tryptophanase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: L-tryptophan + H2O = indole + NH4 + pyruvate. [RHEA:19553]

Tryptophanase activity catalyzes the irreversible, non-oxidative, concerted breakdown of L-tryptophan into indole, pyruvate, and ammonia. This reaction involves the cleavage of the carbon-carbon bond between the alpha-carbon and the beta-carbon of L-tryptophan, resulting in the formation of indole and pyruvate. The reaction also involves the removal of the amino group from L-tryptophan, generating ammonia. Tryptophanase is a pyridoxal 5'-phosphate (PLP)-dependent enzyme, meaning it requires PLP as a cofactor for its catalytic activity. The PLP cofactor acts as an electron sink, stabilizing the reaction intermediates and facilitating the transfer of electrons during the reaction. Tryptophanase is found in various bacteria, including Escherichia coli, and plays a crucial role in tryptophan catabolism. This enzyme is also involved in the production of indole, a signaling molecule that can influence various cellular processes, such as biofilm formation and quorum sensing.'
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Proteins (1)

Compounds (1)