Insights into the molecular basis for the carbenicillinase activity of PSE-4 beta-lactamase from crystallographic and kinetic studies.

@article{Lim2001InsightsIT,
  title={Insights into the molecular basis for the carbenicillinase activity of PSE-4 beta-lactamase from crystallographic and kinetic studies.},
  author={Daniel V. Lim and François Sanschagrin and Leah V. Passmore and Liza H de Castro and Roger C. L{\'e}vesque and Natalie C. J. Strynadka},
  journal={Biochemistry},
  year={2001},
  volume={40 2},
  pages={395-402}
}
PSE-4 is a class A beta-lactamase produced by strains of Pseudomonas aeruginosa and is highly active for the penicillin derivative carbenicillin. The crystal structure of the wild-type PSE-4 carbenicillinase has been determined to 1.95 A resolution by molecular replacement and represents the first structure of a carbenicillinase published to date. A superposition of the PSE-4 structure with that of TEM-1 shows a rms deviation of 1.3 A for 263 Calpha atoms. Most carbenicillinases are unique… CONTINUE READING

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