Quinoprotein glucose dehydrogenase
| Quinoprotein glucose dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.5.2 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
In enzymology, quinoprotein glucose dehydrogenase (EC 1.1.5.2) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are D-glucose and the cofactor ubiquinone. Its products are glucono-δ-lactone and ubiquinol.[1][2][3][4]
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
- ^ Enzyme 1.1.5.2 at KEGG Pathway Database.
- ^ Duine JA, Frank J, van Zeeland JK (December 1979). "Glucose dehydrogenase from Acinetobacter calcoaceticus: a 'quinoprotein'". FEBS Letters. 108 (2): 443–6. Bibcode:1979FEBSL.108..443D. 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. doi:10.1016/S0021-9258(18)31460-1. 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.
Further reading
- 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.
- 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. Bibcode:1999PNAS...9611787O. 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.