ArticleAntimicrobial agents and chemotherapy2016
Comparative Characterization of CTX-M-64 and CTX-M-14 Provides Insights into the Structure and Catalytic Activity of the CTX-M Class of Enzymes.
Article in Antimicrobial agents and chemotherapy, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed.
- Evaluation of Virulence Profiles and Molecular Typing of ESBL-Producing UropathogenicInfection and drug resistance · 2026Article
- Extended-Spectrum Beta-Lactamases ProducingInfection and drug resistance · 2022Review
- Structural and Biochemical Characterization of the Novel CTX-M-151 Extended-Spectrum β-Lactamase and Its Inhibition by Avibactam.Antimicrobial agents and chemotherapy · 2021Article
- Emergence of NDM-1- and CTX-M-3-ProducingFrontiers in microbiology · 2019Article
- Predicting allostery and microbial drug resistance with molecular simulations.Current opinion in structural biology · 2018Review
- Functional Characterization of CTX-M-14 and CTX-M-15 β-Lactamases byAntimicrobial agents and chemotherapy · 2017Article
- Genetic and Functional Characterization ofAntimicrobial agents and chemotherapy · 2017Article
Corrections and comments
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Authors and funding
6 authors.
Funding
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Abstract
Clinical isolates producing hybrid CTX-M β-lactamases, presumably due to recombination between the blaCTX-M-15 and blaCTX-M-14 elements, have emerged in recent years. Among the hybrid enzymes, CTX-M-64 and CTX-M-14 display the most significant difference in catalytic activity. This study aims to investigate the mechanisms underlying such differential enzymatic activities in order to provide insight into the structure/function relationship of this class of enzymes. Sequence alignment analysis showed that the major differences between the amino acid composition of CTX-M-64 and CTX-M-14 lie at both the N and C termini of the enzymes. Single or multiple amino acid substitutions introduced into CTX-M-64 and CTX-M-14 were found to produce only minor effects on hydrolytic functions; such a finding is consistent with the notion that the discrepancy between the functional activities of the two enzymes is not the result of only a few amino acid changes but is attributable to interactions between a unique set of amino acid residues in each enzyme. This theory is supported by the results of the thermal stability assay, which confirmed that CTX-M-64 is significantly more stable than CTX-M-14. Our data confirmed that, in addition to the important residues located in the active site, residues distal to the active site also contribute to the catalytic activity of the enzyme through stabilizing its structural integrity.
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