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Updated: Jul 6, 2026

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
Published on: March 18, 2012
An Atypical Flavin-Containing Monooxygenase Homologue Catalyzes the Third Epoxidation in the Verrucosidin
Hui-Ling Wei1, Xiao-Ling Chen1, Wen-Bing Yin2
1Philipps-Universität Marburg, Fachbereich Pharmazie, Institut für Pharmazeutische Biologie und Biotechnologie, Robert-Koch-Straße 4, 35037 Marburg, Germany.
Abstract:
Penicillium polonicum CGMCC 3.15272 converts deoxyverrucosidin to verrucosidin by epoxidation with an atypical 805-amino acid large flavin-dependent monooxygenase homologue, VecG. Gene deletion, heterologous expression, and mutagenesis proved that both its predicted 458-amino acid N-terminal FMO core and the 242-amino acid C-terminal transmembrane region are essential for the catalysis. VecG differs from its inactive orthologue DovG in strain NRRL 995 in only three amino acids, two of which are more critical for the activity.
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