Pyranose oxidase


In enzymology, a pyranose oxidase is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are D-glucose and oxygen. Its products are glucosone and hydrogen peroxide.
Pyranose oxidase is able to oxidize D-xylose, L-sorbose, D-galactose, and D-glucono-1,5-lactone, which have the same ring conformation and configuration at C-2, C-3 and C-4. It can use oxygen, but also ferrocene ions, quinones and 2,6-dichlorophenolindophenol as oxidizers.
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,,,,,,, and.

Use in biosensors

Recently, pyranose oxidase has been gaining on popularity within biosensors. Unlike glucose oxidase, it can produce higher power output, given that it is not glycosylated, has more favorable value of Michaelis-Menten constants, and can catalytically convert both anomers of glucose. It reacts with a wider range of substrates. Pyranose oxidase does not cause an unwanted pH shift. It is also possible to easily express and produce it in high yields using E. coli.