Pyranose oxidase

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In enzymology, a pyranose oxidase (EC 1.1.3.10) is an enzyme that catalyzes the chemical reaction

D-glucose + O2 2-dehydro-D-glucose + H2O2

Thus, the two substrates of this enzyme are D-glucose and O2, whereas its two products are 2-dehydro-D-glucose and H2O2.

Pyranose oxidase is able to oxidize D-xylose, L-sorbose, D-galactose,[1] and D-glucono-1,5-lactone, which have the same ring conformation and configuration at C-2, C-3 and C-4.[2]

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is pyranose:oxygen 2-oxidoreductase. Other names in common use include glucose 2-oxidase, and pyranose-2-oxidase. This enzyme participates in pentose phosphate pathway. It employs one cofactor, FAD.

Structural studies

As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1TT0, 1TZL, 2F5V, 2F6C, 2IGK, 2IGM, 2IGN, and 2IGO.

Use in biosensors

Pyranose oxidase produce higher power output than does glucose oxidase. It is also easier to express in high yields using E. coli.[1]

References

Further reading

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