In enzymology, a 2-aminohexanoate transaminase (EC 2.6.1.67) is an enzyme that catalyzes the chemical reaction
| 2-aminohexanoate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.67 | ||||||||
| CAS no. | 111310-35-1 | ||||||||
| 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 | ||||||||
| |||||||||
- L-2-aminohexanoate + 2-oxoglutarate 2-oxohexanoate + L-glutamate
Thus, the two substrates of this enzyme are L-2-aminohexanoate and 2-oxoglutarate, whereas its two products are 2-oxohexanoate and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-2-aminohexanoate:2-oxoglutarate aminotransferase. Other names in common use include norleucine transaminase, norleucine (leucine) aminotransferase, and leucine L-norleucine: 2-oxoglutarate aminotransferase. It employs one cofactor, pyridoxal phosphate.
References
edit- Der Garabedian PA, Vermeersch JJ (1987). "Candida L-norleucine,leucine:2-oxoglutarate aminotransferase Purification and properties". Eur. J. Biochem. 167 (1): 141–7. doi:10.1111/j.1432-1033.1987.tb13315.x. PMID 3622507.
