Analysis of the plasticity of location of the Arg244 positive charge within the active site of the TEM-1 beta-lactamase.

@article{Marciano2009AnalysisOT,
  title={Analysis of the plasticity of location of the Arg244 positive charge within the active site of the TEM-1 beta-lactamase.},
  author={David C. Marciano and Nicholas Gene Brown and Timothy G. Palzkill},
  journal={Protein science : a publication of the Protein Society},
  year={2009},
  volume={18 10},
  pages={2080-9}
}
A large number of beta-lactamases have emerged that are capable of conferring bacterial resistance to beta-lactam antibiotics. Comparison of the structural and functional features of this family has refined understanding of the catalytic properties of these enzymes. An arginine residue present at position 244 in TEM-1 beta-lactamase interacts with the carboxyl group common to penicillin and cephalosporin antibiotics and thereby stabilizes both the substrate and transition state complexes. A… CONTINUE READING
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