Contains a noncovalently bound FAD [1,2]. This enzyme catalyses a step in the biosynthesis of rebeccamycin, an indolocarbazole alkaloid produced by the bacterium Lechevalieria aerocolonigenes. During catalysis, the bound FAD is reoxidized at the expense of molecular oxygen, producing one molecule of hydrogen peroxide. The enzyme shows significant preference for 7-chloro-L-tryptophan over L-tryptophan [1].
Enzymatic reactions [BR:br08201]
1. Oxidoreductase reactions
1.4 Acting on the CH-NH2 group of donors
1.4.3 With oxygen as acceptor
1.4.3.23
R09560 7-Chloro-L-tryptophan + Oxygen <=> 2-Imino-3-(7-chloroindol-3-yl)propanoate + Hydrogen peroxide