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.
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
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SYSTEMATIC NAME
IUBMB Comments
D-glucose:ubiquinone oxidoreductase
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.
Matsushita, K.; Shinagawa, E.; Inoue, T.; Adachi, O.; Ameyama, M.
Immunological evidence for two types of PQQ-dependent D-glucose dehydrogenase in bacterial membranes and the location of the enzyme in Escherichia coli