EC 22.214.171.124 - Soluble quinoprotein glucose dehydrogenase
IntEnz Enzyme Nomenclature
glucose dehydrogenase (PQQ-dependent)
24540 [IUBMB]AAName origin: UniProt - CHECKED (C)Formula: R
Charge: 0ChEBI compound status: CHECKED (C)D-glucoseD-glucoseName origin: UniProt - CHECKED (C)Formula: C6H12O6
Charge: 0ChEBI compound status: CHECKED (C)=AH2AH2Name origin: UniProt - CHECKED (C)Formula: H2R
Charge: 0ChEBI compound status: CHECKED (C)
Soluble periplasmic enzyme containing PQQ as prosthetic group, bound to a calcium ion. Electron acceptor is not known. It is assayed with Wurster's Blue or phenazine methosulphate. 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.
Links to other databases
Crystalline quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus.Biochemistry 25: 6043-6048 (1986).
Purification and characterization of quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus L.M.D. 79.41.Biochem. J. 239: 163-167 (1986). [PMID: 3800975]
Cloning of the gene encoding quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus: evidence for the presence of a second enzyme.J. Bacteriol. 170: 2121-2125 (1988). [PMID: 2834325]
Quinoprotein D-glucose dehydrogenase of the Acinetobacter calcoaceticus respiratory chain: membrane-bound and soluble forms are different molecular species.Biochemistry 28: 6276-6280 (1989). [PMID: 2551369]
Structural requirements of pyrroloquinoline quinone dependent enzymatic reactions.Protein Sci. 9: 1265-1273 (2000). [PMID: 10933491]
Soluble and membrane-bound quinoprotein D-glucose dehydrogenases of the Acinetobacter calcoaceticus: the binding process of PQQ to the apoenzymes.Biosci. Biotechnol. Biochem. 59: 1548-1555 (1995).
[EC 126.96.36.199 created 2010]