KEGG   ENZYME: 1.1.3.10Help
Entry
EC 1.1.3.10                 Enzyme                                 

Name pyranose oxidase;
glucose 2-oxidase;
pyranose-2-oxidase
Class Oxidoreductases;
Acting on the CH-OH group of donors;
With oxygen as acceptor
BRITE hierarchy
Sysname pyranose:oxygen 2-oxidoreductase
Reaction(IUBMB) D-glucose + O2 = 2-dehydro-D-glucose + H2O2 [RN:R00302]
Reaction(KEGG) R00302
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Substrate D-glucose [CPD:C00031];
O2 [CPD:C00007]
Product 2-dehydro-D-glucose [CPD:C02779];
H2O2 [CPD:C00027]
Cofactor FAD [CPD:C00016]
Comment A flavoprotein (FAD). Also oxidizes D-xylose, L-sorbose and
D-glucono-1,5-lactone, which have the same ring conformation and
configuration at C-2, C-3 and C-4.
Structures PDB: 1TT0  1TZL  2F5V  2F6C  2IGK  2IGM  2IGN  2IGO  3BG6  3BG7  
     3BLY  3FDY  
Reference
  Authors
  Title

  Journal
  Organism
1  [PMID:5722278]
Janssen FW, Ruelius HW.
Carbohydrate oxidase, a novel enzyme from Polyporus obtusus. II.
Specificity and characterization of reaction products.
Biochim. Biophys. Acta. 167 (1968) 501-10.
Polyporus obtusu
Reference
  Authors
  Title

  Journal
2
Machida, Y. and Nakanishi, T.
Purification and properties of pyranose oxidase from Coriolus
versicolor.
Agric. Biol. Chem. 48 (1984) 2463-2470.
Reference
  Authors
  Title
  Journal
3
Neidleman, S.L., Amon, W.F., Jr. and Geigert, J.
Process for the production of fructose.
Chem. Abstr. 94 (1981) 20737.
Reference
  Authors
  Title

  Journal
  Organism
4  [PMID:5725162]
Ruelius HW, Kerwin RM, Janssen FW.
Carbohydrate oxidase, a novel enzyme from Polyporus obtusus. I.
Isolation and purification.
Biochim. Biophys. Acta. 167 (1968) 493-500.
Coriolus versicolor
Other DBs ExplorEnz - The Enzyme Database: 1.1.3.10
IUBMB Enzyme Nomenclature: 1.1.3.10
ExPASy - ENZYME nomenclature database: 1.1.3.10
BRENDA, the Enzyme Database: 1.1.3.10
CAS: 37250-80-9

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