D-amino-acid transaminase explained

D-alanine transaminase
Ec Number:	2.6.1.21
Cas Number:	37277-85-3
Go Code:	0047810

In enzymology, a D-amino-acid transaminase is an enzyme that catalyzes the chemical reaction:

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 . 1955 . Transamination of D-amino acids by Bacillus subtilis . J. Bacteriol. . 69 . 357–62 . 14367287 . 3 . 10.1128/JB.69.3.357-362.1955 . 357541 .
• Thorne CB, Molnar DM . 1955 . D-Amino acid transamination in bacillus anthracis . J. Bacteriol. . 70 . 420–6 . 13263311 . 4 . 10.1128/JB.70.4.420-426.1955 . 386242 .
• Martinez-Carrion M, Jenkins WT . 1965 . D-Alanine-D-glutamate transaminase. I. Purification and characterization . J. Biol. Chem. . 240 . 3538–46 . 4953710 . 9 .
• Ogawa T, Fukuda M, Sasaoka K . 1973 . Occurrence of D-amino acid aminotransferase in pea seedlings . Biochem. Biophys. Res. Commun. . 52 . 998–1002 . 4710577 . 10.1016/0006-291X(73)91036-X . 3 .
• Yonaha K, Misono H, Yamamoto T, Soda K . 1975 . D-amino acid aminotransferase of Bacillus sphaericus. Enzymologic and spectrometric properties . J. Biol. Chem. . 250 . 6983–9 . 1158891 . 17 .
• Tanizawa K, Masu Y, Asano S, Tanaka H, Soda K . 1989 . Thermostable D-amino acid aminotransferase from a thermophilic Bacillus species. Purification, characterization, and active site sequence determination . J. Biol. Chem. . 264 . 2445–9 . 2914916 . 5 .
• Fotheringham IG, Bledig SA, Taylor PP . 1998 . 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 . 9696787 . 16 . 10.1128/JB.180.16.4319-4323.1998 . 107435 .
• Yoshimura T, Soda K, Ringe D, Petsko G, Manning JM . 1998 . 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 . 9485439 . 10.1021/bi972842p . 9 .
• Sugio S, Petsko GA, Manning JM, Soda K, Ringe D . 1995 . Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity . Biochemistry . 34 . 9661–9 . 7626635 . 10.1021/bi00030a002 . 30 .