1.21.98.2: dichlorochromopyrrolate synthase
This is an abbreviated version!
For detailed information about dichlorochromopyrrolate synthase, go to the full flat file.
Reaction
2 3-(7-chloroindol-3-yl)-2-iminopropanoate + = + + 2 H2O
Synonyms
EC 1.21.3.9, EC 4.3.1.26, RebD
ECTree
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Systematic Name
Systematic Name on EC 1.21.98.2 - dichlorochromopyrrolate synthase
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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].