ArticleScientific reports2012
Characterisation of the organophosphate hydrolase catalytic activity of SsoPox.
Article in Scientific reports, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed.
- Enzymatic quorum quenching alters the phyllosphere microbiome and suppresses a bacterial-induced plant disease.Scientific reports · 2026Article
- N-acyl homoserine lactone signaling modulates bacterial community associated with human dental plaque.NPJ biofilms and microbiomes · 2025Article
- A Thermostable Bacterial Metallohydrolase that Degrades Organophosphate Plasticizers.Chembiochem : a European journal of chemical biology · 2025Article
- A Novel Screening System to Characterize and Engineer Quorum Quenching Lactonases.Biotechnology and bioengineering · 2025Article
- Diffusible Signal Factors andBiology · 2025Review
- Advancements in bioscavenger mediated detoxification of organophosphorus poisoning.Toxicology research · 2024Review
- Changes in Active Site Loop Conformation Relate to the Transition toward a Novel Enzymatic Activity.JACS Au · 2024Article
- Paraoxonase 1 and atherosclerosis.Frontiers in cardiovascular medicine · 2023Review
- Evidence for Complex Interplay between Quorum Sensing and Antibiotic Resistance in Pseudomonas aeruginosa.Microbiology spectrum · 2022Article
- Disrupting quorum sensing alters social interactions in Chromobacterium violaceum.NPJ biofilms and microbiomes · 2021Article
- Enzymes, Reacting with Organophosphorus Compounds as Detoxifiers: Diversity and Functions.International journal of molecular sciences · 2021Review
- Microbial Derived Compounds, a Step Toward Enhancing Microbial Inoculants Technology for Sustainable Agriculture.Frontiers in microbiology · 2021Review
- Quorum quenching enzymes and their effects on virulence, biofilm, and microbiomes: a review of recent advances.Expert review of anti-infective therapy · 2020Review
- Steady-State Kinetics of Enzyme-Catalyzed Hydrolysis of Echothiophate, a P-S Bonded Organophosphorus as Monitored by Spectrofluorimetry.Molecules (Basel, Switzerland) · 2020Article
- Structural and Functional Characterization of New SsoPox Variant Points to the Dimer Interface as a Driver for the Increase in Promiscuous Paraoxonase Activity.International journal of molecular sciences · 2020Article
- Structure Dependent Determination of Organophosphate Targets in Mammalian Tissues Using Activity-Based Protein Profiling.Chemical research in toxicology · 2020Article
- In vivo immobilization of an organophosphorus hydrolyzing enzyme on bacterial polyhydroxyalkanoate nano-granules.Microbial cell factories · 2019Article
- Effects of Signal Disruption Depends on the Substrate Preference of the Lactonase.Frontiers in microbiology · 2019Article
- Signal Disruption Leads to Changes in Bacterial Community Population.Frontiers in microbiology · 2019Article
- Quorum Quenching Lactonase Strengthens Bacteriophage and Antibiotic Arsenal AgainstFrontiers in microbiology · 2019Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SsoPox is a lactonase endowed with promiscuous phosphotriesterase activity isolated from Sulfolobus solfataricus that belongs to the Phosphotriesterase-Like Lactonase family. Because of its intrinsic thermal stability, SsoPox is seen as an appealing candidate as a bioscavenger for organophosphorus compounds. A comprehensive kinetic characterisation of SsoPox has been performed with various phosphotriesters (insecticides) and phosphodiesters (nerve agent analogues) as substrates. We show that SsoPox is active for a broad range of OPs and remains active under denaturing conditions. In addition, its OP hydrolase activity is highly stimulated by anionic detergent at ambient temperature and exhibits catalytic efficiencies as high as k(cat)/K(M) of 10(5) M(-1)s(-1) against a nerve agent analogue. The structure of SsoPox bound to the phosphotriester fensulfothion reveals an unexpected and non-productive binding mode. This feature suggests that SsoPox's active site is sub-optimal for phosphotriester binding, which depends not only upon shape but also on localised charge of the ligand.
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