The dauc-8-en-11-ol synthase from Streptomyces venezuelae was investigated for its catalytic activity towards alternative terpene precursors, specifically designed to enable new cyclisation pathways. Exchange of aromatic amino acid residues at the enzyme surface by site-directed mutagenesis led to a 4-fold increase of the yield in preparative scale incubations, which likely results from an increased enzyme stability instead of improved enzyme kinetics.
Keywords: biocatalyst; isotopic labelling; mutagenesis; terpene cyclisation.
© 2021 The Authors. Chemistry - A European Journal published by Wiley-VCH GmbH.