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A novel thermostable prokaryotic fucoidan active sulfatase PsFucS1 with an unusual quaternary hexameric structure

Sci Rep. 2021-09; 
Maria Dalgaard Mikkelsen, Hang Thi Thuy Cao, Thomas Roret, Nanna Rhein-Knudsen, Jesper Holck, Van Thi Thanh Tran, Thuan Thi Nguyen, Vy Ha Nguyen Tran, Mateusz Jakub Lezyk, Jan Muschiol, Thinh Duc Pham, Mirjam Czjzek, Anne S Meyer
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Custom Vector Construction … coli expression), all devoid of their original signal peptide, were synthesized by GenScript (Piscataway, NJ, USA) and delivered inserted into the pET-45b(+) vector between the KpnI and PacI restriction sites. The E. coli strain DH5α (Invitrogen, Waltham, MA, USA), was used as … Get A Quote

摘要

Fucoidans are sulfated, fucose-rich marine polysaccharides primarily found in cell walls of brown seaweeds (macroalgae). Fucoidans are known to possess beneficial bioactivities depending on their structure and sulfation degree. Here, we report the first functional characterization and the first crystal structure of a prokaryotic sulfatase, PsFucS1, belonging to sulfatase subfamily S1_13, able to release sulfate from fucoidan oligosaccharides. PsFucS1 was identified in the genome of a Pseudoalteromonas sp. isolated from sea cucumber gut. PsFucS1 (57 kDa) is Ca dependent and has an unusually high optimal temperature (68 °C) and thermostability. Further, the PsFucS1 displays a unique quaternary hexameric struct... More

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