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Sorbitol metabolism in Aerobacter aerogenes.
Journal of Bacteriology
|January 1, 1971
Summary
Aerobacter aerogenes PRL-R3 metabolizes sorbitol using a pathway involving sorbitol 6-phosphate. Key enzymes, sorbitol 6-phosphate dehydrogenase and a phosphoenolpyruvate-dependent phosphotransferase system, are essential for this sorbitol metabolism.
Area of Science:
- Microbial metabolism
- Biochemistry
- Enzymology
Background:
- Sorbitol (d-glucitol) is a sugar alcohol utilized by various microorganisms.
- Understanding the specific metabolic pathways is crucial for microbial physiology and biotechnology.
Purpose of the Study:
- To elucidate the sorbitol metabolism pathway in Aerobacter aerogenes PRL-R3.
- To identify the key enzymes involved in sorbitol phosphorylation and oxidation.
Main Methods:
- Enzyme assays to determine phosphorylation and oxidation activities.
- Isolation and characterization of Aerobacter aerogenes PRL-R3 mutants.
- Growth studies of wild-type and mutant strains on sorbitol.
Main Results:
- Sorbitol metabolism proceeds via sorbitol --> sorbitol 6-phosphate --> d-fructose 6-phosphate.
- Phosphoenolpyruvate (PEP):sorbitol 6-phosphotransferase system mediates sorbitol phosphorylation.
- A pyridine-nucleotide-linked dehydrogenase oxidizes sorbitol 6-phosphate.
- Mutants lacking sorbitol 6-phosphate dehydrogenase or phosphotransferase enzyme I failed to grow on sorbitol.
Conclusions:
- The identified pathway and enzymes are critical for Aerobacter aerogenes PRL-R3 growth on sorbitol.
- PEP is the essential phosphate donor for sorbitol phosphorylation, not ATP.