Leucine transaminase
From Wikipedia, the free encyclopedia
Leucine transaminase (EC 2.6.1.6) is an enzyme characterised from rat liver that catalyzes a reversible chemical reaction to interconvert L-leucine and α-ketoglutaric acid with α-ketoisocaproic acid and L-glutamic acid:[1][2]
The enzyme is a transferase, specifically a transaminase, which transfer nitrogenous groups. The systematic name of this enzyme class is L-leucine:2-oxoglutarate aminotransferase. Other names in common use include L-leucine aminotransferase, leucine 2-oxoglutarate transaminase, leucine aminotransferase, and leucine-alpha-ketoglutarate transaminase. It employs one cofactor, pyridoxal phosphate.[3]
