Description
Pyranose oxidase (P2O) catalyzes the oxidation of aldopyranoses at position C-2 to yield the corresponding 2-ketoaldoses. P2O is a homotetrameric protein that contains covalently bound flavin adenine dinucleotide (FAD). The in vivo substrates of P2O are thought to be D-glucose, D-galactose, and D-xylose. They are oxidized to 2-keto-D-glucose (D-arabino-hexos-2-ulose, 2-dehydro-D-glucose), 2-keto-D-galactose (D-lyxo-hexos-2-ulose, 2-dehydro-D-galactose), and 2-keto-D-xylose (D-threopentos-2-ulose, 2-dehydro-D-xylose), respectively. Pyranose oxidase has significant activity with carbohydrates such as, L-sorbose, D-glucono-1,5-lactone, and D-allose. When pyranose oxidase catalyzes the oxidation of aldopyranoses, electrons are transferred to molecular oxygen which results in the formation of hydrogen peroxide.
Abbr
P2O, Recombinant (E. coli)
Appearance
Yellow lyophilizate
Enzyme Commission Number
EC 1.1.3.10
Activity
> 3 U/mg lyophilizate
Molecular Weight
ca. 290 kDa
Michaelis Constant
7.4 x 10^-4 M (D-glucose) 1.5 x 10^-2 M (1,5-anhydroglucitol)
Structure
4 subunits of 64 kDa (SDS-PAGE)
Specificity
D-glucose (100), 1,5-anhydroglucitol (22)
Unit Definition
One unit (U) is defined as the amount of enzyme which produces 1 μmol of hydrogen peroxide per min at 37°C and pH 7.0.
Thermal stability
below 55°C
Synonyms
pyranose oxidase; EC 1.1.3.10; glucose 2-oxidase; pyranose-2-oxidase; 37250-80-9; P2O
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