Biology:Soluble quinoprotein glucose dehydrogenase

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Soluble quinoprotein glucose dehydrogenase
Identifiers
EC number1.1.99.35
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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 [math]\displaystyle{ \rightleftharpoons }[/math] 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. "Crystalline quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus". Biochemistry 25: 6043–6048. 1986. doi:10.1021/bi00368a031. 
  2. "Purification and characterization of quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus L.M.D. 79.41". The Biochemical Journal 239 (1): 163–7. October 1986. PMID 3800975. 
  3. "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. May 1988. PMID 2834325. 
  4. "Quinoprotein D-glucose dehydrogenase of the Acinetobacter calcoaceticus respiratory chain: membrane-bound and soluble forms are different molecular species". Biochemistry 28 (15): 6276–80. July 1989. doi:10.1021/bi00441a020. PMID 2551369. 
  5. "Structural requirements of pyrroloquinoline quinone dependent enzymatic reactions". Protein Science 9 (7): 1265–73. July 2000. doi:10.1110/ps.9.7.1265. 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. 

External links