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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 .
contains noncovalently bound flavin of 0.58 mol per mol of protein. RebO protein that is overexpressed without supplementation of FAD in Escherichia coli BL21(DE3) contains less than 0.5 mol of noncovalently bound flavin per mol of enzyme