An engineered disulfide bond between residues 69 and 238 in extended-spectrum beta-lactamase Toho-1 reduces its activity toward third-generation cephalosporins.

Abstract

Previous crystallographic structural analysis of extended-spectrum beta-lactamase Toho-1 predicted that the high flexibility of beta-strand B3, the region that contains a conserved KTG motif and forms one wall of the substrate-binding site, could be one of the key features contributing to Toho-1 activity toward third-generation cephalosporins. To… (More)

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Cite this paper

@article{ShimizuIbuka2004AnED, title={An engineered disulfide bond between residues 69 and 238 in extended-spectrum beta-lactamase Toho-1 reduces its activity toward third-generation cephalosporins.}, author={Akiko Shimizu-Ibuka and Hiroshi Matsuzawa and Hiroshi Sakai}, journal={Biochemistry}, year={2004}, volume={43 50}, pages={15737-45} }