Quinoprotein glucose dehydrogenase
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Quinoprotein glucose dehydrogenase
| quinoprotein glucose dehydrogenase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| EC number | 1.1.5.2 | ||||||
| CAS number | 81669-60-5 | ||||||
| Databases | |||||||
| IntEnz | IntEnz view | ||||||
| BRENDA | BRENDA entry | ||||||
| ExPASy | NiceZyme view | ||||||
| KEGG | KEGG entry | ||||||
| MetaCyc | metabolic pathway | ||||||
| PRIAM | profile | ||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||
| Gene Ontology | AmiGO / EGO | ||||||
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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
- and Adachi O (1985). "Mode of binding of pyrroloquinoline quinone to apo-glucose dehydrogenase". Agric. Biol. Chem. 49: 1227–1231.
- Duine JA, Frank J, van Zeeland JK (1979). "Glucose dehydrogenase from Acinetobacter calcoaceticus: a 'quinoprotein'". FEBS. Lett. 108 (2): 443–6. doi:10.1016/0014-5793(79)80584-0. 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 (17): 12812–7. 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 (19): 6810–8. doi:10.1021/bi9722610. 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 (21): 11787–91. doi:10.1073/pnas.96.21.11787. PMC 18364. PMID 10518528. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=18364.
- M; Tanaka, M; Sakai, M; Toyama, H; Matsushita, K; Adachi, O; Yamada, M (2001). "C-terminal periplasmic domain of Escherichia coli quinoprotein glucose dehydrogenase transfers electrons to ubiquinone". J. Biol. Chem. 276 (51): 48356–61. doi:10.1074/jbc.M107355200. PMID 11604400.
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