| pyranose oxidase | |
| Ec Number: | 1.1.3.10 |
| Cas Number: | 37250-80-9 |
| Go Code: | 0050233 |
| Width: | 270 |
In enzymology, a pyranose oxidase is an enzyme that catalyzes the chemical reaction
D-glucose + O2
\rightleftharpoons
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.
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes,,,,,,, and .
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.