L-leucine transaminase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: 2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamatic acid. [EC:2.6.1.42, MetaCyc:BRANCHED-CHAINAMINOTRANSFERLEU-RXN]

L-leucine transaminase activity is a crucial enzymatic function that catalyzes the transfer of an amino group from L-leucine to an α-keto acid, typically α-ketoglutarate. This reaction forms α-ketoisocaproate and L-glutamate. The primary role of this activity is in amino acid metabolism, specifically in the breakdown of branched-chain amino acids (BCAAs) like leucine. This process is vital for generating energy, as BCAAs can be used as fuel by various tissues. L-leucine transaminase also plays a crucial role in nitrogen metabolism by contributing to the removal of excess nitrogen from the body. The enzyme's activity is regulated by several factors, including the concentration of its substrates (L-leucine and α-ketoglutarate), cofactors like pyridoxal phosphate (PLP), and the presence of inhibitors. Deficiencies in L-leucine transaminase activity can lead to various metabolic disorders, emphasizing its critical role in maintaining normal physiological function.'
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Proteins (1)

Compounds (1)