ArticleThe Journal of biological chemistry2020
The architecture of the diaminobutyrate acetyltransferase active site provides mechanistic insight into the biosynthesis of the chemical chaperone ectoine.
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- Biosynthesis and import of the cytoprotective extremolytes ectoine and hydroxyectoine in the phylumFrontiers in microbiology · 2026Article
- Genomic and Transcriptomic Analyses Reveal Multiple Strategies forFoods (Basel, Switzerland) · 2024Article
- Metabolic engineering of Halomonas campaniensis strain XH26 to remove competing pathways to enhance ectoine production.Scientific reports · 2023Article
- Protective effect of the stressed supernatant from Lactococcus lactis subsp. lactis and its metabolic analysis.Archives of microbiology · 2022Article
- Enhancing ectoine production by recombinant Escherichia coli through step-wise fermentation optimization strategy based on kinetic analysis.Bioprocess and biosystems engineering · 2021Article
- Development of a Pantetheine Force Field Library for Molecular Modeling.Journal of chemical information and modeling · 2021Article
- Metagenomic Insights Into Functional and Taxonomic Compositions of an Activated Sludge Microbial Community Treating Leachate of a Completed Landfill: A Pathway-Based Analysis.Frontiers in microbiology · 2021Article
- Gcn5-RelatedFrontiers in molecular biosciences · 2021Article
- Degradation of the microbial stress protectants and chemical chaperones ectoine and hydroxyectoine by a bacterial hydrolase-deacetylase complex.The Journal of biological chemistry · 2020Article
Corrections and comments
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Authors and funding
10 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ectoine is a solute compatible with the physiologies of both prokaryotic and eukaryotic cells and is widely synthesized by bacteria as an osmotic stress protectant. Because it preserves functional attributes of proteins and macromolecular complexes, it is considered a chemical chaperone and has found numerous practical applications. However, the mechanism of its biosynthesis is incompletely understood. The second step in ectoine biosynthesis is catalyzed by l-2,4-diaminobutyrate acetyltransferase (EctA; EC 2.3.1.178), which transfers the acetyl group from acetyl-CoA to EctB-formed l-2,4-diaminobutyrate (DAB), yielding
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Registered trials
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