Discovery of a new subfamily expands the catalytic versatility of vanillyl alcohol oxidases
Nils Weindorf, Tobias Rapsch, Willem J. H. van Berkel, Dirk Tischler
TL;DR
Scientists discovered a new type of enzyme that can efficiently convert phenol derivatives into valuable flavor compounds and ketones.
Contribution
A new subfamily of vanillyl alcohol oxidases was identified that enables overoxidation to ketones and deamination reactions.
Findings
PvVAO from Paecilomyces variotii catalyzes oxidative deamination of p-hydroxybenzylamines.
PvVAO can overoxidize benzylic alcohols to ketones at high pH.
Phylogenetic analysis revealed a distinct clade with unique active site features.
Abstract
Flavoenzymes of the 4-phenol oxidoreductase family are versatile biocatalysts that catalyze the oxidation of a wide variety of phenol derivatives to alcohols, aldehydes, ketones or alkenes. The promiscuous FAD-dependent vanillyl alcohol oxidases from Penicillium simplicissimum (PsVAO) and Diplodia corticola (DcVAO) have been described to catalyze the oxidative deamination of p-hydroxybenzylamines, giving rise to valuable flavor compounds, but starting from p-alkyl substituted phenols, the ketones are usually not accessible as these oxidases preferably stop at chiral benzylic alcohols. Here we took a closer look into the fungal VAO family with the aim to identify new members that can perform this deamination reaction and also the overoxidation of benzylic alcohols to ketones at a sufficient rate for application. Phylogenetic and amino acid cluster analysis revealed one clade that…
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Taxonomy
TopicsEnzyme-mediated dye degradation · Biochemical and biochemical processes · Enzyme Catalysis and Immobilization