EC - Quinoprotein glucose dehydrogenase (PQQ, quinone)

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IntEnz Enzyme Nomenclature


Accepted name:
quinoprotein glucose dehydrogenase (PQQ, quinone)
Other names:
D-glucose:(pyrroloquinoline-quinone) 1-oxidoreductase
glucose dehydrogenase (PQQ-dependent)
glucose dehydrogenase (pyrroloquinoline-quinone)
quinoprotein D-glucose dehydrogenase
membrane-bound glucose dehydrogenase
Systematic name:
D-glucose:ubiquinone oxidoreductase




Integral membrane protein containing PQQ as prosthetic group. It also contains bound ubiquinone and Mg2+ or Ca2+. 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. Catalyses 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.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00375
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008876
CAS Registry Number: 81669-60-5


  1. Yamada, M., Sumi, K., Matsushita, K., Adachi, O. and Yamada, Y.
    Topological analysis of quinoprotein glucose dehydrogenase in Escherichia coli and its ubiquinone-binding site.
    J. Biol. Chem. 268: 12812-12817 (1993). [PMID: 8509415]
  2. Dewanti, A.R. and Duine, J.A.
    Reconstitution of membrane-integrated quinoprotein glucose dehydrogenase apoenzyme with PQQ and the holoenzyme's mechanism of action.
    Biochemistry 37: 6810-6818 (1998). [PMID: 9578566]
  3. Duine, J.A., Frank, J. and Van Zeeland, J.K.
    Glucose dehydrogenase from Acinetobacter calcoaceticus: a 'quinoprotein'.
    FEBS Lett. 108: 443-446 (1979). [PMID: 520586]
  4. Ameyama, M., Matsushita, K., Ohno, Y., Shinagawa, E., Adachi, O.
    Existence of a novel prosthetic group, PQQ, in membrane-bound, electron transport chain-linked, primary dehydrogenases of oxidative bacteria.
    FEBS Lett. 130: 179-183 (1981). [PMID: 6793395]
  5. Cozier, G. E., Anthony, C.
    Structure of the quinoprotein glucose dehydrogenase of Escherichia coli modelled on that of methanol dehydrogenase from Methylobacterium extorquens.
    Biochem. J. 312: 679-685 (1995). [PMID: 8554505]
  6. Cozier, G. E., Salleh, R. A., Anthony, C.
    Characterization of the membrane quinoprotein glucose dehydrogenase from Escherichia coli and characterization of a site-directed mutant in which histidine-262 has been changed to tyrosine.
    Biochem. J. 340: 639-647 (1999). [PMID: 10359647]
  7. Elias, M.D., Tanaka, M., Sakai, M., Toyama, H., Matsushita, K., Adachi, O. and Yamada, M.
    C-terminal periplasmic domain of Escherichia coli quinoprotein glucose dehydrogenase transfers electrons to ubiquinone.
    J. Biol. Chem. 276: 48356-48361 (2001). [PMID: 11604400]
  8. James, P. L., Anthony, C.
    The metal ion in the active site of the membrane glucose dehydrogenase of Escherichia coli.
    Biochim. Biophys. Acta 1647: 200-205 (2003). [PMID: 12686133]
  9. Elias, M. D., Nakamura, S., Migita, C. T., Miyoshi, H., Toyama, H., Matsushita, K., Adachi, O., Yamada, M.
    Occurrence of a bound ubiquinone and its function in Escherichia coli membrane-bound quinoprotein glucose dehydrogenase.
    J. Biol. Chem. 279: 3078-3083 (2004). [PMID: 14612441]
  10. Mustafa, G., Ishikawa, Y., Kobayashi, K., Migita, C. T., Elias, M. D., Nakamura, S., Tagawa, S., Yamada, M.
    Amino acid residues interacting with both the bound quinone and coenzyme, pyrroloquinoline quinone, in Escherichia coli membrane-bound glucose dehydrogenase.
    J. Biol. Chem. 283: 22215-22221 (2008). [PMID: 18550551]

[EC created 1982 as, transferred 2003 to EC, modified 2010]