ArticleAntimicrobial agents and chemotherapy2006
Prediction of the evolution of ceftazidime resistance in extended-spectrum beta-lactamase CTX-M-9.
Article in Antimicrobial agents and chemotherapy, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 36 citations in OpenAlex.
- Directed evolution of a beta-lactamase samples a wide variety of conformational states.Protein science : a publication of the Protein Society · 2025Article
- Mapping the determinants of catalysis and substrate specificity of the antibiotic resistance enzyme CTX-M β-lactamase.Communications biology · 2023Article
- Synergistic effects of functionally distinct substitutions in β-lactamase variants shed light on the evolution of bacterial drug resistance.The Journal of biological chemistry · 2018Article
- Predicting allostery and microbial drug resistance with molecular simulations.Current opinion in structural biology · 2018Review
- Kinetic characterization of GES-22 β-lactamase harboring the M169L clinical mutation.The Journal of antibiotics · 2016Article
- Excess positional mutual information predicts both local and allosteric mutations affecting beta lactamase drug resistance.Bioinformatics (Oxford, England) · 2016Article
- A Structure-Based Classification of Class A β-Lactamases, a Broadly Diverse Family of Enzymes.Clinical microbiology reviews · 2016Review
- Characterization of the global stabilizing substitution A77V and its role in the evolution of CTX-M β-lactamases.Antimicrobial agents and chemotherapy · 2015Article
- High Prevalence and Significant Association of ESBL and QNR Genes in Pathogenic Klebsiella pneumoniae Isolates of Patients from Kolkata, India.Indian journal of microbiology · 2012Article
- Characterization of the inhibitor-resistant SHV β-lactamase SHV-107 in a clinical Klebsiella pneumoniae strain coproducing GES-7 enzyme.Antimicrobial agents and chemotherapy · 2012Article
- Twelve positions in a β-lactamase that can expand its substrate spectrum with a single amino acid substitution.PloS one · 2012Article
- Distant and new mutations in CTX-M-1 beta-lactamase affect cefotaxime hydrolysis.Antimicrobial agents and chemotherapy · 2011Article
- Exploring the inhibition of CTX-M-9 by beta-lactamase inhibitors and carbapenems.Antimicrobial agents and chemotherapy · 2011Article
- CTX-M-93, a CTX-M variant lacking penicillin hydrolytic activity.Antimicrobial agents and chemotherapy · 2011Article
- Mutational events in cefotaximase extended-spectrum beta-lactamases of the CTX-M-1 cluster involved in ceftazidime resistance.Antimicrobial agents and chemotherapy · 2008Article
- The Lys234Arg substitution in the enzyme SHV-72 is a determinant for resistance to clavulanic acid inhibition.Antimicrobial agents and chemotherapy · 2008Article
- Convergent in vivo and in vitro selection of ceftazidime resistance mutations at position 167 of CTX-M-3 beta-lactamase in hypermutable Escherichia coli strains.Antimicrobial agents and chemotherapy · 2008Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A random mutagenesis technique was used to predict the evolutionary potential of beta-lactamase CTX-M-9 toward the acquisition of improved catalytic activity against ceftazidime. Thirty CTX-M mutants were obtained during three rounds of mutagenesis. These mutants conferred 1- to 128-fold-higher MICs of ceftazidime than the parental enzyme CTX-M-9. The CTX-M mutants contained one to six amino acid substitutions. Mutants harbored the substitutions Asp240Gly and Pro167Ser, which were previously observed in clinical CTX-M enzymes. Additional substitutions, notably Arg164His, Asp179Gly, and Arg276Ser, were observed near the active site. The kinetic constants of the three most active mutants revealed two distinct ways of improving catalytic efficiency against ceftazidime. One enzyme had a 17-fold-higher k(cat) value than CTX-M-9 against ceftazidime. The other two had 75- to 300-fold-lower Km values than CTX-M-9 against ceftazidime. The current emergence of CTX-M beta-lactamases with improved activity against ceftazidime may therefore be the beginning of an evolutionary process which might subsequently generate a great diversity of CTX-M-type ceftazidimases.
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