ReviewBiomolecules2019
The Role of the Ω-Loop in Regulation of the Catalytic Activity of TEM-Type β-Lactamases.
Review in Biomolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 49 citations in OpenAlex.
- Review
- Strategic design of a multi-tier database for class A β-lactamase BlaC variants of M. tuberculosis: advancing the fight against antibacterial resistance.The Journal of antibiotics · 2025Article
- A protein dynamics-based deep learning model enhances predictions of fitness and epistasis.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Effect of Mutations on the Evolution of Extended Spectrum β-lactamases (ESBL).The protein journal · 2025Review
- Alpha and Omega Classification of β-Lactamase/Transpeptidase-like Superfamily Proteins Based on the Comparison of Their Structural Catalytic Cores.Molecules (Basel, Switzerland) · 2025Article
- Physicochemical, functional, and evolutionary characteristics of protein loop regions in human andBiophysics and physicobiology · 2025Article
- The Impact of Ser165Glu Substitution Within the Ω-Loop on the Hydrolytic Activity of a Novel Ambler Class A β-Lactamase Variant LAP-3.Infection and drug resistance · 2025Article
- Molecular insights into the evolutionary trajectory of aAntimicrobial agents and chemotherapy · 2024Article
- Clinical emergence of a novel extended-spectrum variant deriving from the OXY-1 β-lactamase.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2024Article
- The Evolution of the Acylation Mechanism inACS catalysis · 2024Article
- Saturation Mutagenesis and Molecular Modeling: The Impact of Methionine 182 Substitutions on the Stability of β-Lactamase TEM-1.International journal of molecular sciences · 2024Article
- Revisiting the hydrolysis of ampicillin catalyzed by Temoneira-1 β-lactamase, and the effect of Ni(II), Cd(II) and Hg(II).Protein science : a publication of the Protein Society · 2023Article
- Exploring avibactam and relebactam inhibition ofAntimicrobial agents and chemotherapy · 2023Article
- Mutations responsible for the carbapenemase activity of SME-1.RSC advances · 2022Article
- A topological data analytic approach for discovering biophysical signatures in protein dynamics.PLoS computational biology · 2022Article
- Structural Characterization of the D179N and D179Y Variants of KPC-2 β-Lactamase: Ω-Loop Destabilization as a Mechanism of Resistance to Ceftazidime-Avibactam.Antimicrobial agents and chemotherapy · 2022Article
- Opening of a cryptic pocket in β-lactamase increases penicillinase activity.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- In-Vitro Selection of Ceftazidime/Avibactam Resistance in OXA-48-Like-ExpressingAntibiotics (Basel, Switzerland) · 2021Article
- β-Lactamases: Sequence, Structure, Function, and Inhibition.Biomolecules · 2021Article
- Can We Exploit β-Lactamases Intrinsic Dynamics for Designing More Effective Inhibitors?Antibiotics (Basel, Switzerland) · 2020Review
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
Bacterial resistance to β-lactams, the most commonly used class of antibiotics, poses a global challenge. This resistance is caused by the production of bacterial enzymes that are termed β-lactamases (βLs). The evolution of serine-class A β-lactamases from penicillin-binding proteins (PBPs) is related to the formation of the Ω-loop at the entrance to the enzyme's active site. In this loop, the Glu166 residue plays a key role in the two-step catalytic cycle of hydrolysis. This residue in TEM-type β-lactamases, together with Asn170, is involved in the formation of a hydrogen bonding network with a water molecule, leading to the deacylation of the acyl-enzyme complex and the hydrolysis of the β-lactam ring of the antibiotic. The activity exhibited by the Ω-loop is attributed to the positioning of its N-terminal residues near the catalytically important residues of the active site. The structure of the Ω-loop of TEM-type β-lactamases is characterized by low mutability, a stable topology, and structural flexibility. All of the revealed features of the Ω-loop, as well as the mechanisms related to its involvement in catalysis, make it a potential target for novel allosteric inhibitors of β-lactamases.
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