EC 126.96.36.199 - Tryptophanase
IntEnz Enzyme Nomenclature
L-tryptophan indole-lyase (deaminating)
19553 [IUBMB]H2OH2OName origin: UniProt - CHECKED (C)Formula: H2O
Charge: 0ChEBI compound status: CHECKED (C)L-tryptophanL-tryptophanName origin: UniProt - CHECKED (C)Formula: C11H12N2O2
Charge: 0ChEBI compound status: CHECKED (C)=indoleindoleName origin: UniProt - CHECKED (C)Formula: C8H7N
Charge: 0ChEBI compound status: CHECKED (C)NH4+NH4(+)Name origin: UniProt - CHECKED (C)Formula: H4N
Charge: 1ChEBI compound status: CHECKED (C)
A pyridoxal-phosphate protein, requiring K+. The enzyme cleaves a carbon-carbon bond, releasing indole and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 188.8.131.52, 2-iminobutanoate/2-iminopropanoate deaminase. Also catalyses 2,3-elimination and β-replacement reactions of some indole-substituted tryptophan analogues of L-cysteine, L-serine and other 3-substituted amino acids.
Links to other databases
Properties of tryptophanase from Escherichia coli.Biochim. Biophys. Acta 65: 233-244 (1962). [PMID: 14017164]
Tryptophanase from Aeromonas liquifaciens. Purification, molecular weight and some chemical, catalytic and immunological properties.Biochim. Biophys. Acta 315: 449-463 (1973).
Properties of crystalline tryptophanase.J. Biol. Chem. 240: 1211-1218 (1965). [PMID: 14284727]
Tryptophanase: structure, catalytic activities, and mechanism of action.Adv. Enzymol. Relat. Areas Mol. Biol. 42: 287-333 (1975). [PMID: 236639]
[EC 184.108.40.206 created 1972]