Jump to content

Soluble quinoprotein glucose dehydrogenase

From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by BrownHairedGirl (talk | contribs) at 15:27, 29 September 2019 (replace links to deleted portals: Portal:Molecular and Cellular BiologyPortal:Biology). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

Soluble quinoprotein glucose dehydrogenase
Identifiers
EC no.1.1.99.35
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

Soluble quinoprotein glucose dehydrogenase (EC 1.1.99.35, soluble glucose dehydrogenase, sGDH, glucose dehydrogenase (PQQ-dependent)) is an enzyme with systematic name D-glucose:acceptor oxidoreductase.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction

D-glucose + acceptor D-glucono-1,5-lactone + reduced acceptor

This soluble periplasmic enzyme contains PQQ as prosthetic group, and is bound to a calcium ion. Electron acceptor is not known.

References

  1. ^ Geiger O, Gorisch H (1986). "Crystalline quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus". Biochemistry. 25: 6043–6048. doi:10.1021/bi00368a031.
  2. ^ Dokter P, Frank J, Duine JA (October 1986). "Purification and characterization of quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus L.M.D. 79.41". The Biochemical Journal. 239 (1): 163–7. PMC 1147254. PMID 3800975.
  3. ^ Cleton-Jansen AM, Goosen N, Wenzel TJ, van de Putte P (May 1988). "Cloning of the gene encoding quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus: evidence for the presence of a second enzyme". Journal of Bacteriology. 170 (5): 2121–5. PMC 211095. PMID 2834325.
  4. ^ Matsushita K, Shinagawa E, Adachi O, Ameyama M (July 1989). "Quinoprotein D-glucose dehydrogenase of the Acinetobacter calcoaceticus respiratory chain: membrane-bound and soluble forms are different molecular species". Biochemistry. 28 (15): 6276–80. doi:10.1021/bi00441a020. PMID 2551369.
  5. ^ Oubrie A, Dijkstra BW (July 2000). "Structural requirements of pyrroloquinoline quinone dependent enzymatic reactions". Protein Science. 9 (7): 1265–73. doi:10.1110/ps.9.7.1265. PMC 2144678. PMID 10933491.
  6. ^ Matsushita, K.; Toyama, H.; Ameyama, M.; Adachi, O.; Dewanti, A.; Duine, J.A. (1995). "Soluble and membrane-bound quinoprotein D-glucose dehydrogenases of the Acinetobacter calcoaceticus : the binding process of PQQ to the apoenzymes". Biosci. Biotechnol. Biochem. 59: 1548–1555. doi:10.1271/bbb.59.1548.