ArticleAntimicrobial agents and chemotherapy2008
E240V substitution increases catalytic efficiency toward ceftazidime in a new natural TEM-type extended-spectrum beta-lactamase, TEM-149, from Enterobacter aerogenes and Serratia marcescens clinical isolates.
Article in Antimicrobial agents and chemotherapy, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Saturation mutagenesis map of generalist versus specialist adaptations of β-lactamase to novel antibiotics.bioRxiv : the preprint server for biology · 2026Article
- A Two Amino Acid Duplication, L167E168, in the Ω-Loop Drastically Decreases Carbapenemase Activity of KPC-53, a Natural Class A β-Lactamase.Antimicrobial agents and chemotherapy · 2022Article
- Kinetic Profile and Molecular Dynamic Studies Show that Y229W Substitution in an NDM-1/L209F Variant Restores the Hydrolytic Activity of the Enzyme toward Penicillins, Cephalosporins, and Carbapenems.Antimicrobial agents and chemotherapy · 2019Article
- TEM-184, a Novel TEM-Derived Extended-Spectrum β-Lactamase with Enhanced Activity against Aztreonam.Antimicrobial agents and chemotherapy · 2018Article
- Kinetic study of the effect of histidines 240 and 164 on TEM-149 enzyme probed by β-lactam inhibitors.Antimicrobial agents and chemotherapy · 2014Article
- Non-phenotypic tests to detect and characterize antibiotic resistance mechanisms in Enterobacteriaceae.Diagnostic microbiology and infectious disease · 2013Review
- R164H and V240H replacements by site-directed mutagenesis of TEM-149 extended-spectrum β-lactamase: kinetic analysis of TEM-149H240 and TEM-149H164-H240 laboratory mutants.Antimicrobial agents and chemotherapy · 2013Article
- Infections with VIM-1 metallo-{beta}-lactamase-producing enterobacter cloacae and their correlation with clinical outcome.Journal of clinical microbiology · 2009Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The aim of this study was to characterize a novel extended-spectrum beta-lactamase that belongs to the TEM family, the TEM-149 enzyme, and that was isolated from the urine of two hospitalized patients from different hospitals in southern Italy. The peculiarity of this enzyme was the finding of a valine residue at position 240. The array of amino acid substitutions found in TEM-149 was as follows: E104K, R164S, M182T, and E240V. A reversion of a threonine residue at position 182 was also performed to create a new mutant, TEM-149 T182M, in order to assess the contribution of this substitution on the kinetic profile and the stability of TEM-149. The bla TEM-149 and bla TEM-149/T182M genes were cloned into pBC-SK, and the corresponding enzymes were purified from recombinant Escherichia coli HB101 by the same procedure. Both enzymes hydrolyzed all beta-lactams tested, with a preference for ceftazidime, which was found to be the best substrate. By comparison of the kinetic parameters of the TEM-149 and the TEM-149 T182M enzymes, a reduction of the catalytic efficiency for the TEM-149 T182M mutant was observed against all substrates tested except benzylpenicillin, cefotaxime, and aztreonam. Tazobactam, clavulanic acid, and sulbactam were good inhibitors of the TEM-149 beta-lactamase.
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