D-amino-acid transaminase

From Wikipedia, the free encyclopedia

In enzymology, a D-amino-acid transaminase (EC 2.6.1.21) 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1A0G, 1DAA, 1G2W, 2DAA, 2DAB, 3DAA, 4DAA, and 5DAA.

[edit] References

IUBMB entry for 2.6.1.21
BRENDA references for 2.6.1.21 (Recommended.)
PubMed references for 2.6.1.21
PubMed Central references for 2.6.1.21
Google Scholar references for 2.6.1.21
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THORNE CB, MOLNAR DM (1955). "D-Amino acid transamination in bacillus anthracis". J. Bacteriol. 70: 420–6. PMID 13263311.
Martinez-Carrion M, Jenkins WT (1965). "D-Alanine-D-glutamate transaminase. I. Purification and characterization". J. Biol. Chem. 240: 3538–46. PMID 4953710.
Ogawa T, Fukuda M, Sasaoka K (1973). "Occurrence of D-amino acid aminotransferase in pea seedlings". Biochem. Biophys. Res. Commun. 52: 998–1002. PMID 4710577.
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. PMID 1158891.
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. PMID 2914916.
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. PMID 9696787.
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. PMID 9485439.
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. PMID 7626635.