ArticleScientific reports2017
Rational engineering of a native hyperthermostable lactonase into a broad spectrum phosphotriesterase.
Article in Scientific reports, 2017. 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.
- AI-Driven Enzyme Engineering: Emerging Models and Next-Generation Biotechnological Applications.Molecules (Basel, Switzerland) · 2025Review
- N-acyl homoserine lactone signaling modulates bacterial community associated with human dental plaque.NPJ biofilms and microbiomes · 2025Article
- Enhancing stability of enzymes for industrial applications: molecular insights and emerging approaches.World journal of microbiology & biotechnology · 2025Review
- Revisiting D-Acylases for D-Amino Acid Production.Microbial biotechnology · 2025Article
- Quorum quenching enzymes disrupt bacterial communication in a sex- and dose-dependent manner.Animal models and experimental medicine · 2025Article
- 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
- Current status and emerging frontiers in enzyme engineering: An industrial perspective.Heliyon · 2024Review
- Changes in Active Site Loop Conformation Relate to the Transition toward a Novel Enzymatic Activity.JACS Au · 2024Article
- The Role of Quorum Sensing Molecules in Bacterial-Plant Interactions.Metabolites · 2023Review
- Nature-inspired Enzyme engineering and sustainable catalysis: biochemical clues from the world of plants and extremophiles.Frontiers in bioengineering and biotechnology · 2023Review
- Evidence for Complex Interplay between Quorum Sensing and Antibiotic Resistance in Pseudomonas aeruginosa.Microbiology spectrum · 2022Article
- Applying molecular and phenotypic screening assays to identify efficient quorum quenching lactonases.Enzyme and microbial technology · 2022Article
- An integrative approach to improving the biocatalytic reactions of whole cells expressing recombinant enzymes.World journal of microbiology & biotechnology · 2021Review
- Engineering acyl-homoserine lactone-interfering enzymes toward bacterial control.The Journal of biological chemistry · 2020Review
- Hybrid Thermophilic/Mesophilic Enzymes Reveal a Role for Conformational Disorder in Regulation of Bacterial Enzyme I.Journal of molecular biology · 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
- Signal Disruption Leads to Changes in Bacterial Community Population.Frontiers in microbiology · 2019Article
- Enzymatic Bioremediation of Organophosphate Compounds-Progress and Remaining Challenges.Frontiers in bioengineering and biotechnology · 2019Review
- Biotechnology of extremely thermophilic archaea.FEMS microbiology reviews · 2018Review
- Structural and Biochemical Characterization of AaL, a Quorum Quenching Lactonase with Unusual Kinetic Properties.Scientific reports · 2018Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The redesign of enzyme active sites to alter their function or specificity is a difficult yet appealing challenge. Here we used a structure-based design approach to engineer the lactonase SsoPox from Sulfolobus solfataricus into a phosphotriesterase. The five best variants were characterized and their structure was solved. The most active variant, αsD6 (V27A-Y97W-L228M-W263M) demonstrates a large increase in catalytic efficiencies over the wild-type enzyme, with increases of 2,210-fold, 163-fold, 58-fold, 16-fold against methyl-parathion, malathion, ethyl-paraoxon, and methyl-paraoxon, respectively. Interestingly, the best mutants are also capable of degrading fensulfothion, which is reported to be an inhibitor for the wild-type enzyme, as well as others that are not substrates of the starting template or previously reported W263 mutants. The broad specificity of these engineered variants makes them promising candidates for the bioremediation of organophosphorus compounds. Analysis of their structures reveals that the increase in activity mainly occurs through the destabilization of the active site loop involved in substrate binding, and it has been observed that the level of disorder correlates with the width of the enzyme specificity spectrum. This finding supports the idea that active site conformational flexibility is essential to the acquisition of broader substrate specificity.
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