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- W2085868976 abstract "The role of the serine residue found at position 237 in the carbapenemase Sme-1 has been investigated by constructing a mutant in which Ser-237 was replaced by an alanine. The S237A mutant showed a catalytic behavior against penicillins and aztreonam very similar to that of Sme-1. By contrast, S237A was characterized by a reduced catalytic efficiency against cephems, such as cephalothin and cephaloridine. In addition, the weak activity of Sme-1 against the cephamycin cefoxitin was hardly detectable with the mutant enzyme. Finally, the Ser-237→Ala mutation resulted in a marked decrease in catalytic activity against imipenem, showing that Ser-237 contributes to the carbapenemase activity of the class A β-lactamase Sme-1." @default.
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- W2085868976 date "1999-08-01" @default.
- W2085868976 modified "2023-10-16" @default.
- W2085868976 title "Role of Ser-237 in the substrate specificity of the carbapenem-hydrolyzing class A β-lactamase Sme-1" @default.
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- W2085868976 doi "https://doi.org/10.1016/s0167-4838(99)00138-7" @default.
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