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Biochemical Characterization of Glucosylglycerol-Phosphate Synthase of Synechocystis sp. Strain PCC 6803: Comparison of Crude, Purified, and Recombinant Enzymes

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Abstract

Glucosylglycerol-phosphate synthase (GGPS), the key enzyme of the glucosylglycerol biosynthesis in salt-stressed cells of Synechocystis, was biochemically analyzed in crude extracts, after partial purification by FPLC and after overexpression of the gene ggpS in Escherichia coli and purification to homogenity of the recombinant protein, respectively. These GGPS preparations behaved similarly with regard to temperature stability, pH optimum, Mg2+ dependence, inhibition by phosphates, and Km values, but differed in their dependence on NaCl concentration: crude enzyme needed activation by addition of NaCl, whereas both partially-purified and recombinant GGPS showed high activities independent of the NaCl concentration.

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Authors and Affiliations

  1. Department of Biology, University of Rostock, Doberaner Str. 143, 18051 Rostock, Germany, , , , , , DE

    Martin Hagemann, Uta Effmert, Thomas Kerstan & Norbert Erdmann

  2. Department of Biology, Ernst-Moritz-Arndt-Universität, Grimmer Str. 88, 17487 Greifswald, Germany, , , , , , DE

    Arne Schoor

Authors
  1. Martin Hagemann
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  2. Uta Effmert
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  3. Thomas Kerstan
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  4. Arne Schoor
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  5. Norbert Erdmann
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Received: 19 January 2001 / Accepted: 21 February 2001

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Hagemann, M., Effmert, U., Kerstan, T. et al. Biochemical Characterization of Glucosylglycerol-Phosphate Synthase of Synechocystis sp. Strain PCC 6803: Comparison of Crude, Purified, and Recombinant Enzymes. Curr Microbiol 43, 278–283 (2001). https://doi.org/10.1007/s002840010301

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  • DOI: https://doi.org/10.1007/s002840010301

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