The Enzyme Database

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Accepted name: glucose 1-dehydrogenase (PQQ, quinone)
Reaction: D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
Other name(s): quinoprotein glucose dehydrogenase; membrane-bound glucose dehydrogenase; mGDH; glucose dehydrogenase (PQQ-dependent); glucose dehydrogenase (pyrroloquinoline-quinone); quinoprotein D-glucose dehydrogenase
Systematic name: D-glucose:ubiquinone oxidoreductase
Comments: Integral membrane protein containing PQQ as a cofactor. 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: BRENDA, EXPASY, KEGG, MetaCyc, PDB, 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 (1993) 12812–12817. [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 (1998) 6810–6818. [DOI] [PMID: 9578566]
3.  Duine, J.A., Frank, J. and Van Zeeland, J.K. Glucose dehydrogenase from Acinetobacter calcoaceticus: a 'quinoprotein'. FEBS Lett. 108 (1979) 443–446. [DOI] [PMID: 520586]
4.  Ameyama, M., Matsushita, K., Ohno, Y., Shinagawa, E. and Adachi, O. Existence of a novel prosthetic group, PQQ, in membrane-bound, electron transport chain-linked, primary dehydrogenases of oxidative bacteria. FEBS Lett. 130 (1981) 179–183. [DOI] [PMID: 6793395]
5.  Cozier, G.E. and Anthony, C. Structure of the quinoprotein glucose dehydrogenase of Escherichia coli modelled on that of methanol dehydrogenase from Methylobacterium extorquens. Biochem. J. 312 (1995) 679–685. [PMID: 8554505]
6.  Cozier, G.E., Salleh, R.A. and 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 (1999) 639–647. [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 (2001) 48356–48361. [DOI] [PMID: 11604400]
8.  James, P.L. and Anthony, C. The metal ion in the active site of the membrane glucose dehydrogenase of Escherichia coli. Biochim. Biophys. Acta 1647 (2003) 200–205. [DOI] [PMID: 12686133]
9.  Elias, M.D., Nakamura, S., Migita, C.T., Miyoshi, H., Toyama, H., Matsushita, K., Adachi, O. and Yamada, M. Occurrence of a bound ubiquinone and its function in Escherichia coli membrane-bound quinoprotein glucose dehydrogenase. J. Biol. Chem. 279 (2004) 3078–3083. [DOI] [PMID: 14612441]
10.  Mustafa, G., Ishikawa, Y., Kobayashi, K., Migita, C.T., Elias, M.D., Nakamura, S., Tagawa, S. and 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 (2008) 22215–22221. [DOI] [PMID: 18550551]
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