EC Explorer

1.21.98.2

dichlorochromopyrrolate synthase

2 3-(7-chloroindol-3-yl)-2-iminopropanoate + H₂O₂ = dichlorochromopyrrolate + NH₃ + 2 H₂O

RebD, chromopyrrolic acid synthase, chromopyrrolate synthase

3-(7-chloroindol-3-yl)-2-iminopropanoate ammonia-lyase (dichlorochromopyrrolate-forming)

This enzyme catalyses a step in the biosynthesis of rebeccamycin, an indolocarbazole alkaloid produced by the bacterium Lechevalieria aerocolonigenes. The enzyme is a dimeric heme-protein oxidase that catalyses the oxidative dimerization of two L-tryptophan-derived molecules to form dichlorochromopyrrolic acid, the precursor for the fused six-ring indolocarbazole scaffold of rebeccamycin [1]. Contains one molecule of heme b per monomer, as well as non-heme iron that is not part of an iron-sulfur center [2]. In vivo the enzyme uses hydrogen peroxide, formed by the enzyme upstream in the biosynthetic pathway (EC 1.4.3.23, 7-chloro-L-tryptophan oxidase) as the electron acceptor. However, the enzyme is also able to catalyse the reaction using molecular oxygen [3].

created 2010 as EC 4.3.1.26, transferred 2013 to EC 1.21.3.9, transferred 2016 to EC 1.21.98.2