2-aminohexanoate transaminase
From Wikipedia, the free encyclopedia
In enzymology, a 2-aminohexanoate transaminase (EC 2.6.1.67) is an enzyme that catalyzes the chemical reaction
- 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.
[edit] References
- IUBMB entry for 2.6.1.67
- BRENDA references for 2.6.1.67 (Recommended.)
- PubMed references for 2.6.1.67
- PubMed Central references for 2.6.1.67
- Google Scholar references for 2.6.1.67
- Der Garabedian PA, Vermeersch JJ (1987). "Candida L-norleucine,leucine:2-oxoglutarate aminotransferase Purification and properties". Eur. J. Biochem. 167: 141–7. doi: . PMID 3622507.
[edit] External links
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- The CAS registry number for this enzyme class is 111310-35-1.