Identification of Key Active-Site Positions Controlling the Chemoselectivity of Aspergillus Brasiliensis Unspecific Peroxygenase.

ABSTRACT: Heme-containing unspecific peroxygenases (UPOs) have attracted significant attention as biocatalysts for oxidation reactions due to their ability to function without expensive nicotinamide cofactors. In the recent study, the UPO from aspergillus brasiliensis (AbrUPO) is found to catalyze the aromatic hydroxylation of substituted benzenes, a feature that distinguishes AbrUPO from other reported wild-type UPOs. To elucidate the underlying factors in the active site and substrate access channel of AbrUPO-which contains fewer phenylalanine residues compared to other UPOs that primarily catalyze benzylic hydroxylation-twenty two AbrUPO variants with single, double, triple, or quadruple amino acid substitutions were constructed to mimic the active sites or substrate access channels of other UPOs

SUBMITTER: Schmitz F 

PROVIDER: S-EPMC12117455 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature