tryptophanamidase | |||||||||
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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 | ||||||||
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In enzymology, a tryptophanamidase (EC 3.5.1.57) is an enzyme that catalyzes the chemical reaction
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.
In enzymology, a phenylalanine dehydrogenase (EC 1.4.1.20) is an enzyme that catalyzes the chemical reaction
In enzymology, a tryptophan dehydrogenase (EC 1.4.1.19) is an enzyme that catalyzes the chemical reaction
The enzyme tryptophanase (EC 4.1.99.1) catalyzes the chemical reaction
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Tryptophanyl aminopeptidase is an enzyme. This enzyme catalyses the following chemical reaction