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Related Experiment Videos

D-Mannitol utilization in Salmonella typhimurium.

D Berkowitz

    Journal of Bacteriology
    |January 1, 1971
    PubMed
    Summary
    This summary is machine-generated.

    Salmonella typhimurium metabolizes d-mannitol via phosphorylation and conversion to fructose-6-phosphate. Mutants lacking key enzymes show sensitivity to mannitol, highlighting its role in bacterial physiology.

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    Area of Science:

    • Biochemistry
    • Microbiology
    • Genetics

    Background:

    • D-mannitol metabolism is crucial for bacterial survival and energy production.
    • Understanding these pathways in Salmonella typhimurium provides insights into microbial physiology.

    Purpose of the Study:

    • To biochemically and genetically analyze d-mannitol metabolism in Salmonella typhimurium.
    • To characterize d-mannitol mutants and their associated phenotypes.

    Main Methods:

    • Biochemical assays to determine enzyme activity.
    • Genetic mapping to locate mutations on the Salmonella chromosome.
    • Phenotypic analysis of bacterial growth and viability in the presence of d-mannitol.

    Main Results:

    Related Experiment Videos

  • D-mannitol is phosphorylated by the phosphoenolpyruvate-dependent phosphotransferase system.
  • Mannitol-1-phosphate dehydrogenase converts d-mannitol-1-phosphate to d-fructose-6-phosphate.
  • Mutants lacking mannitol-1-phosphate dehydrogenase exhibit sensitivity to d-mannitol, including growth inhibition or cell lysis.
  • Expression of mannitol genes in adenyl cyclase-deficient strains requires cyclic adenosine-3',5'-monophosphate.

    • Conclusions:

    • The phosphoenolpyruvate-dependent phosphotransferase system and mannitol-1-phosphate dehydrogenase are key components of d-mannitol metabolism in Salmonella typhimurium.
    • Defects in these pathways lead to d-mannitol sensitivity, underscoring the importance of this metabolic route.
    • Cyclic adenosine-3',5'-monophosphate plays a regulatory role in the expression of mannitol metabolism genes.