Accessing Chemo- and Regioselective Benzylic and Aromatic Oxidations by Protein Engineering of an Unspecific Peroxygenase.

ABSTRACT: Unspecific peroxygenases (UPOs) enable oxyfunctionalizations of a broad substrate range with unparalleled activities. Tailoring these enzymes for chemo- and regioselective transformations represents a grand challenge due to the difficulties in their heterologous productions. Herein, we performed protein engineering in Saccharomyces cerevisiae using the MthUPO from Myceliophthora thermophila. More than 5300 transformants were screened. This protein engineering led to a significant reshaping of the active site as elucidated by computational modelling. The reshaping was responsible for the increased oxyfunctionalization activity, with improved k _cat/K _m values of up to 16.5-fold for the model substrate 5-nitro-1,3-benzodioxole. Moreover

SUBMITTER: Knorrscheidt A 

PROVIDER: S-EPMC8496131 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature