ArticleScientific reports2021
The Komagataeibacter europaeus GqqA is the prototype of a novel bifunctional N-Acyl-homoserine lactone acylase with prephenate dehydratase activity.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 9 citations in OpenAlex.
- In Situ Online Spectroscopy and Light Scattering Techniques.Advances in biochemical engineering/biotechnology · 2026Review
- Quorum Quenching Approaches against Bacterial-Biofilm-Induced Antibiotic Resistance.Antibiotics (Basel, Switzerland) · 2024Review
- Effects of the microbial community on the formation of volatile compounds and biogenic amines during the traditional brewing ofCurrent research in food science · 2022Article
- Quorum sensing in human gut and food microbiomes: Significance and potential for therapeutic targeting.Frontiers in microbiology · 2022Review
- Innovative microbial disease biocontrol strategies mediated by quorum quenching and their multifaceted applications: A review.Frontiers in plant science · 2022Review
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Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
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Abstract
Previously, we reported the isolation of a quorum quenching protein (QQ), designated GqqA, from Komagataeibacter europaeus CECT 8546 that is highly homologous to prephenate dehydratases (PDT) (Valera et al. in Microb Cell Fact 15, 88. https://doi.org/10.1186/s12934-016-0482-y , 2016). GqqA strongly interfered with N-acyl-homoserine lactone (AHL) quorum sensing signals from Gram-negative bacteria and affected biofilm formation in its native host strain Komagataeibacter europaeus. Here we present and discuss data identifying GqqA as a novel acylase. ESI-MS-MS data showed unambiguously that GqqA hydrolyzes the amide bond of the acyl side-chain of AHL molecules, but not the lactone ring. Consistent with this observation the protein sequence does not carry a conserved Zn
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