Tryptophanamidase
Appearance
tryptophanamidase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC no. | 3.5.1.57 | ||||||||
CAS no. | 76689-19-5 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
|
In enzymology, a tryptophanamidase (EC 3.5.1.57) is an enzyme that catalyzes the chemical reaction
- L-tryptophanamide + H2O 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
[edit]- 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.