Impact of Mutations at Arg220 and Thr237 in PER-2 β-Lactamase on Conformation, Activity, and Susceptibility to Inhibitors.

doi:10.1128/AAC.02193-16

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Article

Impact of Mutations at Arg220 and Thr237 in PER-2 β-Lactamase on Conformation, Activity, and Susceptibility to Inhibitors.

Antimicrobial agents and chemotherapy - 1 Jun 2017

Ruggiero Melina, Curto Lucrecia, Brunetti Florencia, Sauvage Eric, Galleni Moreno, Power Pablo, Gutkind Gabriel

Abstract excerpt

PER-2 accounts for up to 10% of oxyimino-cephalosporin resistance in Klebsiella pneumoniae and Escherichia coli in Argentina and hydrolyzes both cefotaxime and ceftazidime with high catalytic efficiencies (kcat/Km ). Through crystallographic analyses, we recently proposed the existence of a hydrogen bond network connecting Ser70-Gln69-oxyanion water-Thr237-Arg220 that might be important for the activity and...

Topics

Cefepime
Cefotaxime
Ceftazidime
Cephalosporins
Clavulanic Acid
Escherichia coli
Klebsiella pneumoniae
Microbial Sensitivity Tests
Mutation
beta-Lactamase Inhibitors
beta-Lactamases

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Identifiers

PMID: 28320728
DOI: 10.1128/AAC.02193-16
PMCID: PMC5444140

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