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Related Experiment Videos

Vinylglycolate resistance in Escherichia coli.

L Shaw, F Grau, H R Kaback

    Journal of Bacteriology
    |March 1, 1975
    PubMed
    Summary

    Escherichia coli mutants resistant to vinylglycolate were identified. These mutants, lacking lactate dehydrogenases, show reduced inhibition by vinylglycolate, revealing its oxidation to 2-keto-3-butenoate.

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    Area of Science:

    • Microbiology
    • Biochemistry

    Background:

    • Vinylglycolate previously inhibited the phosphoenolpyruvate-dependent phosphotransferase system (PTS) in Escherichia coli.
    • The mechanism of vinylglycolate inhibition and its relationship with lactate metabolism were not fully understood.

    Purpose of the Study:

    • To isolate and characterize vinylglycolate-resistant mutants of Escherichia coli K-12.
    • To elucidate the mechanism by which vinylglycolate inhibits the phosphoenolpyruvate-dependent phosphotransferase system.

    Main Methods:

    • Isolation and characterization of vinylglycolate-resistant mutants.
    • Assays for lactate dehydrogenase activity, lactate and vinylglycolate transport, and hexose uptake via PTS.
    • Testing the effect of vinylglycolate on wild-type and mutant strains using whole cells and isolated membrane vesicles.

    Main Results:

    • Two double mutants (JSH 150, JSH 151) lacking both L- and D-lactate dehydrogenases were identified.
    • Lactate transport and hexose uptake via PTS remained functional in all isolated mutants.
    • Vinylglycolate exhibited significantly reduced inhibition in the double mutants compared to other strains.
    • The degree of vinylglycolate inhibition correlated with the activity of lactate dehydrogenases.

    Conclusions:

    • Vinylglycolate is oxidized to 2-keto-3-butenoate prior to inhibiting the phosphoenolpyruvate-dependent phosphotransferase system.
    • Lactate dehydrogenases play a crucial role in the activation or detoxification of vinylglycolate.
    • These findings provide new insights into the metabolic interactions and resistance mechanisms in Escherichia coli.

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