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P4234

Sigma-Aldrich

Pyranose Oxidase from Coriolus sp.

recombinant, expressed in E. coli, ≥2.7 units/mg solid

Synonym(s):

Pyranose: Oxygen 2-Oxidoreductase

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in E. coli

form

powder

specific activity

≥2.7 units/mg solid

shipped in

wet ice

storage temp.

−20°C

General description

Pyranose oxidase (P2O), a homotetrameric protein consists of a covalently bound flavin adenine dinucleotide (FAD). It is seen mostly among wood-degrading basidiomycetes.

Application

Pyranose Oxidase from Coriolus sp. has been used in the enzymatic oxidation of D-glucose (DG). It has also been used as a component in oxygen scavenging system (OSS) to increase the lifetime of the fluorophores.

Biochem/physiol Actions

Pyranose oxidase (P2O) can be used in clinical chemistry to determine 1,5-anhydro-d-glucitol marker, used for glycemic control in diabetes patients.
Pyranose oxidase (P2O) catalyzes the oxidation of aldopyranoses at position C-2 to yield the corresponding 2-ketoaldoses. 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.

Unit Definition

One unit produces 1.0 μmol of hydrogen peroxide per minute at 37 °C, pH 7.0.

Other Notes

Contains glutamate

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Purification and Characterization of Pyranose Oxidase from the White Rot Fungus Trametes multicolor
Leitner C, et al.
Applied and Environmental Microbiology, 67(8), 3636-3636 (2001)
Tien-Chye Tan et al.
Journal of molecular biology, 402(3), 578-594 (2010-08-17)
Flavoenzymes perform a wide range of redox reactions in nature, and a subclass of flavoenzymes carry covalently bound cofactor. The enzyme-flavin bond helps to increase the flavin's redox potential to facilitate substrate oxidation in several oxidases. The formation of the
C Leitner et al.
Applied and environmental microbiology, 67(8), 3636-3644 (2001-07-27)
We purified an intracellular pyranose oxidase from mycelial extracts of the white rot fungus Trametes multicolor by using ammonium sulfate fractionation, hydrophobic interaction, ion-exchange chromatography, and gel filtration. The native enzyme has a molecular mass of 270 kDa as determined
Tien-Chye Tan et al.
Journal of molecular biology, 409(4), 588-600 (2011-04-26)
Trametes multicolor pyranose 2-oxidase (P2O) is a flavoprotein oxidase that oxidizes d-glucose at C2 to 2-keto-d-glucose by a highly regioselective mechanism. In this work, fluorinated sugar substrates were used as mechanistic probes to investigate the basis of regioselectivity in P2O.
Mor R Alkaslasi et al.
Nature communications, 12(1), 2471-2471 (2021-05-02)
In vertebrates, motor control relies on cholinergic neurons in the spinal cord that have been extensively studied over the past hundred years, yet the full heterogeneity of these neurons and their different functional roles in the adult remain to be

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