ArticlePloS one2013
Differential active site loop conformations mediate promiscuous activities in the lactonase SsoPox.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed.
- Enzymatic quorum quenching alters the phyllosphere microbiome and suppresses a bacterial-induced plant disease.Scientific reports · 2026Article
- Phages and quorum sensing: findings to consider in phage therapy.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2026Review
- N-acyl homoserine lactone signaling modulates bacterial community associated with human dental plaque.NPJ biofilms and microbiomes · 2025Article
- Unlocking Lactonase Enzymes as Biocatalysts for the Deracemisation of Chiral γ-Thiolactones.Angewandte Chemie (International ed. in English) · 2025Article
- Impeding Quorum Sensing Among the Intestinal Microbiota Impacts the Metastatic Rate of Colorectal Cancer.Cancer medicine · 2025Article
- A Novel Screening System to Characterize and Engineer Quorum Quenching Lactonases.Biotechnology and bioengineering · 2025Article
- Quorum quenching enzymes disrupt bacterial communication in a sex- and dose-dependent manner.Animal models and experimental medicine · 2025Article
- Targeting quorum sensing for manipulation of commensal microbiota.BMC biotechnology · 2024Review
- Catalytic Redundancies and Conformational Plasticity Drives Selectivity and Promiscuity in Quorum Quenching Lactonases.JACS Au · 2024Article
- Applications of Microbial Organophosphate-Degrading Enzymes to Detoxification of Organophosphorous Compounds for Medical Countermeasures against Poisoning and Environmental Remediation.International journal of molecular sciences · 2024Review
- Changes in Active Site Loop Conformation Relate to the Transition toward a Novel Enzymatic Activity.JACS Au · 2024Article
- Engineering quorum quenching acylases with improved kinetic and biochemical properties.Protein science : a publication of the Protein Society · 2024Article
- Enzymes with Lactonase Activity against Fungal Quorum Molecules as Effective Antifungals.Biomolecules · 2024Article
- Disrupting quorum sensing as a strategy to inhibit bacterial virulence in human, animal, and plant pathogens.Pathogens and disease · 2024Article
- Thermostable Lactonases InhibitInternational journal of molecular sciences · 2023Article
- Mutexa: A Computational Ecosystem for Intelligent Protein Engineering.Journal of chemical theory and computation · 2023Review
- Field testing of an enzymatic quorum quencher coating additive to reduce biocorrosion of steel.Microbiology spectrum · 2023Article
- Reducing the virulence of Pseudomonas aeruginosa by using multiple quorum-quenching enzymes.Journal of industrial microbiology & biotechnology · 2023Article
- Targeting Multidrug-Recalcitrant Pseudomonas aeruginosa Biofilms: Combined-Enzyme Treatment Enhances Antibiotic Efficacy.Antimicrobial agents and chemotherapy · 2023Article
- Lactonase-mediated inhibition of quorum sensing largely alters phenotypes, proteome, and antimicrobial activities inFrontiers in cellular and infection microbiology · 2023Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enzymes are proficient catalysts that enable fast rates of Michaelis-complex formation, the chemical step and products release. These different steps may require different conformational states of the active site that have distinct binding properties. Moreover, the conformational flexibility of the active site mediates alternative, promiscuous functions. Here we focused on the lactonase SsoPox from Sulfolobus solfataricus. SsoPox is a native lactonase endowed with promiscuous phosphotriesterase activity. We identified a position in the active site loop (W263) that governs its flexibility, and thereby affects the substrate specificity of the enzyme. We isolated two different sets of substitutions at position 263 that induce two distinct conformational sampling of the active loop and characterized the structural and kinetic effects of these substitutions. These sets of mutations selectively and distinctly mediate the improvement of the promiscuous phosphotriesterase and oxo-lactonase activities of SsoPox by increasing active-site loop flexibility. These observations corroborate the idea that conformational diversity governs enzymatic promiscuity and is a key feature of protein evolvability.
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