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P4234

Sigma-Aldrich

Pyranose Oxidase from Coriolus sp.

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

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Synonym(s):
Pyranose: Oxygen 2-Oxidoreductase
CAS Number:
Enzyme Commission number:
MDL number:
NACRES:
NA.54

recombinant

expressed in E. coli

Quality Level

form

powder

specific activity

≥2.7 units/mg solid

shipped in

wet ice

storage temp.

−20°C

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P4105SAE0051G9637
vibrant-m

P4234

Pyranose Oxidase from Coriolus sp.

shipped in

wet ice

shipped in

-

shipped in

-

shipped in

-

form

powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

recombinant

expressed in E. coli

recombinant

-

recombinant

expressed in E. coli

recombinant

-

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

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

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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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
Oliver Spadiut et al.
The FEBS journal, 277(13), 2892-2909 (2010-06-10)
Pyranose 2-oxidase from Trametes multicolor is a 270 kDa homotetrameric enzyme that participates in lignocellulose degradation by wood-rotting fungi and oxidizes a variety of aldopyranoses present in lignocellulose to 2-ketoaldoses. The active site in pyranose 2-oxidase is gated by a
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.
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
Nicholas C Bauer et al.
The Journal of biological chemistry, 296, 100540-100540 (2021-03-17)
The functions of long noncoding (lnc)RNAs, such as MEG3, are defined by their interactions with other RNAs and proteins. These interactions, in turn, are shaped by their subcellular localization and temporal context. Therefore, it is important to be able to

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