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Glucose dehydrogenase activity in Acinetobacter species
1Unité des Entérobactéries, Institut Pasteur, Paris.
Research in Microbiology
|October 1, 1989
Summary
This study investigated D-glucose oxidation in Acinetobacter species, revealing that glucose dehydrogenase (GDH) activity varies significantly. The findings challenge the old taxonomic scheme and highlight the need for modern identification methods like carbon source utilization tests.
Area of Science:
- Microbiology
- Biochemistry
- Taxonomy
Background:
- Acinetobacter species exhibit diverse metabolic capabilities.
- D-glucose oxidation is a key metabolic characteristic.
- Previous taxonomic classifications relied on limited metabolic data.
Purpose of the Study:
- To investigate D-glucose oxidation by Acinetobacter species.
- To characterize the glucose dehydrogenase (GDH) enzyme involved.
- To evaluate the utility of glucose oxidation for Acinetobacter taxonomy.
Main Methods:
- Studied 14C-glucose oxidation kinetics in non-proliferating cells.
- Separated oxidation products using DEAE-cellulose paper chromatography.
- Assessed GDH activity through inhibition studies with various carbohydrates and pyrroloquinoline quinone (PQQ).
Main Results:
- Glucose oxidation is primarily mediated by membrane-bound GDH.
- Two groups of Acinetobacter strains were identified based on GDH affinity for glucose.
- PQQ addition restored GDH activity in many, but not all, glucose-non-oxidizing strains, indicating variability in enzyme function.
Conclusions:
- The traditional taxonomic scheme for Acinetobacter based solely on glucose oxidation is inadequate.
- Glucose oxidation patterns are inconsistent across Acinetobacter species.
- Modern identification methods, such as carbon source utilization tests, are essential for accurate Acinetobacter species-level identification.