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.
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.
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.
Structure L-lysine 6-transaminase belongs to the aminotransferase class-III family. Crystal structures of L-lysine 6-transaminase reveal a Glu243 “switch” through which the enzyme changes substrate specificities.
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