TRYPTOPHANASE
\tɹˈɪptəfˌane͡ɪs], \tɹˈɪptəfˌaneɪs], \t_ɹ_ˈɪ_p_t_ə_f_ˌa_n_eɪ_s]\
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An enzyme that catalyzes the conversion of L-tryptophan and water to indole, pyruvate, and ammonia. It is a pyridoxal-phosphate protein, requiring K+. It also catalyzes 2,3-elimination and beta-replacement reactions of some indole-substituted tryptophan analogs of L-cysteine, L-serine, and other 3-substituted amino acids. (From Enzyme Nomenclature, 1992) EC 4.1.99.1.
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