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An Atypical Flavin-Containing Monooxygenase Homologue Catalyzes the Third Epoxidation in the Verrucosidin Biosynthesis Click to copy article link Article link copied!
Scaffold modification, including late-stage oxidative tailoring, enables biosynthetic pathways to generate structurally distinct products from closely related intermediates. (1,2) Usually, even a single oxygenation event can alter product structure. Flavin-dependent monooxygenases (FMOs) often play important roles in these processes by epoxidation or hydroxylation. (3−7) This is particularly relevant for pathways that produce closely related metabolites differing only in oxidation state.
Deletion of bZIP Transcription Factor PratfA Reveals Specialized Metabolites Potentially Regulating Stress Response in Penicillium raistrickii
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