A secondary drug resistance mutation of TEM-1 beta-lactamase that suppresses misfolding and aggregation.

@article{Sideraki2001ASD,
  title={A secondary drug resistance mutation of TEM-1 beta-lactamase that suppresses misfolding and aggregation.},
  author={V Sideraki and Wei Huang and Timothy G. Palzkill and Hiram F. Gilbert},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2001},
  volume={98 1},
  pages={283-8}
}
In Gram-negative bacteria, TEM-1 beta-lactamase provides the major mechanism of plasmid-mediated beta-lactam resistance. Natural variants of TEM-1 with increased antibiotic resistance have appeared in response to the use of extended-spectrum beta-lactam antibiotics (e.g., ceftazidime) and beta-lactamase inhibitors (e.g., clavulanic acid). Some of the variant enzymes are more efficient at catalyzing beta-lactam hydrolysis, whereas others are more resistant to inhibitors. M182T is a substitution… CONTINUE READING

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