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.
History
EC 1.1.99.35 created 2010
Reference
1
Authors
Geiger, O. and Gorisch, H.
Title
Crystalline quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus.
Quinoprotein D-glucose dehydrogenase of the Acinetobacter calcoaceticus respiratory chain: membrane-bound and soluble forms are different molecular species.