L-lysine 6-transaminase
From Wikipedia, the free encyclopedia
L-lysine 6-transaminase (EC 2.6.1.36) is an enzyme originally characterised from Flavobacterium fuscum that catalyzes a reversible chemical reaction that interconverts L-lysine and α-ketoglutaric acid with L-allysine and glutamic acid.[1][2]
This enzyme is a transferase, specifically a transaminase, which transfer nitrogenous groups. This enzyme participates in lysine biosynthesis. It uses pyridoxal phosphate as a cofactor.[3]
Nomenclature
The systematic name of this enzyme class is L-lysine:2-oxoglutarate 6-aminotransferase. Other names in common use include
- lysine 6-aminotransferase,
- lysine epsilon-aminotransferase,
- lysine epsilon-transaminase,
- lysine:2-ketoglutarate 6-aminotransferase,
- L-lysine-alpha-ketoglutarate aminotransferase, and
- L-lysine-alpha-ketoglutarate 6-aminotransferase.[3]
