ArticleAntimicrobial agents and chemotherapy2015
Residues Distal to the Active Site Contribute to Enhanced Catalytic Activity of Variant and Hybrid β-Lactamases Derived from CTX-M-14 and CTX-M-15.
Article in Antimicrobial agents and chemotherapy, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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33 citing papers in PubMed, 42 citations in OpenAlex.
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- Distribution and characteristics of ceftiofur-resistant Escherichia coli throughout the broiler production chain in Korea.Veterinary research · 2026Article
- Molecular Epidemiology of Extended-spectrum β-Lactamase-producingAnnals of laboratory medicine · 2026Article
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- Emergence of a clinical Salmonella enterica serovar 1,4,[5], 12: i:-isolate, ST3606, in China with susceptibility decrease to ceftazidime-avibactam carrying a novel blaEuropean journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2024Article
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- Poultry production as the main reservoir of ciprofloxacin- and tigecycline-resistant extended-spectrum β-lactamase (ESBL)-producingApplied and environmental microbiology · 2023Article
- Epidemiological, Genetic, and Phenotypic Characteristics of Non-TyphoidalMicroorganisms · 2023Article
- Genomic Insights into GlobalMicrobiology spectrum · 2023Article
- Portable Differential Detection of CTX-M ESBL Gene Variants,Microbiology spectrum · 2023Article
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- Prevalence and Characterization of ESBL/AmpC ProducingAntibiotics (Basel, Switzerland) · 2021Article
- IS26-mediated amplification of blaOXA-1 and blaCTX-M-15 with concurrent outer membrane porin disruption associated with de novo carbapenem resistance in a recurrent bacteraemia cohort.The Journal of antimicrobial chemotherapy · 2021Article
- First Report of a FoodborneFrontiers in microbiology · 2021Article
- The Amino Acid Changes T55A, A273P and R277C in the Beta-Lactamase CTX-M-14 RenderMicroorganisms · 2020Article
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9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A variety of CTX-M-type extended-spectrum β-lactamases (ESBLs), including hybrid ones, have been reported in China that are uncommon elsewhere. To better characterize the substrate profiles and enzymatic mechanisms of these enzymes, we performed comparative kinetic analyses of both parental and hybrid CTX-M enzymes, including CTX-M-15, -132, -123, -64, -14 and -55, that are known to confer variable levels of β-lactam resistance in the host strains. All tested enzymes were susceptible to serine β-lactamase inhibitors, with sulbactam exhibiting the weakest inhibitory effects. CTX-M-55, which differs from CTX-M-15 by one substitution, A(77)V, displayed enhanced catalytic activity (kcat/Km) against expanded-spectrum cephalosporins (ESCs). CTX-M-55 exhibits higher structure stability, most likely by forming hydrophobic interactions between A(77)V and various key residues in different helices, thereby stabilizing the core architecture of the helix cluster, and indirectly contributes to a more stable active site conformation, which in turn shows higher catalytic efficiency and is more tolerant to temperature change. Analyses of the hybrids and their parental prototypes showed that evolution from CTX-M-15 to CTX-M-132, CTX-M-123, and CTX-M-64, characterized by gradual enhancement of catalytic activity to ESCs, was attributed to introduction of different substitutions to amino acids distal to the active site of CTX-M-15. Similarly, the increased hydrolytic activities against cephalosporins and sensitivity to β-lactamase inhibitors, clavulanic acid and sulbactam, of CTX-M-64 were partly due to the amino acids that were different from CTX-M-14 and located at both the C and N termini of CTX-M-64. These data indicate that residues distal to the active site of CTX-Ms contributed to their enhanced catalytic activities to ESCs.
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