Pyranose oxidase (POx) is an FAD-dependent oxidoreductase, and like glucose oxidase (GOx) it is a member of the glucose-methanol-choline (GMC) superfamily of oxidoreductases. POx oxidizes several monosaccharides including D-glucose, D-galactose, and D-xylose, while concurrently oxygen is reduced to hydrogen peroxide. In addition to this oxidase activity, POx shows pronounced activity with alternative electron acceptors that include various quinones or (complexed) metal ions. Even though POx in general shows properties that are more favourable than those of GOx (e.g., a considerably higher catalytic efficiency (kcat/Km) for D-glucose, significantly lower Michaelis constants Km for D-glucose, reactivity with both anomeric forms of D-glucose) it is much less frequently used for both biosensor and biofuel cell applications than GOx. POx has been applied in biosensing of D-glucose, D-galactose, and D-xylose, and in combination with α-glucosidase also maltose. An attractive application is in biosensors constructed for the measurement of 1,5-anhydro-D-glucitol, a recognised biomarker in diabetes. Bioelectrochemical applications of POx had been restricted to enzymes of fungal origin. The recent discovery and characterisation of POx from bacterial sources, which show properties that are very distinct from the fungal enzymes, might open new possibilities for further applications in bioelectrochemistry.