Pyranose dehydrogenase (acceptor)

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Pyranose dehydrogenase (acceptor)
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EC no. 1.1.99.29
CAS no. 190606-21-4
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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.

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<span class="mw-page-title-main">NAD(P)H dehydrogenase (quinone)</span>

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D-xylose reductase (EC 1.1.1.307, XylR, XyrA, msXR, dsXR, monospecific xylose reductase, dual specific xylose reductase, NAD(P)H-dependent xylose reductase, xylose reductase) is an enzyme with systematic name xylitol:NAD(P)+ oxidoreductase. This enzyme catalyses the following chemical reaction

Crotonyl-CoA reductase (EC 1.3.1.86, butyryl-CoA dehydrogenase, butyryl dehydrogenase, unsaturated acyl-CoA reductase, ethylene reductase, enoyl-coenzyme A reductase, unsaturated acyl coenzyme A reductase, butyryl coenzyme A dehydrogenase, short-chain acyl CoA dehydrogenase, short-chain acyl-coenzyme A dehydrogenase, 3-hydroxyacyl CoA reductase, butanoyl-CoA:(acceptor) 2,3-oxidoreductase, CCR) is an enzyme with systematic name butanoyl-CoA:NADP+ 2,3-oxidoreductase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Medium-chain acyl-CoA dehydrogenase</span>

Medium-chain acyl-CoA dehydrogenase is an enzyme with systematic name medium-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">NADH:ubiquinone reductase (non-electrogenic)</span> Class of enzymes

NADH:ubiquinone reductase (non-electrogenic) (EC 1.6.5.9, NDH-2, ubiquinone reductase, coenzyme Q reductase, dihydronicotinamide adenine dinucleotide-coenzyme Q reductase, DPNH-coenzyme Q reductase, DPNH-ubiquinone reductase, NADH-coenzyme Q oxidoreductase, NADH-coenzyme Q reductase, NADH-CoQ oxidoreductase, NADH-CoQ reductase) is an enzyme with systematic name NADH:ubiquinone oxidoreductase. This enzyme catalyses the following chemical reaction:

Aldos-2-ulose dehydratase (EC 4.2.1.110, pyranosone dehydratase, AUDH, 1,5-anhydro-D-fructose dehydratase (microthecin-forming)) is an enzyme with systematic name 1,5-anhydro-D-fructose hydro-lyase (microthecin-forming). This enzyme catalyses the following chemical reaction

References

  1. Volc J, Kubatova E, Wood DA, Daniel G (March 1997). "Pyranose 2-dehydrogenase, a novel sugar oxidoreductase from the basidiomycete fungus Agaricus bisporus". Archives of Microbiology. 167 (2/3): 119–25. doi:10.1007/s002030050424. PMID   9042751.
  2. Volc J, Sedmera P, Halada P, Přikrylova V, 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.
  3. Volc J, Sedmera P, Halada P, Prikrylová V, Haltrich D (October 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". Carbohydrate Research. 329 (1): 219–25. doi:10.1016/s0008-6215(00)00167-1. PMID   11086703.
  4. Volc J, Kubátová E, Daniel G, Sedmera P, Haltrich D (September 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". Archives of Microbiology. 176 (3): 178–86. doi:10.1007/s002030100308. PMID   11511865.
  5. Volc J, Sedmera P, Halada P, Daniel G, Přikrylová V, 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.