The plant Selaginella moellendorffii possesses enzymes for synthesis and hydrolysis of the compatible solutes mannosylglycerate and glucosylglycerate |
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Authors: | Ana Nobre Nuno Empadinhas Maria Fernanda Nobre Eva Correia Lourenço Christopher Maycock Maria Rita Ventura Ana Mingote Milton S da Costa |
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Institution: | 1. CNC, Center for Neuroscience and Cell Biology, University of Coimbra, 3004-517, Coimbra, Portugal 2. Department of Life Sciences, University of Coimbra, 3001-401, Coimbra, Portugal 3. ITQB, Institute of Chemical and Biological Technology, New University of Lisbon, 2780-901, Oeiras, Portugal 4. Department of Chemistry and Biochemistry, Faculty of Sciences, University of Lisbon, 1749-016, Lisbon, Portugal
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Abstract: | A mannosylglycerate synthase (MgS) gene detected in the genome of Selaginella moellendorffii was expressed in E. coli and the recombinant enzyme was purified and characterized. A remarkable and unprecedented feature of this enzyme was the ability to efficiently synthesize mannosylglycerate (MG) and glucosylglycerate (GG) alike, with maximal activity at 50 °C, pH 8.0 and with Mg2+ as reaction enhancer. We have also identified a novel glycoside hydrolase gene in this plant’s genome, which was functionally confirmed to be highly specific for the hydrolysis of MG and GG and named MG hydrolase (MgH), due to its homology with bacterial MgHs. The recombinant enzyme was maximally active at 40 °C and at pH 6.0–6.5. The activity was independent of cations, but Mn2+ was a strong stimulator. Regardless of these efficient enzymatic resources we could not detect MG or GG in S. moellendorffii or in the extracts of five additional Selaginella species. Herein, we describe the properties of the first eukaryotic enzymes for the synthesis and hydrolysis of the compatible solutes, MG and GG. |
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