino acid aminotransferase of Bacillus sphaericus. Enzymologic and spectrometric properties". J. Biol. Chem. 250 6983–9.
• Tanizawa K, Masu Y, Asano S, Tanaka H, Soda K "Thermostable D-amino acid aminotransferase from a thermophilic Bacillus species. Purification, characterization, and active site sequence determination". J. Biol. Chem. 264 2445–9.
• Fotheringham IG, Bledig SA, Taylor PP "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 4319–23.
• Yoshimura T, Soda K, Ringe D, Petsko G, Manning JM "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 2879–88.
• Sugio S, Petsko GA, Manning JM, Soda K, Ringe D "Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity". Biochemistry. 34 9661–9.

External links

The CAS registry number for this enzyme class is .

Gene Ontology (GO) codes