Requires heme. The enzyme from Chromobacterium violaceum is specific for tryptophan derivatives possessing its carboxyl group free or as an amide or ester, and an unsubstituted indole ring. Also catalyses the α,β dehydrogenation of L-tryptophan side chains in peptides. The product of the reaction can hydrolyse spontaneously to form (indol-3-yl)pyruvate.
Genet, R., Denoyelle, C. and Menez, A. Purification and partial characterization of an amino acid α,β-dehydrogenase, L-tryptophan 2′,3′-oxidase from Chromobacterium violaceum. J. Biol. Chem.269 (1994) 18177–18184. [PMID: 8027079]
Genet, R., Benetti, P.H., Hammadi, A. and Menez, A. L-Tryptophan 2′,3′-oxidase from Chromobacterium violaceum. Substrate specificity and mechanistic implications. J. Biol. Chem.270 (1995) 23540–23545. [DOI] [PMID: 7559518]
[EC 126.96.36.199 created 2000 as EC 188.8.131.52, transferred 2003 to EC 184.108.40.206]