• Source: D-amino-acid transaminase

In enzymology, a D-amino-acid transaminase (EC 2.6.1.21) is an enzyme that catalyzes the chemical reaction:

D-alanine + 2-oxoglutarate



⇌


{\displaystyle \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 1A0G, 1DAA, 1G2W, 2DAA, 2DAB, 3DAA, 4DAA, and 5DAA.




References



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.
Ogawa T, Fukuda M, Sasaoka K (1973). "Occurrence of D-amino acid aminotransferase in pea seedlings". Biochem. Biophys. Res. Commun. 52 (3): 998–1002. 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.
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.
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.
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.

Kata Kunci Pencarian:

• Asam aminobutirat gamma
• Biokimia
• Metabolisme
• Hipertrigliseridemia
• D-amino-acid transaminase
• Amino acid synthesis
• Alanine transaminase
• Aspartate transaminase
• Branched chain amino acid transaminase 1
• GABA
• Aspartic acid
• 4-aminobutyrate transaminase
• Glutamic acid
• Amino acid