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Soluble quinoprotein glucose dehydrogenase

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Soluble quinoprotein glucose dehydrogenase
Identifiers
EC no.1.1.99.35
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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

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  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.
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