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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