glucose 1-dehydrogenase (PQQ, quinone);
quinoprotein glucose dehydrogenase;
membrane-bound glucose dehydrogenase;
mGDH;
glucose dehydrogenase (PQQ-dependent);
glucose dehydrogenase (pyrroloquinoline-quinone);
quinoprotein D-glucose dehydrogenase

Oxidoreductases;
Acting on the CH-OH group of donors;
With a quinone or similar compound as acceptor

D-glucose:ubiquinone oxidoreductase

D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol [RN:R06620]

R06620

D-glucose [CPD:C00031];
ubiquinone [CPD:C00399]

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.

1  [PMID:8509415]

Yamada M, Sumi K, Matsushita K, Adachi O, Yamada Y.

Topological analysis of quinoprotein glucose dehydrogenase in Escherichia coli and its ubiquinone-binding site.

J. Biol. Chem. 268 (1993) 12812-7.

Escherichia coli [GN:eco]

2  [PMID:9578566]

Dewanti AR, Duine JA.

Reconstitution of membrane-integrated quinoprotein glucose dehydrogenase apoenzyme with PQQ and the holoenzyme's mechanism of action.

Biochemistry. 37 (1998) 6810-8.

Acinetobacter calcoaceticus

3  [PMID:520586]

Duine JA, Frank J, van Zeeland JK.

Glucose dehydrogenase from Acinetobacter calcoaceticus: a 'quinoprotein'.

FEBS. Lett. 108 (1979) 443-6.

Acinetobacter calcoaceticus

4  [PMID:6793395]

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 (1981) 179-83.

5  [PMID:8554505]

Cozier GE, Anthony C

Structure of the quinoprotein glucose dehydrogenase of Escherichia coli modelled  on that of methanol dehydrogenase from Methylobacterium extorquens.

Biochem. J. 312 ( Pt 3) (1995) 679-85.

6  [PMID:10359647]

Cozier GE, Salleh RA, 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 ( Pt 3) (1999) 639-47.

7  [PMID:11604400]

Elias M, Tanaka M, Sakai M, Toyama H, Matsushita K, Adachi O, Yamada M.

C-terminal periplasmic domain of Escherichia coli quinoprotein glucose dehydrogenase transfers electrons to ubiquinone.

J. Biol. Chem. 276 (2001) 48356-61.

Escherichia coli [GN:eco]

8  [PMID:12686133]

James PL, Anthony C

The metal ion in the active site of the membrane glucose dehydrogenase of Escherichia coli.

Biochim. Biophys. Acta. 1647 (2003) 200-5.

9  [PMID:14612441]

Elias MD, Nakamura S, Migita CT, 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 (2004) 3078-83.

10 [PMID:18550551]

Mustafa G, Ishikawa Y, Kobayashi K, Migita CT, Elias MD, 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 (2008) 22215-21.