ArticleScientific reports2019
Illuminating the catalytic core of ectoine synthase through structural and biochemical analysis.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed, 39 citations in OpenAlex.
- Biosynthesis and import of the cytoprotective extremolytes ectoine and hydroxyectoine in the phylumFrontiers in microbiology · 2026Article
- A Structural Landscape Depiction of Dynamic Stability Centers of Local Structure in Protein Thermostability Engineering.Research (Washington, D.C.) · 2026Article
- Multiple Functions of Compatible Solute Ectoine and Strategies for Constructing Overproducers for Biobased Production.Molecular biotechnology · 2024Review
- Bioactivity profiling of the extremolyte ectoine as a promising protectant and its heterologous production.3 Biotech · 2022Review
- Whole-Genome Sequencing of the Tropical Marine Bacterium Nocardiopsis dassonvillei NCIM 5124, Containing the Ectoine Biosynthesis Gene ClusterMicrobiology resource announcements · 2022Article
- Genome analysis suggests the bacterial family Acetobacteraceae is a source of undiscovered specialized metabolites.Antonie van Leeuwenhoek · 2022Article
- Re-classification ofiScience · 2021Article
- Halomonas sedimenti sp. nov., a Halotolerant Bacterium Isolated from Deep-Sea Sediment of the Southwest Indian Ocean.Current microbiology · 2021Article
- Desert Environments Facilitate Unique Evolution of Biosynthetic Potential inMolecules (Basel, Switzerland) · 2021Article
- Isolation and Evaluation of Rhizosphere Actinomycetes With Potential Application for BiocontrollingFrontiers in microbiology · 2021Article
- The MocR/GabR Ectoine and Hydroxyectoine Catabolism Regulator EnuR: Inducer and DNA Binding.Frontiers in microbiology · 2021Article
- Boosting Escherichia coli's heterologous production rate of ectoines by exploiting the non-halophilic gene cluster from Acidiphilium cryptum.Extremophiles : life under extreme conditions · 2020Article
- Degradation of the microbial stress protectants and chemical chaperones ectoine and hydroxyectoine by a bacterial hydrolase-deacetylase complex.The Journal of biological chemistry · 2020Article
- The architecture of the diaminobutyrate acetyltransferase active site provides mechanistic insight into the biosynthesis of the chemical chaperone ectoine.The Journal of biological chemistry · 2020Article
- Biosynthesis of the Stress-Protectant and Chemical Chaperon Ectoine: Biochemistry of the Transaminase EctB.Frontiers in microbiology · 2019Article
- Amphibian skin-associated Pigmentiphaga: Genome sequence and occurrence across geography and hosts.PloS one · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ectoine synthase (EctC) is the signature enzyme for the production of ectoine, a compatible solute and chemical chaperone widely synthesized by bacteria as a cellular defense against the detrimental effects of osmotic stress. EctC catalyzes the last step in ectoine synthesis through cyclo-condensation of the EctA-formed substrate N-gamma-acetyl-L-2,4-diaminobutyric acid via a water elimination reaction. We have biochemically and structurally characterized the EctC enzyme from the thermo-tolerant bacterium Paenibacillus lautus (Pl). EctC is a member of the cupin superfamily and forms dimers, both in solution and in crystals. We obtained high-resolution crystal structures of the (Pl)EctC protein in forms that contain (i) the catalytically important iron, (ii) iron and the substrate N-gamma-acetyl-L-2,4-diaminobutyric acid, and (iii) iron and the enzyme reaction product ectoine. These crystal structures lay the framework for a proposal for the EctC-mediated water-elimination reaction mechanism. Residues involved in coordinating the metal, the substrate, or the product within the active site of ectoine synthase are highly conserved among a large group of EctC-type proteins. Collectively, the biochemical, mutational, and structural data reported here yielded detailed insight into the structure-function relationship of the (Pl)EctC enzyme and are relevant for a deeper understanding of the ectoine synthase family as a whole.
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.