ArticleScientific reports2015
Crystal structure of VmoLac, a tentative quorum quenching lactonase from the extremophilic crenarchaeon Vulcanisaeta moutnovskia.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed.
- The characterization of a new stabilized lactonase from the endophytic fungi Aspergillus pseudonomiae with anti-bacterial and anti-fungal properties.Protein science : a publication of the Protein Society · 2026Article
- Enzymatic quorum quenching alters the phyllosphere microbiome and suppresses a bacterial-induced plant disease.Scientific reports · 2026Article
- A Novel Screening System to Characterize and Engineer Quorum Quenching Lactonases.Biotechnology and bioengineering · 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
- Changes in Active Site Loop Conformation Relate to the Transition toward a Novel Enzymatic Activity.JACS Au · 2024Article
- Field testing of an enzymatic quorum quencher coating additive to reduce biocorrosion of steel.Microbiology spectrum · 2023Article
- Evidence for Complex Interplay between Quorum Sensing and Antibiotic Resistance in Pseudomonas aeruginosa.Microbiology spectrum · 2022Article
- The exceptionally efficient quorum quenching enzyme LrsL suppressesFrontiers in microbiology · 2022Article
- Biocontrol of Biofilm Formation: Jamming of Sessile-Associated Rhizobial Communication by Rhodococcal Quorum-Quenching.International journal of molecular sciences · 2021Article
- Unveiling the Impact of Antibiotics and Alternative Methods for Animal Husbandry: A Review.Antibiotics (Basel, Switzerland) · 2021Review
- Quorum quenching enzymes and their effects on virulence, biofilm, and microbiomes: a review of recent advances.Expert review of anti-infective therapy · 2020Review
- Discovering, Characterizing, and Applying Acyl Homoserine Lactone-Quenching Enzymes to Mitigate Microbe-Associated Problems Under Saline Conditions.Frontiers in microbiology · 2019Article
- Signal Disruption Leads to Changes in Bacterial Community Population.Frontiers in microbiology · 2019Article
- Effects of Signal Disruption Depends on the Substrate Preference of the Lactonase.Frontiers in microbiology · 2019Article
- Structural and Biochemical Characterization of AaL, a Quorum Quenching Lactonase with Unusual Kinetic Properties.Scientific reports · 2018Article
- Highly active enzymes by automated combinatorial backbone assembly and sequence design.Nature communications · 2018Article
- Optimization of Cholinesterase-Based Catalytic Bioscavengers Against Organophosphorus Agents.Frontiers in pharmacology · 2018Article
- Rational engineering of a native hyperthermostable lactonase into a broad spectrum phosphotriesterase.Scientific reports · 2017Article
- The quorum-quenching lactonase from Alicyclobacter acidoterrestris: purification, kinetic characterization, crystallization and crystallographic analysis.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Improving the 'tool box' for robust industrial enzymes.Journal of industrial microbiology & biotechnology · 2017Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A new representative of the Phosphotriesterase-Like Lactonases (PLLs) family from the hyperthermophilic crenarchaeon Vulcanisaeta moutnovskia has been characterized and crystallized. VmoLac is a native, proficient lactonase with promiscuous, low phosphotriesterase activity. VmoLac therefore represents an interesting candidate for engineering studies, with the aim of developing an efficient bacterial quorum-quenching agent. Here, we provide an extensive biochemical and kinetic characterization of VmoLac and describe the X-ray structures of the enzyme bound to a fatty acid and to its cognate substrate 3-oxo-C10 AHL (Acyl-Homoserine Lactone). The structures highlight possible structural determinants that may be involved in its extreme thermal stability (Tm = 128 °C). Moreover, the structure reveals that the substrate binding mode of VmoLac significantly differs from those of its close homologues, possibly explaining the substrate specificity of the enzyme. Finally, we describe the specific interactions between the enzyme and its substrate, and discuss the possible lactone hydrolysis mechanism of VmoLac.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.