In enzymology, a 2-aminohexanoate transaminase (EC 2.6.1.67) is an enzyme that catalyzes the chemical reaction

L-2-aminohexanoate + 2-oxoglutarate ${\displaystyle \rightleftharpoons }$ 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.

• 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.