ArticleAntimicrobial agents and chemotherapy2012
Substrate spectrum extension of PenA in Burkholderia thailandensis with a single amino acid deletion, Glu168del.
Article in Antimicrobial agents and chemotherapy, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 18 citations in OpenAlex.
- Exploring the deletion landscape ofbioRxiv : the preprint server for biology · 2025Article
- Evolutionary Dynamics and Functional Differences in Clinically Relevant Pen β-Lactamases fromJournal of chemical information and modeling · 2025Article
- Article
- A study of Rose Bengal against a 2-keto-3-deoxy-d-Journal of enzyme inhibition and medicinal chemistry · 2020Article
- Mutations in ArgS Arginine-tRNA Synthetase Confer Additional Antibiotic Tolerance Protection to Extended-Spectrum-β-Lactamase-Producing Burkholderia thailandensis.Antimicrobial agents and chemotherapy · 2020Article
- Exploring the Role of the Ω-Loop in the Evolution of Ceftazidime Resistance in the PenA β-Lactamase from Burkholderia multivorans, an Important Cystic Fibrosis Pathogen.Antimicrobial agents and chemotherapy · 2017Article
- High adaptability of the omega loop underlies the substrate-spectrum-extension evolution of a class A β-lactamase, PenL.Scientific reports · 2016Article
- Antibiotic resistance in Burkholderia species.Drug resistance updates : reviews and commentaries in antimicrobial and anticancer chemotherapy · 2016Review
- Structural and Functional Aspects of Class A Carbapenemases.Current drug targets · 2016Review
- A Structure-Based Classification of Class A β-Lactamases, a Broadly Diverse Family of Enzymes.Clinical microbiology reviews · 2016Review
- Deletion mutations conferring substrate spectrum extension in the class A β-lactamase.Antimicrobial agents and chemotherapy · 2014Article
- The tandem repeats enabling reversible switching between the two phases of β-lactamase substrate spectrum.PLoS genetics · 2014Article
- Mechanisms of antibiotic resistance in Burkholderia pseudomallei: implications for treatment of melioidosis.Future microbiology · 2012Review
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
We describe a deletion mutation in a class A β-lactamase, PenA, of Burkholderia thailandensis that extended the substrate spectrum of the enzyme to include ceftazidime. Glu168del was located in a functional domain called the omega loop causing expansion of the space in the loop, which in turn increased flexibility at the active site. This deletion mutation represents a rare but significant alternative mechanical path to substrate spectrum extension in PenA besides more common substitution mutations.
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