ArticleThe Journal of biological chemistry2020
Degradation of the microbial stress protectants and chemical chaperones ectoine and hydroxyectoine by a bacterial hydrolase-deacetylase complex.
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 10 papers.
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Who cites it
10 citing papers in PubMed.
- Deciphering the evolutionary history of ectoine catabolism, a compatible solute utilized byApplied and environmental microbiology · 2026Article
- Differences in composition and potential function of the bacterial communities of cave- and surface-dwelling Mexican salamanders.Animal microbiome · 2025Article
- Rational engineering of Halomonas salifodinae to enhance hydroxyectoine production under lower-salt conditions.Applied microbiology and biotechnology · 2024Article
- Properties and biotechnological applications of microbial deacetylase.Applied microbiology and biotechnology · 2023Review
- Bioactivity profiling of the extremolyte ectoine as a promising protectant and its heterologous production.3 Biotech · 2022Review
- The Retrospective on AtypicalMicroorganisms · 2022Review
- Enhancing ectoine production by recombinant Escherichia coli through step-wise fermentation optimization strategy based on kinetic analysis.Bioprocess and biosystems engineering · 2021Article
- Microbial production of ectoine and hydroxyectoine as high-value chemicals.Microbial cell factories · 2021Review
- Stressed out: Bacterial response to high salinity using compatible solute biosynthesis and uptake systems, lessons fromComputational and structural biotechnology journal · 2021Review
- The MocR/GabR Ectoine and Hydroxyectoine Catabolism Regulator EnuR: Inducer and DNA Binding.Frontiers in microbiology · 2021Article
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
When faced with increased osmolarity in the environment, many bacterial cells accumulate the compatible solute ectoine and its derivative 5-hydroxyectoine. Both compounds are not only potent osmostress protectants, but also serve as effective chemical chaperones stabilizing protein functionality. Ectoines are energy-rich nitrogen and carbon sources that have an ecological impact that shapes microbial communities. Although the biochemistry of ectoine and 5-hydroxyectoine biosynthesis is well understood, our understanding of their catabolism is only rudimentary. Here, we combined biochemical and structural approaches to unravel the core of ectoine and 5-hydroxy-ectoine catabolisms. We show that a conserved enzyme bimodule consisting of the EutD ectoine/5-hydroxyectoine hydrolase and the EutE deacetylase degrades both ectoines. We determined the high-resolution crystal structures of both enzymes, derived from the salt-tolerant bacteria
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