ArticleThe FEBS journal2025
Shifting the substrate scope of dimeric pyranose oxidase from monosaccharide to glycoside preference through oligomeric state modification.
Article in The FEBS journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Pyranose oxidase (POx) and C-glycoside oxidase (CGOx) are FAD-dependent oxidoreductases belonging to the glucose-methanol-choline oxidoreductase superfamily and share the same sequence space. Despite a shared structural fold, these two members possess homologous domains that enable (arm and head domain) or disable (insertion-1 domain and barrel-shaped bottom) oligomerization. POxs with a higher oligomerization state (dimeric or tetrameric) exclusively catalyze the oxidation of monosaccharides (d-glucose, d-xylose). In contrast, the monomeric state of POxs/CGOxs is observed to prefer glycosides (homoorientin, phlorizin) and has low activity with free monosaccharides. We aimed to engineer dimeric POx from Kitasatospora aureofaciens (KaPOx) to form a functional monomer, and monomeric POx/CGOx from Streptomyces canus (ScPOx) to a dimeric structure. Deletion of the head and arm domains of the KaPOx subunit resulted in enzyme variants with a less hydrophobic surface, thus affecting its oligomerization. These monomeric KaPOx variants KaPOx_xal and KaPOx_xalh resembled monomeric wild-type POxs/CGOxs and preferred glycosides as substrates over monosaccharides with catalytic efficiencies for phlorizin being 24 × 10
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