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Partially purified trehalose phosphorylase (EC 2.4.1.64) from Euglena gracilis SM-ZK was inhibited by fructose 2,6-bisphosphate in both synthetic and degradative directions. Ki value for trehalose phosphorolysis was 1.2 microM and that for trehalose synthesis was 0.5 microM. Functions of fructose 2,6-bisphosphate in Euglena, particularly in the regulative mechanism of the two reserve carbohydrates, paramylon and trehalose, are discussed.
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