ArticleJournal of bacteriology2011
A specialized aspartokinase enhances the biosynthesis of the osmoprotectants ectoine and hydroxyectoine in Pseudomonas stutzeri A1501.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 74 citations in OpenAlex.
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- Biosynthesis and import of the cytoprotective extremolytes ectoine and hydroxyectoine in the phylumFrontiers in microbiology · 2026Article
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- Metabolic response ofFrontiers in microbiology · 2026Article
- Bacterial osmoprotectants-a way to survive in saline conditions and potential crop allies.FEMS microbiology reviews · 2025Review
- Intracellular self-assembly and metabolite analysis of key enzymes for L-lysine synthesis based on key components of cellulosomes.Frontiers in microbiology · 2025Article
- Metagenomics-assembled genomes reveal microbial metabolic adaptation to athalassohaline environment, the case Lake Barkol, China.Frontiers in microbiology · 2025Article
- Rational engineering of Halomonas salifodinae to enhance hydroxyectoine production under lower-salt conditions.Applied microbiology and biotechnology · 2024Article
- Comparative genomic analysis of Halomonas campaniensis wild-type and ultraviolet radiation-mutated strains reveal genomic differences associated with increased ectoine production.International microbiology : the official journal of the Spanish Society for Microbiology · 2023Article
- Metabolic engineering of Halomonas campaniensis strain XH26 to remove competing pathways to enhance ectoine production.Scientific reports · 2023Article
- Ectoine Effect on Mechanical Properties of Vesicles in Aqueous Solution.The Journal of membrane biology · 2022Article
- Genome analysis of the salt-resistant Paludifilum halophilum DSM 102817World journal of microbiology & biotechnology · 2021Article
- Dual-function oleaginous biocatalysts for non-sterile cultivation and solvent-free biolipid bioextraction to reduce biolipid-based biofuel production costs.The Science of the total environment · 2021Article
- Comparative Genomics ofFrontiers in microbiology · 2021Article
- Stressed out: Bacterial response to high salinity using compatible solute biosynthesis and uptake systems, lessons fromComputational and structural biotechnology journal · 2021Review
- Osmotic Adaptation and Compatible Solute Biosynthesis of Phototrophic Bacteria as Revealed from Genome Analyses.Microorganisms · 2020Article
- From Organic Wastes to Bioplastics: Feasibility of Nonsterile Poly(3-hydroxybutyrate) Production byACS omega · 2020Article
- 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
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The compatible solutes ectoine and hydroxyectoine are widely produced by bacteria as protectants against osmotic and temperature stress. l-Aspartate-beta-semialdehyde is used as the precursor molecule for ectoine/hydroxyectoine biosynthesis that is catalyzed by the EctABCD enzymes. l-Aspartate-beta-semialdehyde is a central intermediate in different biosynthetic pathways and is produced from l-aspartate by aspartokinase (Ask) and aspartate-semialdehyde-dehydrogenase (Asd). Ask activity is typically stringently regulated by allosteric control to avoid gratuitous synthesis of aspartylphosphate. Many organisms have evolved multiple forms of aspartokinase, and feedback regulation of these specialized Ask enzymes is often adapted to the cognate biochemical pathways. The ectoine/hydroxyectoine biosynthetic genes (ectABCD) are followed in a considerable number of microorganisms by an askgene (ask_ect), suggesting that Ask_Ect is a specialized enzyme for this osmoadaptive biosynthetic pathway. However, none of these Ask_Ect enzymes have been functionally characterized. Pseudomonas stutzeri A1501 synthesizes both ectoine and hydroxyectoine in response to increased salinity, and it possesses two Ask enzymes: Ask_Lys and Ask_Ect. We purified both Ask enzymes and found significant differences with regard to their allosteric control: Ask_LysC was inhibited by threonine and in a concerted fashion by threonine and lysine, whereas Ask_Ect showed inhibition only by threonine. The ectABCD_askgenes from P. stutzeri A1501 were cloned and functionally expressed in Escherichia coli, and this led to osmostress protection. An E. colistrain carrying the plasmid-based ectABCD_askgene cluster produced significantly more ectoine/hydroxyectoine than a strain expressing the ectABCDgene cluster alone. This finding suggests a specialized role for Ask_Ect in ectoine/hydroxyectoine biosynthesis.
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