Tryptophanase
Definition:
EC Tree > 4 Lyases > 4.1 Carbon-carbon lyases > 4.1.99 Other carbon-carbon lyases > 4.1.99.1 tryptophanase
Tryptophanase is a pyridoxal-phosphate-dependent C-C lyase requiring K+. It cleaves the C-C bond of L-tryptophan with water, releasing indole and an unstable enamine that tautomerizes to an imine and undergoes hydrolytic deamination to pyruvate and ammonia (the latter can also be catalyzed by EC 3.5.99.10). It is expressed in enteric bacteria during stationary phase and is used in tryptophan degradation and indole signaling. Structurally it is a PLP-dependent fold-I beta-family enzyme.
Tryptophanase is a pyridoxal-phosphate-dependent C-C lyase requiring K+. It cleaves the C-C bond of L-tryptophan with water, releasing indole and an unstable enamine that tautomerizes to an imine and undergoes hydrolytic deamination to pyruvate and ammonia (the latter can also be catalyzed by EC 3.5.99.10). It is expressed in enteric bacteria during stationary phase and is used in tryptophan degradation and indole signaling. Structurally it is a PLP-dependent fold-I beta-family enzyme.
References:
Biomedical Dictionary
The Biomedical Dictionary is a comprehensive and professional collection of biological academic terms and subject datas. All explanations are supported by authoritative books or high impact factor literatures, and you can acquire accurate explanations of the biomedical terms you want to know.
Molarity Calculator
Dilution Calculator
