Role of ser-237 in the substrate specificity of the carbapenem-hydrolyzing class A beta-lactamase Sme-1.

doi:10.1016/s0167-4838(99)00138-7

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Article

Role of ser-237 in the substrate specificity of the carbapenem-hydrolyzing class A beta-lactamase Sme-1.

Biochimica et biophysica acta - 17 Aug 1999

Sougakoff W, Naas T, Nordmann P, Collatz E, Jarlier V

Abstract excerpt

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...

Topics

Alanine
Carbapenems
Enterobacteriaceae
Escherichia coli
Hydrolysis
Imipenem
Mutagenesis, Site-Directed
Mutation
Serine
Substrate Specificity
beta-Lactam Resistance
beta-Lactamases

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Open in PubMed

Identifiers

PMID: 10446368
DOI: 10.1016/s0167-4838(99)00138-7

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