Soluble quinoprotein glucose dehydrogenase

Soluble quinoprotein glucose dehydrogenase (EC 1.1.99.35, soluble glucose dehydrogenase, sGDH, glucose dehydrogenase (PQQ-dependent)) is an enzyme with systematic name D-glucose:acceptor oxidoreductase.^[1]^[2]^[3]^[4]^[5]^[6] This enzyme catalyses the following chemical reaction

D-glucose + acceptor

\rightleftharpoons

D-glucono-1,5-lactone + reduced acceptor

This soluble periplasmic enzyme contains PQQ as prosthetic group, and is bound to a calcium ion. Electron acceptor is not known.

References

↑ Geiger, O.; Gorisch, H. (1986). "Crystalline quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus". Biochemistry. 25: 6043–6048. doi:10.1021/bi00368a031.
↑ Dokter, P.; Frank, J.; Duine, J.A. (1986). "Purification and characterization of quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus L.M.D. 79.41". Biochem. J. 239 (1): 163–167. PMC 1147254. PMID 3800975.
↑ Cleton-Jansen, A.M.; Goosen, N.; Wenzel, T.J.; van de Putte, P. (1988). "Cloning of the gene encoding quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus: evidence for the presence of a second enzyme". J. Bacteriol. 170 (5): 2121–2125. PMC 211095. PMID 2834325.
↑ Matsushita, K.; Shinagawa, E.; Adachi, O.; Ameyama, M. (1989). "Quinoprotein D-glucose dehydrogenase of the Acinetobacter calcoaceticus respiratory chain: membrane-bound and soluble forms are different molecular species". Biochemistry. 28 (15): 6276–6280. doi:10.1021/bi00441a020. PMID 2551369.
↑ Oubrie, A.; Dijkstra, B.W. (2000). "Structural requirements of pyrroloquinoline quinone dependent enzymatic reactions". Protein Sci. 9 (7): 1265–1273. doi:10.1110/ps.9.7.1265. PMC 2144678. PMID 10933491.
↑ Matsushita, K.; Toyama, H.; Ameyama, M.; Adachi, O.; Dewanti, A.; Duine, J.A. (1995). "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. doi:10.1271/bbb.59.1548.

External links

Soluble quinoprotein glucose dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH)

Oxidoreductases: alcohol oxidoreductases (EC 1.1)

1.1.1: NAD/NADP acceptor	3-hydroxyacyl-CoA dehydrogenase 3-hydroxybutyryl-CoA dehydrogenase Alcohol dehydrogenase Aldo-keto reductase 1A1 1B1 1B10 1C1 1C3 1C4 7A2 Aldose reductase Beta-Ketoacyl ACP reductase Carbohydrate dehydrogenases Carnitine dehydrogenase D-malate dehydrogenase (decarboxylating) DXP reductoisomerase Glucose-6-phosphate dehydrogenase Glycerol-3-phosphate dehydrogenase HMG-CoA reductase IMP dehydrogenase Isocitrate dehydrogenase Lactate dehydrogenase L-threonine dehydrogenase L-xylulose reductase Malate dehydrogenase Malate dehydrogenase (decarboxylating) Malate dehydrogenase (NADP+) Malate dehydrogenase (oxaloacetate-decarboxylating) Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) Phosphogluconate dehydrogenase Sorbitol dehydrogenase Hydroxysteroid dehydrogenase: 3 Beta 3-beta-HSD NSDHL 11 Beta HSD11B1 HSD11B2 17 Beta

1.1.2: cytochrome acceptor	D-lactate dehydrogenase (cytochrome) D-lactate dehydrogenase (cytochrome c-553) Mannitol dehydrogenase (cytochrome)

1.1.3: oxygen acceptor	Glucose oxidase L-gulonolactone oxidase Xanthine oxidase

1.1.4: disulfide as acceptor	Vitamin K epoxide reductase Vitamin-K-epoxide reductase (warfarin-insensitive)

1.1.5: quinone/similar acceptor	Malate dehydrogenase (quinone) Quinoprotein glucose dehydrogenase

1.1.99: other acceptors	Choline dehydrogenase L2HGDH

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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