Quinoprotein glucose dehydrogenase explained
| Quinoprotein glucose dehydrogenase |
| Ec Number: | 1.1.5.2 |
| Cas Number: | 81669-60-5 |
In enzymology, a quinoprotein glucose dehydrogenase 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
- 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 . 10.1271/bbb1961.49.1227. free .
- Duine JA, Frank J, van Zeeland JK . Glucose dehydrogenase from Acinetobacter calcoaceticus: a 'quinoprotein' . FEBS Letters . 108 . 2 . 443–6 . December 1979 . 520586 . 10.1016/0014-5793(79)80584-0 . free . 1979FEBSL.108..443D .
- Yamada M, Sumi K, Matsushita K, Adachi O, Yamada Y . Topological analysis of quinoprotein glucose dehydrogenase in Escherichia coli and its ubiquinone-binding site . The Journal of Biological Chemistry . 268 . 17 . 12812–7 . June 1993 . 10.1016/S0021-9258(18)31460-1 . 8509415 . free .
- Dewanti AR, Duine JA . Reconstitution of membrane-integrated quinoprotein glucose dehydrogenase apoenzyme with PQQ and the holoenzyme's mechanism of action . Biochemistry . 37 . 19 . 6810–8 . May 1998 . 9578566 . 10.1021/bi9722610 .
- Oubrie A, Rozeboom HJ, Dijkstra BW . 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 . October 1999 . 10518528 . 18364 . 10.1073/pnas.96.21.11787 . 1999PNAS...9611787O . free .
- Elias M, Tanaka M, Sakai M, Toyama H, Matsushita K, Adachi O, Yamada M . C-terminal periplasmic domain of Escherichia coli quinoprotein glucose dehydrogenase transfers electrons to ubiquinone . The Journal of Biological Chemistry . 276 . 51 . 48356–61 . December 2001 . 11604400 . 10.1074/jbc.M107355200 . free .
