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dependence of glycosyltransferases in Dictyostelium discoideum on the structure of polyisoprenols

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...

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Bibliographic Details
Published in:Molecular and cellular biochemistry 1981-01, Vol.34 (2), p.65-72
Main Authors: Rossler, H.H, Schneider-Seelbach, E, Malati, T, Risse, H.J
Format: Article
Language:English
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Summary: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.
ISSN:0300-8177
1573-4919
DOI:10.1007/BF02354860