L-leucine:2-oxoglutarate aminotransferase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate. [EC:2.6.1.6, MetaCyc:LEUCINE-AMINOTRANSFERASE-RXN]

L-leucine:2-oxoglutarate aminotransferase activity catalyzes the reversible transfer of an amino group from L-leucine to 2-oxoglutarate. This reaction results in the formation of α-ketoisocaproate and L-glutamate. The enzyme is involved in the catabolism of branched-chain amino acids, specifically leucine, and plays a crucial role in nitrogen metabolism. L-leucine:2-oxoglutarate aminotransferase is a pyridoxal phosphate-dependent enzyme, meaning it requires the cofactor pyridoxal phosphate for its activity. The enzyme utilizes a ping-pong mechanism where the amino group from leucine is first transferred to the pyridoxal phosphate cofactor, forming a Schiff base intermediate. Subsequently, the amino group is transferred from the cofactor to 2-oxoglutarate, regenerating the enzyme and producing L-glutamate. This enzyme activity is essential for maintaining metabolic homeostasis and plays a role in various physiological processes, including protein synthesis, energy production, and immune response.'
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Proteins (1)

Compounds (1)