Pyranose dehydrogenase (acceptor)
Pyranose dehydrogenase (acceptor) (EC 1.1.99.29, pyranose dehydrogenase, pyranose-quinone oxidoreductase, quinone-dependent pyranose dehydrogenase, PDH) is an enzyme with systematic name pyranose:acceptor oxidoreductase.[1][2][3][4][5] This enzyme catalyses the following chemical reaction
- (1) a pyranose + acceptor
a pyranos-2-ulose (or a pyranos-3-ulose or a pyranos-2,3-diulose) + reduced acceptor
- (2) a pyranoside + acceptor
a pyranosid-3-ulose (or a pyranosid-3,4-diulose) + reduced acceptor
This enzyme requires FAD. A number of aldoses and ketoses in pyranose form, as well as glycosides, gluco-oligosaccharides, sucrose and lactose can act as a donor.
References
- ↑ Volc, J., Kubátová, E., Wood, D. and Daniel, G. (1997). "Pyranose 2-dehydrogenase, a novel sugar oxidoreductase from the basidiomycete fungus Agaricus bisporus". Arch. Microbiol. 167: 119–125. doi:10.1007/s002030050424. PMID 9042751.
- ↑ Volc, J., Sedmera, P., Halada, P., Pøikyrlová, V. and Daniel, G. (1998). "C-2 and C-3 oxidation of D-Glc, and C-2 oxidation of D-Gal by pyranose dehydrogenase from Agaricus bisporus". Carbohydr. Res. 310: 151–156. doi:10.1016/s0008-6215(98)00151-7.
- ↑ Volc, J., Sedmera, P., Halada, P., Pøikyrlová, V. and Haltrich, D. (2000). "Double oxidation of D-xylose to D-glycero-pentos-2,3-diulose (2,3-diketo-D-xylose) by pyranose dehydrogenase from the mushroom Agaricus bisporus". Carbohydr. Res. 329: 219–225. doi:10.1016/s0008-6215(00)00167-1. PMID 11086703.
- ↑ Volc, J., Kubátová, E., Daniel, G., Sedmera, P. and Haltrich, D. (2001). "Screening of basidiomycete fungi for the quinone-dependent sugar C-2/C-3 oxidoreductase, pyranose dehydrogenase, and properties of the enzyme from Macrolepiota rhacodes". Arch. Microbiol. 176: 178–186. doi:10.1007/s002030100308. PMID 11511865.
- ↑ Volc, J., Sedmera, P., Halada, P., Daniel, G., Pøikyrlová, V. and Haltrich, D. (2002). "C-3 oxidation of non-reducing sugars by a fungal pyranose dehydrogenase: spectral characterization". J. Mol. Catal., B Enzym. 17: 91–100. doi:10.1016/s1381-1177(02)00014-0.
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