ArticleScientific reports2016
Engineering of a thermostable esterase Est816 to improve its quorum-quenching activity and the underlying structural basis.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 20 citations in OpenAlex.
- Developing a Silver Nanocomposite With Quorum-Quenching Enzyme Ag-Est816 to Prevent Periodontitis.International dental journal · 2026Article
- Quorum-Quenching AHL-Lactonase Est816 Inhibits Polymicrobial Subgingival-Plaque-Derived Biofilm Formation.Dentistry journal · 2025Article
- Article
- The Role of Quorum Sensing Molecules in Bacterial-Plant Interactions.Metabolites · 2023Review
- Engineering acyl-homoserine lactone-interfering enzymes toward bacterial control.The Journal of biological chemistry · 2020Review
- Engineering quorum quenching enzymes: progress and perspectives.Biochemical Society transactions · 2019Review
- Aii810, a Novel Cold-AdaptedFrontiers in microbiology · 2017Article
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
N-acyl-homoserine lactones (AHLs) are small diffusible molecules called autoinducers that mediate cell-to-cell communications. Enzymatic degradation of AHLs is a promising bio-control strategy known as quorum-quenching. To improve the quorum-quenching activity of a thermostable esterase Est816, which had been previously cloned, we have engineered the enzyme by random mutagenesis. One of the mutants M2 with double amino acid substitutions (A216V/K238N) showed 3-fold improvement on catalytic efficiency. Based on the crystal structure determined at 2.64 Å, rational design of M2 was conducted, giving rise to the mutant M3 (A216V/K238N/L122A). The k
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Registered trials
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