Evidence map›Paper›PMID 23071703›Full record

ArticlePloS one2012

Structural and enzymatic characterization of the lactonase SisLac from Sulfolobus islandicus.

Julien Hiblot, Guillaume Gotthard, Eric Chabriere, Mikael Elias

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.8field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

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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.

2 · The registry

The trial behind it

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3 · Its place in the literature

Who cites it

43 citing papers in PubMed, 85 citations in OpenAlex.

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  12. An Engineered β-Hairpin Peptide Forming Thermostable Complexes with ZnChembiochem : a European journal of chemical biology · 2023
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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

4 authors at 3 institutions in 2 countries.

Julien HiblotURMITE UMR CNRS-IRD 6236, IFR48, Faculté de Médecine et de Pharmacie, Université de la Méditerranée, Marseille, France.
Guillaume Gotthard
Eric Chabriere
Mikael Elias
Unité de Recherche sur les Maladies Infectieuses et Tropicales Emergentes · FRInstitut de Recherche pour le Développement · FRWeizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundA new member of the Phosphotriesterase-Like Lactonases (PLL) family from the hyperthermophilic archeon Sulfolobus islandicus (SisLac) has been characterized. SisLac is a native lactonase that exhibits a high promiscuous phosphotriesterase activity. SisLac thus represents a promising target for engineering studies, exhibiting both detoxification and bacterial quorum quenching abilities, including human pathogens such as Pseudomonas aeruginosa. METHODOLOGY/PRINCIPAL

findingsHere, we describe the substrate specificity of SisLac, providing extensive kinetic studies performed with various phosphotriesters, esters, N-acyl-homoserine lactones (AHLs) and other lactones as substrates. Moreover, we solved the X-ray structure of SisLac and structural comparisons with the closely related SsoPox structure highlighted differences in the surface salt bridge network and the dimerization interface. SisLac and SsoPox being close homologues (91% sequence identity), we undertook a mutational study to decipher these structural differences and their putative consequences on the stability and the catalytic properties of these proteins. CONCLUSIONS/SIGNIFICANCE: We show that SisLac is a very proficient lactonase against aroma lactones and AHLs as substrates. Hence, data herein emphasize the potential role of SisLac as quorum quenching agent in Sulfolobus. Moreover, despite the very high sequence homology with SsoPox, we highlight key epistatic substitutions that influence the enzyme stability and activity.

Indexed as

Acyl-ButyrolactonesAmino Acid SequenceCrystallography, X-RayEnzyme StabilityEsterasesHydrogen-Ion ConcentrationKineticsModels, MolecularMolecular Sequence DataPhosphoric Triester HydrolasesProtein ConformationProtein MultimerizationQuorum SensingSequence Homology, Amino AcidSubstrate SpecificitySulfolobusAcyl-ButyrolactonesEsterasesPhosphoric Triester Hydrolases

Identifiers

PMID23071703
PMCPMC3468530
OpenAlexW2039905950

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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.