The complexed structure and antimicrobial activity of a non‐β‐lactam inhibitor of AmpC β‐lactamase

@article{Powers1999TheCS,
  title={The complexed structure and antimicrobial activity of a non‐β‐lactam inhibitor of AmpC β‐lactamase},
  author={R. A. Powers and J. Bl{\'a}zquez and G. S. Weston and B. Shoichet and M. Morosini and F. Baquero},
  journal={Protein Science},
  year={1999},
  volume={8}
}
β‐Lactamases are the major resistance mechanism to β‐lactam antibiotics and pose a growing threat to public health. Recently, bacteria have become resistant to β‐lactamase inhibitors, making this problem pressing. In an effort to overcome this resistance, non‐β‐lactam inhibitors of β‐lactamases were investigated for complementarity to the structure of AmpC β‐lactamase from Escherichia coli. This led to the discovery of an inhibitor, benzo (b)thiophene‐2‐boronic acid (BZBTH2B), which inhibited… Expand
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