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Tryptophanamidase

From Wikipedia, the free encyclopedia
tryptophanamidase
Identifiers
EC no.3.5.1.57
CAS no.76689-19-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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

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  • 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.