Molecular Characterization of a Stereoselective and Promiscuous Flavanone 3-Hydroxylase fromCarthamus tinctoriusL

)-flavanones. Homology modeling and molecular docking combined with site-directed mutagenesis identified the amino acid residues necessary for hydroxylation. These findings demonstrate the potential versatility of CtF3H1 in regio- and stereohydroxylation and provide molecular insights into the catalytic mechanism of F3H for further enzyme engineering.