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.
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.
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. PMID8509415.
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. PMID9578566.
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. PMID11604400.