ArticleBiochemistry2015
Structural and Biochemical Characterization of AidC, a Quorum-Quenching Lactonase with Atypical Selectivity.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 0 citations in OpenAlex.
- Computational design of metallohydrolases.Nature · 2026Article
- In Silico Identification of Potential Biomarker-Binding Proteins for Noninvasive Diagnosis of Buruli Ulcer Disease.Bioinformatics and biology insights · 2026Article
- Development and Biochemical Characterization of Quorum Quenching Enzyme from Deep-SeaMicroorganisms · 2025Article
- Reducing the virulence of Pseudomonas aeruginosa by using multiple quorum-quenching enzymes.Journal of industrial microbiology & biotechnology · 2023Article
- N-acylhomoserine lactonase-based hybrid nanoflowers: a novel and practical strategy to control plant bacterial diseases.Journal of nanobiotechnology · 2022Article
- The exceptionally efficient quorum quenching enzyme LrsL suppressesFrontiers in microbiology · 2022Article
- Cyclobutanone Inhibitor of Cobalt-Functionalized Metallo-γ-Lactonase AiiA with Cyclobutanone Ring Opening in the Active Site.ACS omega · 2021Article
- Engineering acyl-homoserine lactone-interfering enzymes toward bacterial control.The Journal of biological chemistry · 2020Review
- 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
- Structural and Biochemical Characterization of AaL, a Quorum Quenching Lactonase with Unusual Kinetic Properties.Scientific reports · 2018Article
- Characterization of AiiK, an AHL lactonase, from Kurthia huakui LAM0618Scientific reports · 2018Article
- AidP, a novel N-Acyl homoserine lactonase gene from Antarctic Planococcus sp.Scientific reports · 2017Article
- Engineering of a thermostable esterase Est816 to improve its quorum-quenching activity and the underlying structural basis.Scientific reports · 2016Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Quorum-quenching catalysts are of interest for potential application as biochemical tools for interrogating interbacterial communication pathways, as antibiofouling agents, and as anti-infective agents in plants and animals. Herein, the structure and function of AidC, an N-acyl-l-homoserine lactone (AHL) lactonase from Chryseobacterium, is characterized. Steady-state kinetics show that zinc-supplemented AidC is the most efficient wild-type quorum-quenching enzymes characterized to date, with a kcat/KM value of approximately 2 × 10(6) M(-1) s(-1) for N-heptanoyl-l-homoserine lactone. The enzyme has stricter substrate selectivity and significantly lower KM values (ca. 50 μM for preferred substrates) compared to those of typical AHL lactonases (ca. >1 mM). X-ray crystal structures of AidC alone and with the product N-hexanoyl-l-homoserine were determined at resolutions of 1.09 and 1.67 Å, respectively. Each structure displays as a dimer, and dimeric oligiomerization was also observed in solution by size-exclusion chromatography coupled with multiangle light scattering. The structures reveal two atypical features as compared to previously characterized AHL lactonases: a "kinked" α-helix that forms part of a closed binding pocket that provides affinity and enforces selectivity for AHL substrates and an active-site His substitution that is usually found in a homologous family of phosphodiesterases. Implications for the catalytic mechanism of AHL lactonases are discussed.
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