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| EC | 4.1.99.1 | ||||||||
| Accepted name: | tryptophanase | ||||||||
| Reaction: | L-tryptophan + H2O = indole + pyruvate + NH3 (overall reaction) (1a) L-tryptophan = indole + 2-aminoprop-2-enoate (1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous) (1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous) |
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| Other name(s): | L-tryptophanase; L-tryptophan indole-lyase (deaminating); TNase | ||||||||
| Systematic name: | L-tryptophan indole-lyase (deaminating; pyruvate-forming) | ||||||||
| Comments: | 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 3.5.99.10, 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: | BRENDA, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9024-00-4 | ||||||||
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