||Soluble periplasmic enzyme containing a tightly-bound PQQ cofactor that is bound to a calcium ion. As the electron acceptor is not known, the enzyme has been assayed with Wurster's Blue or phenazine methosulfate. It has negligible sequence or structure similarity to other quinoproteins. It catalyses an exceptionally high rate of oxidation of a wide range of aldose sugars, including D-glucose, galactose, arabinose and xylose, and also the disaccharides lactose, cellobiose and maltose. It has been described only in Acinetobacter calcoaceticus.
||Geiger, O. and Gorisch, H. Crystalline quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus. Biochemistry 25 (1986) 6043–6048.
||Dokter, P., Frank, J. and Duine, J.A. Purification and characterization of quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus L.M.D. 79.41. Biochem. J. 239 (1986) 163–167. [PMID: 3800975]
||Cleton-Jansen, A.M., Goosen, N., Wenzel, T.J. and van de Putte, P. Cloning of the gene encoding quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus: evidence for the presence of a second enzyme. J. Bacteriol. 170 (1988) 2121–2125. [DOI] [PMID: 2834325]
||Matsushita, K., Shinagawa, E., Adachi, O. and Ameyama, M. Quinoprotein D-glucose dehydrogenase of the Acinetobacter calcoaceticus respiratory chain: membrane-bound and soluble forms are different molecular species. Biochemistry 28 (1989) 6276–6280. [PMID: 2551369]
||Oubrie, A. and Dijkstra, B.W. Structural requirements of pyrroloquinoline quinone dependent enzymatic reactions. Protein Sci. 9 (2000) 1265–1273. [DOI] [PMID: 10933491]
||Matsushita, K., Toyama, H., Ameyama, M., Adachi, O., Dewanti, A. and Duine, J.A. Soluble and membrane-bound quinoprotein D-glucose dehydrogenases of the Acinetobacter calcoaceticus : the binding process of PQQ to the apoenzymes. Biosci. Biotechnol. Biochem. 59 (1995) 1548–1555.