Adaptation to sulfonamide resistance in Neisseria meningitidis may have required compensatory changes to retain enzyme function: kinetic analysis of dihydropteroate synthases from N. meningitidis expressed in a knockout mutant of Escherichia coli.

@article{Fermr1997AdaptationTS,
  title={Adaptation to sulfonamide resistance in Neisseria meningitidis may have required compensatory changes to retain enzyme function: kinetic analysis of dihydropteroate synthases from N. meningitidis expressed in a knockout mutant of Escherichia coli.},
  author={Christian Ferm{\'e}r and G{\"o}te Swedberg},
  journal={Journal of bacteriology},
  year={1997},
  volume={179 3},
  pages={831-7}
}
Previously, the effects of three point mutations (at amino acid positions 31, 84, and 194) in the gene coding for a sulfonamide-resistant dihydropteroate synthase of Neisseria meningitidis were analyzed by site-directed mutagenesis. Changes at positions 31 and 194 abolished the phenotypic expression of sulfonamide resistance, while a change at position 84 appeared to be neutral. These studies are here extended to correlate the alterations in phenotype with effects on enzyme kinetics by… CONTINUE READING

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