ArticleJournal of bacteriology2004
A gene from the mesophilic bacterium Dehalococcoides ethenogenes encodes a novel mannosylglycerate synthase.
Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 38 citations in OpenAlex.
- Substrate-driven microbial specialization and cooperative dechlorination of chlorinated pollutants in estuarine ecosystems.Applied and environmental microbiology · 2026Article
- Exploring the Potential ofFrontiers in bioengineering and biotechnology · 2021Article
- Production of mannosylglycerate in Saccharomyces cerevisiae by metabolic engineering and bioprocess optimization.Microbial cell factories · 2018Article
- Genome sequence of the organohalide-respiring Dehalogenimonas alkenigignens type strain (IP3-3(T)).Standards in genomic sciences · 2016Article
- Experimental validation of in silico model-predicted isocitrate dehydrogenase and phosphomannose isomerase from Dehalococcoides mccartyi.Microbial biotechnology · 2016Article
- Mannosylglycerate: structural analysis of biosynthesis and evolutionary history.Extremophiles : life under extreme conditions · 2014Review
- Genome sequencing of a single cell of the widely distributed marine subsurface Dehalococcoidia, phylum Chloroflexi.The ISME journal · 2014Article
- Article
- Organic cofactors in the metabolism of Dehalococcoides mccartyi strains.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Article
- Complete genome sequence of Dehalogenimonas lykanthroporepellens type strain (BL-DC-9(T)) and comparison to "Dehalococcoides" strains.Standards in genomic sciences · 2012Article
- Single-step pathway for synthesis of glucosylglycerate in Persephonella marina.Journal of bacteriology · 2007Article
- Glucosylglycerate biosynthesis in the deepest lineage of the Bacteria: characterization of the thermophilic proteins GpgS and GpgP from Persephonella marina.Journal of bacteriology · 2007Article
- Characterization of the biosynthetic pathway of glucosylglycerate in the archaeon Methanococcoides burtonii.Journal of bacteriology · 2006Article
- Compatible solutes of the hyperthermophile Palaeococcus ferrophilus: osmoadaptation and thermoadaptation in the order thermococcales.Applied and environmental microbiology · 2005Article
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7 authors at 4 institutions in 2 countries.
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Abstract
Mannosylglycerate (MG) is a common compatible solute found in thermophilic and hyperthermophilic prokaryotes. In this study we characterized a mesophilic and bifunctional mannosylglycerate synthase (MGSD) encoded in the genome of the bacterium Dehalococcoides ethenogenes. mgsD encodes two domains with extensive homology to mannosyl-3-phosphoglycerate synthase (MPGS, EC 2.4.1.217) and to mannosyl-3-phosphoglycerate phosphatase (MPGP, EC 3.1.3.70), which catalyze the consecutive synthesis and dephosphorylation of mannosyl-3-phosphoglycerate to yield MG in Pyrococcus horikoshii, Thermus thermophilus, and Rhodothermus marinus. The bifunctional MGSD was overproduced in Escherichia coli, and we confirmed the combined MPGS and MPGP activities of the recombinant enzyme. The optimum activity of the enzyme was at 50 degrees C. To examine the properties of each catalytic domain of MGSD, we expressed them separately in E. coli. The monofunctional MPGS was unstable, while the MPGP was stable and was characterized. Dehalococcoides ethenogenes cannot be grown sufficiently to identify intracellular compatible solutes, and E. coli harboring MGSD did not accumulate MG. However, Saccharomyces cerevisiae expressing mgsD accumulated MG, confirming that this gene product can synthesize this compatible solute and arguing for a role in osmotic adjustment in the natural host. We did not detect MGSD activity in cell extracts of S. cerevisiae. Here we describe the first gene and enzyme for the synthesis of MG from a mesophilic microorganism and discuss the possible evolution of this bifunctional MGSD by lateral gene transfer from thermophilic and hyperthermophilic organisms.
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