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ENZYME entry: EC 1.1.5.2

Accepted Name
Quinoprotein glucose dehydrogenase (PQQ, quinone).
Alternative Name(s)
D-glucose:(pyrroloquinoline-quinone) 1-oxidoreductase.
Glucose dehydrogenase (PQQ-dependent).
Glucose dehydrogenase (pyrroloquinoline-quinone).
Quinoprotein D-glucose dehydrogenase.
Reaction catalysed
D-glucose + ubiquinone <=> D-glucono-1,5-lactone + ubiquinol
Cofactor(s)
Ca(2+) or Mg(2+); Pyrroloquinoline quinone.
Comment(s)
  • Integral membrane protein containing PQQ as prosthetic group.
  • It also contains bound ubiquinone and Mg(2+) or Ca(2+).
  • Electron acceptor is membrane ubiquinone but usually assayed with phenazine methosulfate.
  • Like in all other quinoprotein alcohol dehydrogenases the catalytic domain has an 8-bladed 'propeller' structure.
  • It occurs in a wide range of bacteria.
  • Catalyzes a direct oxidation of the pyranose form of D-glucose to the lactone and thence to D-gluconate in the periplasm.
  • Oxidizes other monosaccharides including the pyranose forms of pentoses.
  • Formerly EC 1.1.99.17.
Cross-references
PROSITEPDOC00375
BRENDA1.1.5.2
EC2PDB1.1.5.2
ExplorEnz1.1.5.2
PRIAM enzyme-specific profiles1.1.5.2
KEGG Ligand Database for Enzyme Nomenclature1.1.5.2
IUBMB Enzyme Nomenclature1.1.5.2
IntEnz1.1.5.2
MEDLINEFind literature relating to 1.1.5.2
MetaCyc1.1.5.2
UniProtKB/Swiss-Prot
P13650, DHGB_ACICA;  P15877, DHG_ECOLI;  P27175, DHG_GLUOX;  

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All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.1.5.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-