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- W2559608889 abstract "In this study we provide the first biochemical characterization of a bacterial pyranose 2-oxidase (AsP2Ox) from Arthrobacter siccitolerans. The enzyme catalyzes the oxidation of several aldopyranoses at the C-2 position, coupling it to the reduction of dioxygen to hydrogen peroxide. Pyranose 2-oxidases belong to the glucose-methanol-choline oxidoreductase family. A structural model based on the known X-ray structure of P2Ox from Phanerochaete chrysosporium supports that AsP2Ox shares structural features with well-characterized fungal P2Oxs. The gene coding for AsP2Ox was cloned and heterologously expressed in Escherichia coli. The purified recombinant enzyme is a 64-kDa monomer containing a non-covalently bound flavin adenine dinucleotide (FAD) cofactor, distinct features as compared with fungal counterparts that are ∼ 270 kDa homotetramers with covalent-linked FAD. AsP2Ox exhibits a redox potential of −50 mV, an optimum temperature of 37 °C and an optimum pH at 6.5. AsP2Ox oxidizes d-glucose at the highest efficiency, using additionally d-galactose, d-xylose, l-arabinose and d-ribose as electron donors, coupling their oxidation to the reduction of both dioxygen and 1,4-benzoquinone. AsP2Ox shows a relatively low thermal stability with a melting temperature (Tm) of 43 °C and a half-life (t1/2) at 40 °C of 25 min. This work expands the repertoire of bacterial oxidoreductases with importance in biotechnological and diagnostic applications." @default.
- W2559608889 created "2016-12-08" @default.
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- W2559608889 date "2016-11-01" @default.
- W2559608889 modified "2023-10-16" @default.
- W2559608889 title "Characterization of a bacterial pyranose 2-oxidase from Arthrobacter siccitolerans" @default.
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- W2559608889 doi "https://doi.org/10.1016/j.molcatb.2016.11.005" @default.
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