- Source: Tryptophanamidase
In enzymology, a tryptophanamidase (EC 3.5.1.57) is an enzyme that catalyzes the chemical reaction
L-tryptophanamide + H2O
⇌
{\displaystyle \rightleftharpoons }
L-tryptophan + NH3
Thus, the two substrates of this enzyme are L-tryptophanamide and H2O, whereas its two products are L-tryptophan and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is L-tryptophanamide amidohydrolase. Other names in common use include tryptophan aminopeptidase, and L-tryptophan aminopeptidase. It employs one cofactor, manganese.
References
Iwayama A, Kimura T, Adachi O, Ameyama M (1983). "Crystallization and characterization of a novel aminopeptidase from Trichosporon cutaneum". Agric. Biol. Chem. 47 (11): 2483–2493. doi:10.1271/bbb1961.47.2483.
