Kinetics of the Interaction between BAL29880 and LK157 and the Class C β-Lactamase CHE-1 | Zendy

Adriana Fernea | Zendy; Moreno Galleni | Zendy; JeanMarie Frère | Zendy

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Kinetics of the Interaction between BAL29880 and LK157 and the Class C β-Lactamase CHE-1

Author(s) -

Adriana Fernea,

Moreno Galleni,

JeanMarie Frère

Publication year - 2016

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.02062-15

Subject(s) - enterobacter cloacae , avibactam , kinetics , enzyme , chemistry , residue (chemistry) , stereochemistry , enterobacteriaceae , lactam , mutant , beta lactamase inhibitors , reaction rate constant , microbiology and biotechnology , substrate specificity , enzyme kinetics , active site , biology , biochemistry , escherichia coli , gene , physics , quantum mechanics

The chromosome-encoded class C β-lactamase CHE-1 produced by Enterobacter cloacae exhibits a lower sensitivity to avibactam than the P99 enzyme from which it is derived by a 6-residue deletion in the H-10 helix. In the present study, we investigated the sensitivity of CHE-1 to two other β-lactamase inhibitors: LK-157 (or Lek 157), a tricyclic β-lactam, and BAL29880, a bridged monobactam. With both compounds, the second-order rate constants for inactivation were significantly lower for CHE-1, which can thus be considered an inactivator-resistant mutant of P99. However, the second-order rate constant for the inactivation by BAL29880 probably remains adequate for a rather rapid reaction with CHE-1 in the absence of protection by the substrate.

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