Mannosyltransferases in plasma membranes of Dictyostelium discoideum synthesize polyisoprenylphosphomannosides from exogenous polyisoprenylphosphates and GDP-mannose. The specificity of the enzymes depends on the chain length and the saturation of the polyisoprenols. Maximum activity is reached by a alpha-saturated C-55 polyisoprenylphosphate.
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