Roles of residues Cys69, Asn104, Phe160, Gly232, Ser237, and Asp240 in extended-spectrum beta-lactamase Toho-1.

@article{ShimizuIbuka2011RolesOR,
  title={Roles of residues Cys69, Asn104, Phe160, Gly232, Ser237, and Asp240 in extended-spectrum beta-lactamase Toho-1.},
  author={Akiko Shimizu-Ibuka and Mika Oishi and Shoko Yamada and Yoshikazu Ishii and Kiyoshi Mura and Hiroshi Sakai and Hiroshi Matsuzawa},
  journal={Antimicrobial agents and chemotherapy},
  year={2011},
  volume={55 1},
  pages={284-90}
}
Toho-1, which is also designated CTX-M-44, is an extended-spectrum class A β-lactamase that has high activity toward cefotaxime. In this study, we investigated the roles of residues suggested to be critical for the substrate specificity expansion of Toho-1 in previous structural analyses. Six amino acid residues were replaced one by one with amino acids that are often observed in the corresponding position of non-extended-spectrum β-lactamases. The mutants produced in Escherichia coli strains… CONTINUE READING

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