| Literature DB >> 10446368 |
W Sougakoff1, T Naas, P Nordmann, E Collatz, V Jarlier.
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 beta-lactamase Sme-1.Entities:
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Year: 1999 PMID： 10446368 DOI： 10.1016/s0167-4838(99)00138-7
Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002