ArticleScientific reports2017
Bifunctional quorum-quenching and antibiotic-acylase MacQ forms a 170-kDa capsule-shaped molecule containing spacer polypeptides.
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 11 papers.
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11 citing papers in PubMed, 20 citations in OpenAlex.
- The Biosynthetic Pathway for the Hybrid NRPS-NIS Siderophore Nocardichelin Contains NcdG, a Succinylase that Cleaves the Hydroxamate Bond of the Acylcadaverine Intermediate.ACS chemical biology · 2026Article
- An acyl-homoserine lactone acylase found in Stenotrophomonas maltophilia exhibits both quorum quenching activity and the ability to degrade penicillin antibiotics.Scientific reports · 2025Article
- Engineering quorum quenching acylases with improved kinetic and biochemical properties.Protein science : a publication of the Protein Society · 2024Article
- Selection and Molecular Response of AHL-lactonase (aiiA) Producing Bacillus sp. Under Penicillin G-induced Conditions.The protein journal · 2023Article
- Bile Salt Hydrolase Degrades β-Lactam Antibiotics and Confers Antibiotic Resistance onFrontiers in microbiology · 2022Article
- Isolation of a Highly Thermostable Bile Salt Hydrolase With Broad Substrate Specificity FromFrontiers in microbiology · 2022Article
- Quorum Quenching Enzyme (PF-1240) Capable to Degrade AHLs as a Candidate for Inhibiting Quorum Sensing in Food Spoilage BacteriumFoods (Basel, Switzerland) · 2021Article
- The Komagataeibacter europaeus GqqA is the prototype of a novel bifunctional N-Acyl-homoserine lactone acylase with prephenate dehydratase activity.Scientific reports · 2021Article
- Engineering quorum quenching enzymes: progress and perspectives.Biochemical Society transactions · 2019Review
- NovelFrontiers in microbiology · 2019Article
- Cultivation Renaissance in the Post-Metagenomics Era: Combining the New and Old.Microbes and environments · 2019Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Understanding the molecular mechanisms of bacterial antibiotic resistance will help prepare against further emergence of multi-drug resistant strains. MacQ is an enzyme responsible for the multi-drug resistance of Acidovorax sp. strain MR-S7. MacQ has acylase activity against both N-acylhomoserine lactones (AHLs), a class of signalling compounds involved in quorum sensing, and β-lactam antibiotics. Thus, MacQ is crucial as a quencher of quorum sensing as well as in conferring antibiotic resistance in Acidovorax. Here, we report the X-ray structures of MacQ in ligand-free and reaction product complexes. MacQ forms a 170-kDa capsule-shaped molecule via face-to-face interaction with two heterodimers consisting of an α-chain and a β-chain, generated by the self-cleaving activity of a precursor polypeptide. The electron density of the spacer polypeptide in the hollow of the molecule revealed the close orientation of the peptide-bond atoms of Val20SP-Gly21SP to the active-site, implying a role of the residues in substrate binding. In mutational analyses, uncleaved MacQ retained degradation activity against both AHLs and penicillin G. These results provide novel insights into the mechanism of self-cleaving maturation and enzymatic function of N-terminal nucleophile hydrolases.
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