Biology:2-aminohexanoate transaminase
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Short description: Class of enzymes
2-aminohexanoate transaminase | |||||||||
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Identifiers | |||||||||
EC number | 2.6.1.67 | ||||||||
CAS number | 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 | ||||||||
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In enzymology, a 2-aminohexanoate transaminase (EC 2.6.1.67) is an enzyme that catalyzes the chemical reaction
- L-2-aminohexanoate + 2-oxoglutarate [math]\displaystyle{ \rightleftharpoons }[/math] 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
- "Candida L-norleucine,leucine:2-oxoglutarate aminotransferase Purification and properties". Eur. J. Biochem. 167 (1): 141–7. 1987. doi:10.1111/j.1432-1033.1987.tb13315.x. PMID 3622507.
Original source: https://en.wikipedia.org/wiki/2-aminohexanoate transaminase.
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