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Gewählte Publikation:

Kostelac, A; Sutzl, L; Puc, J; Furlanetto, V; Divne, C; Haltrich, D.
(2022): Biochemical Characterization of Pyranose Oxidase from Streptomyces canus-Towards a Better Understanding of Pyranose Oxidase Homologues in Bacteria
INT J MOL SCI. 2022; 23(21), 13595 FullText FullText_BOKU

Pyranose oxidase (POx, glucose 2-oxidase; EC, 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 ScPOx as well. Some of these glycosides are characteristic substrates for the recently described FAD-dependent C-glycoside 3-oxidase from Microbacterium trichothecenolyticum. Here, we show that FAD-dependent C-glycoside 3-oxidases and pyranose oxidases are enzymes belonging to the same sequence space.
Autor*innen der BOKU Wien:
Haltrich Dietmar
Kostelac Anja
Sützl Leander

Find related publications in this database (Keywords)
pyranose oxidase
bacterial lignocellulose degradation

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