D-amino-acid transaminase (EC 2.6.1.21) is an enzyme originally characterised from bacteria that catalyzes several reversible chemical reactions that interconvert specific D-amino acids and α-ketoglutaric acid with the corresponding α-keto acid and D-glutamic acid. For example, it can use D-alanine as a substrate:[1][2][3]
| D-alanine transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.21 | ||||||||
| CAS no. | 37277-85-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In some organisms, the enzyme can use alternative keto acids instead of α-ketoglutaric acid.[4] It has been found in pea,[5] and the genes coding for the enzyme have been studied in Bacillus sphaericus.[6][7]
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.[8] 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.[9][10]
Structural studies
editReferences
edit- ↑ Thorne CB, Gomez CG, Housewright RD (1955). "Transamination of D-amino acids by Bacillus subtilis". J. Bacteriol. 69 (3): 357–62. doi:10.1128/JB.69.3.357-362.1955. PMC 357541. PMID 14367287.
- ↑ Thorne CB, Molnar DM (1955). "D-Amino acid transamination in Bacillus anthracis". J. Bacteriol. 70 (4): 420–6. doi:10.1128/JB.70.4.420-426.1955. PMC 386242. PMID 13263311.
- ↑ Martinez-Carrion M, Jenkins WT (1965). "D-Alanine-D-glutamate transaminase. I. Purification and characterization". J. Biol. Chem. 240 (9): 3538–46. doi:10.1016/S0021-9258(18)97177-2. PMID 4953710.
- ↑ 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 (5): 2445–9. doi:10.1016/S0021-9258(19)81633-2. PMID 2914916.
- ↑ Ogawa T, Fukuda M, Sasaoka K (1973). "Occurrence of D-amino acid aminotransferase in pea seedlings". Biochem. Biophys. Res. Commun. 52 (3): 998–1002. Bibcode:1973BBRC...52..998O. doi:10.1016/0006-291X(73)91036-X. 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 (17): 6983–9. doi:10.1016/S0021-9258(19)41029-6. PMID 1158891.
- ↑ 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 (16): 4319–23. doi:10.1128/JB.180.16.4319-4323.1998. PMC 107435. PMID 9696787.
- ↑ Enzyme 2.6.1.21 at KEGG Pathway Database.
- ↑ 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 (9): 2879–88. doi:10.1021/bi972842p. 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 (30): 9661–9. doi:10.1021/bi00030a002. PMID 7626635.
