ArticleAntimicrobial agents and chemotherapy2014
Deletion mutations conferring substrate spectrum extension in the class A β-lactamase.
Article in Antimicrobial agents and chemotherapy, 2014. 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.
- 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
- The Importance of Porins and β-Lactamase in Outer Membrane Vesicles on the Hydrolysis of β-Lactam Antibiotics.International journal of molecular sciences · 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
- Effect of β-Lactamase inhibitors on in vitro activity of β-Lactam antibiotics againstAntimicrobial resistance and infection control · 2016Article
- 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
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 four new deletion mutations in a class A β-lactamase PenA in Burkholderia thailandensis, each conferring an extended substrate spectrum. Single-amino-acid deletions T171del, I173del, and P174del and a two-amino-acid deletion, R165_T167delinsP, occurred in the omega loop, increasing the flexibility of the binding cavity. This rare collection of mutations has significance, allowing exploration of the diverse evolutionary trajectories of β-lactamases and as potential future mutations conferring high-level ceftazidime resistance on isolates from clinical settings, compared with amino acid substitution mutations.
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