Quinoprotein glucose dehydrogenase

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In enzymology, a quinoprotein glucose dehydrogenase (EC 1.1.5.2) is an enzyme that catalyzes the chemical reaction

D-glucose + ubiquinone D-glucono-1,5-lactone + ubiquinol

Thus, the two substrates of this enzyme are D-glucose and ubiquinone, whereas its two products are D-glucono-1,5-lactone and ubiquinol.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a quinone or similar compound as acceptor. The systematic name of this enzyme class is D-glucose:ubiquinone oxidoreductase. Other names in common use include D-glucose:(pyrroloquinoline-quinone) 1-oxidoreductase, glucose dehydrogenase (PQQ-dependent), glucose dehydrogenase (pyrroloquinoline-quinone), and quinoprotein D-glucose dehydrogenase. This enzyme participates in pentose phosphate pathway. It employs one cofactor, PQQ.

References

  • IUBMB entry for 1.1.5.2
  • BRENDA references for 1.1.5.2 (Recommended.)
  • PubMed references for 1.1.5.2
  • PubMed Central references for 1.1.5.2
  • Google Scholar references for 1.1.5.2
  • and Adachi O (1985). "Mode of binding of pyrroloquinoline quinone to apo-glucose dehydrogenase". Agric. Biol. Chem. 49: 1227&ndash, 1231.
  • Duine JA, Frank J, van Zeeland JK (1979). "Glucose dehydrogenase from Acinetobacter calcoaceticus: a 'quinoprotein'". FEBS. Lett. 108: 443&ndash, 6. PMID 520586.
  • Yamada M, Sumi K, Matsushita K, Adachi O, Yamada Y (1993). "Topological analysis of quinoprotein glucose dehydrogenase in Escherichia coli and its ubiquinone-binding site". J. Biol. Chem. 268: 12812&ndash, 7. PMID 8509415.
  • Dewanti AR, Duine JA (1998). "Reconstitution of membrane-integrated quinoprotein glucose dehydrogenase apoenzyme with PQQ and the holoenzyme's mechanism of action". Biochemistry. 37: 6810&ndash, 8. PMID 9578566.
  • Oubrie A, Rozeboom HJ, Dijkstra BW (1999). "Active-site structure of the soluble quinoprotein glucose dehydrogenase complexed with methylhydrazine: a covalent cofactor-inhibitor complex". Proc. Natl. Acad. Sci. U. S. A. 96: 11787&ndash, 91. PMID 10518528.
  • M (2001). "C-terminal periplasmic domain of Escherichia coli quinoprotein glucose dehydrogenase transfers electrons to ubiquinone". J. Biol. Chem. 276: 48356&ndash, 61. PMID 11604400.

External links

The CAS registry number for this enzyme class is 81669-60-5.

Gene Ontology (GO) codes

Template:1.1-enzyme-stub


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