Enzyme-substrate matching in biocatalysis: in silico studies to predict substrate preference of ten putative ene-reductases from Mucor circinelloides MUT44

摘要: Ene-reductases are flavoproteins able to catalyse the reduction of carbon-carbon double bonds with many potential applications in biocatalysis. The fungus Mucor circinelloides MUT44 has high ene-reductase activity when grown presence substrates carrying different electron-withdrawing groups. Genome sequencing revealed ten putative genes coding for ene-reductases that can be potentially exploited biocatalytic purposes. To this end, availability a method predict which isoform binds and turns over specific substrate would help choose best catalyst desired bioconversion. Here, homology models enzymes first generated, validated show proteins share typical TIM barrel fold conserved β-hairpin cap on one side non-conserved subdomain capping other side, where FMN cofactor is accommodated. The active site terms both volume charge distribution whereas residues responsible recognition catalysis generally conserved. Docking cyclohexenone into shows binding almost superimposable found pentaerythritol tetranitrate reductase complex (PDB ID 1GVQ) isoforms 1, 2, 6 10. The data demonstrate silico predictions used new fungal substrate-enzyme matching selection most suitable biotransformation.