Biochemical Characterization of Pyranose Oxidase from <i>Streptomyces canus</i>-Towards a Better Understanding of Pyranose Oxidase Homologues in Bacteria.

ABSTRACT: Pyranose oxidase (POx, glucose 2-oxidase; EC 1.1.3.10, pyranose:oxygen 2-oxidoreductase) is an FAD-dependent oxidoreductase and a member of the auxiliary activity (AA) enzymes (subfamily AA3_4) in the CAZy database. Despite the general interest in fungal POxs, only a few bacterial POxs have been studied so far. Here, we report the biochemical characterization of a POx from Streptomyces canus (ScPOx), the sequence of which is positioned in a separate, hitherto unexplored clade of the POx phylogenetic tree. Kinetic analyses revealed that ScPOx uses monosaccharide sugars (such as d-glucose, d-xylose, d-galactose) as its electron-donor substrates, albeit with low catalytic efficiencies. Interestingly, various C- and O-glycosides (such as puerarin) were oxidized by Sc

SUBMITTER: Kostelac A 

PROVIDER: S-EPMC9659204 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature