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