The in vivo and in vitro substrate specificity of quinoprotein glucose dehydrogenase of Acinetobacter calcoaceticus LMD79.41

P. Dokter, Jack Pronk, B.J. van Schie, J.P. van Dijken, J.A. Duine*

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

23 Citations (Scopus)

Abstract

Quinoprotein glucose dehydrogenase (GDH; EC 1.1.99.17) was partially purified from cell-free extracts of Acinetobacter calcoaceticus LMD79.41. The enzyme oxidized monosaccharides (d-glucose, d-allose, 2-deoxy-d-glucose, d-galactose, d-mannose, d-xylose, d-ribose and l-arabinose) as well as disaccharides (d-lactose, d-maltose and d-cellobiose).

Intact cells of A. calcoaceticus LMD79.41 also oxidized these monosaccharides, but not the disaccharides.

The difference in substrate specificity can not be explained by impermeability of the outer membrane for disaccharides, since right-side-out membrane vesicles did not oxidize disaccharides either. Destruction of the cytoplasmic membrane strongly affected the catalytic properties of GDH. Not only did the affinity towards some monosaccharides change substantially, but disaccharides also became good substrates upon solubilization of the enzyme. Thus, at least in A. calcoaceticus LMD79.41, the oxidation of disaccharides by GDH can be considered as an in vitro ‘artefact’ caused by the removal of the enzyme from its natural environment.
Original languageEnglish
Pages (from-to)195-200
JournalFEMS Microbiology Letters
Volume43
Issue number2
DOIs
Publication statusPublished - 1987

Keywords

  • Acinetobacter calcoaceticus
  • Glucose dehydrogenase
  • Quinoprotein
  • (Substrate specificity)

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