Information on EC - dichlorochromopyrrolate synthase

for references in articles please use BRENDA:EC1.21.98.2
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IUBMB Comments
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 . Contains one molecule of heme b per monomer, as well as non-heme iron that is not part of an iron-sulfur center . In vivo the enzyme uses hydrogen peroxide, formed by the enzyme upstream in the biosynthetic pathway (EC, 7-chloro-L-tryptophan oxidase) as the electron acceptor. However, the enzyme is also able to catalyse the reaction using molecular oxygen .
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The enzyme appears in viruses and cellular organisms
RebD, more
2 3-(7-chloroindol-3-yl)-2-iminopropanoate + H2O2 = dichlorochromopyrrolate + NH3 + 2 H2O
show the reaction diagram
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