Quinoprotein glucose dehydrogenase

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Quinoprotein glucose dehydrogenase
EC number1.1.5.2
CAS number81669-60-5
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum

In enzymology, a quinoprotein glucose dehydrogenase (EC 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.


Further reading[edit]

  • Ameyama M, Nonobe M, Hayashi M, Shinagawa E, Matsushita K, Adachi O (1985). "Mode of binding of pyrroloquinoline quinone to apo-glucose dehydrogenase". Agric. Biol. Chem. 49 (4): 1227–1231. doi:10.1271/bbb1961.49.1227.
  • Duine JA, Frank J, van Zeeland JK (December 1979). "Glucose dehydrogenase from Acinetobacter calcoaceticus: a 'quinoprotein'". FEBS Letters. 108 (2): 443–6. doi:10.1016/0014-5793(79)80584-0. PMID 520586.
  • Yamada M, Sumi K, Matsushita K, Adachi O, Yamada Y (June 1993). "Topological analysis of quinoprotein glucose dehydrogenase in Escherichia coli and its ubiquinone-binding site". The Journal of Biological Chemistry. 268 (17): 12812–7. PMID 8509415.
  • Dewanti AR, Duine JA (May 1998). "Reconstitution of membrane-integrated quinoprotein glucose dehydrogenase apoenzyme with PQQ and the holoenzyme's mechanism of action". Biochemistry. 37 (19): 6810–8. doi:10.1021/bi9722610. PMID 9578566.
  • Oubrie A, Rozeboom HJ, Dijkstra BW (October 1999). "Active-site structure of the soluble quinoprotein glucose dehydrogenase complexed with methylhydrazine: a covalent cofactor-inhibitor complex". Proceedings of the National Academy of Sciences of the United States of America. 96 (21): 11787–91. doi:10.1073/pnas.96.21.11787. PMC 18364. PMID 10518528.
  • Elias M, Tanaka M, Sakai M, Toyama H, Matsushita K, Adachi O, Yamada M (December 2001). "C-terminal periplasmic domain of Escherichia coli quinoprotein glucose dehydrogenase transfers electrons to ubiquinone". The Journal of Biological Chemistry. 276 (51): 48356–61. doi:10.1074/jbc.M107355200. PMID 11604400.