Vinylglycolate resistance in Escherichia coli.

AUTOR(ES)

Shaw, L

RESUMO

Escherichia coli K-12 vinylglycolate-resistant mutants have been isolated and characterized. Two of the mutants, JSH 150 and JSH 151, have been determined to be double mutants, lacking both membrane-bound L-and D-lactate dehydrogenases. The lactate transport system is intact in all strains; both radioactive lactate and vinylglycolate are actively taken up. Likewise, the phosphoenolypyruvate-dependent phosphotransferase system for hexose uptake is active. Vinylglycolate, previously shown to inhibit the phosphoenolpyruvate-dependent phosphotransferase system, has very little effect in the double mutants. The extent of vinylglycolate inhibition in other mutants seems directly related to the activity of the lactate dehydrogenases. This indicates that vinylglycolate is oxidized to 2-keto-3-butenoate before inactivating the phosphoenolpyruvate-dependent phosphotransferase system. These results were found in whole cells and confirmed in isolated membrane vesicles.

Documentos Relacionados

• Fleroxacin resistance in Escherichia coli.
• Tiamulin resistance mutations in Escherichia coli.
• Mechanisms of acid resistance in enterohemorrhagic Escherichia coli.
• Plasmid-controlled resistance to copper in Escherichia coli.
• Gene amplification contributes to sulfonamide resistance in Escherichia coli.