Pyranose oxidase
From Proteopedia
Jump to navigationJump to search
| ||||||||||||
3D Structures of pyranose oxidase
Updated on 23-August-2026
FunctionPyranose oxidase or pyranose 2-oxidase (P2O) or C-glucosyl oxidoreductase catalyzes the conversion of D-glucose and molecular oxygen to 2-dehydro-D-glucose and H2O2. It is abundant in lignin-degrading white rot fungi. P2O is a tetramer flavoprotein containing the prosthetic group FAD in each monomer. P2O oxidizes several aldopyranoses with the preferred electron donors being D-glucose, D-xylose and D-sorbose[1]. RelevanceConverting common sugars and sugar derivatives with P2O provides a pool of sugar-derived intermediates for the synthesis of rare sugars, fine chemicals and drugs. Structural highlightsThe active site of P2O is gated by a highly conserved loop which determines the substrate specificity. Water molecules are shown as red spheres. The active site contains the FAD cofactor[2].
| ||||||||||||
Updated on 23-August-2026
This page was last modified 07:49, 23 August 2026.