2-aminohexanoate transaminase
| 2-aminohexanoate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.67 | ||||||||
| CAS no. | 111310-35-1 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
2-aminohexanoate transaminase (EC 2.6.1.67) is a pyridoxal phosphate-dependent enzyme that catalyzes the chemical reaction
The two substrates of this enzyme characterised from Candida guilliermondii are L-norleucine and α-ketoglutaric acid. Its products are 2-oxohexanoic acid and L-glutamic acid.[1]
This enzyme is a transferase, specifically a transaminase, 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.[2]
References
- ↑ 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.
- ↑ Enzyme 2.6.1.67 at KEGG Pathway Database.