L-isoleucine transaminase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: 2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoic acid + L-glutamic acid. [EC:2.6.1.42, MetaCyc:BRANCHED-CHAINAMINOTRANSFERILEU-RXN]

L-isoleucine transaminase activity catalyzes the transfer of an amino group from L-isoleucine to an alpha-keto acid, typically alpha-ketoglutarate. This reaction results in the formation of alpha-keto-beta-methylvalerate and L-glutamate. The enzyme utilizes pyridoxal phosphate (PLP) as a cofactor, which is essential for the catalytic process. The reaction proceeds through a series of steps involving the formation of a Schiff base intermediate between PLP and the amino group of L-isoleucine. This intermediate undergoes a series of rearrangements and proton transfers, leading to the transfer of the amino group to alpha-ketoglutarate. The resulting alpha-keto-beta-methylvalerate is a key intermediate in the catabolism of L-isoleucine, a branched-chain amino acid. L-isoleucine transaminase activity plays a crucial role in amino acid metabolism, particularly in the breakdown of branched-chain amino acids. It is involved in the synthesis of glutamate, an important neurotransmitter and precursor for other amino acids. Deficiencies in L-isoleucine transaminase activity can lead to various metabolic disorders, affecting energy production and neurotransmitter function.'
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Proteins (1)

Compounds (1)