In enzymology, a pyranose oxidase (EC 1.1.3.10) is an enzyme that catalyzes the chemical reaction
D-glucose + O2 ⇌ {\displaystyle \rightleftharpoons } 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, and D-glucono-1,5-lactone, which have the same ring conformation and configuration at C-2, C-3 and C-4. 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 PDB: 1TT0, PDB: 1TZL, PDB: 2F5V, PDB: 2F6C, PDB: 2IGK, PDB: 2IGM, PDB: 2IGN, and PDB: 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.
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