The 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 alpha-saturated C-55 polyisoprenylphosphate.
D000117:Acetylglucosamine / Q000378:metabolism; D002454:Cell Differentiation; D002462:Cell Membrane / Q000201:enzymology; D004023:Dictyostelium / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D005643:Fucose / Q000378:metabolism; D006602:Hexosyltransferases / Q000378:metabolism*; D008358:Mannose / Q000378:metabolism; D011106:Polyisoprenyl Phosphates / Q000378:metabolism*; D013329:Structure-Activity Relationship
D011106:Polyisoprenyl Phosphates; C029686:alpha-dihydroisoprenylphosphates; D005643:Fucose; D006602:Hexosyltransferases; D008358:Mannose; D000117:Acetylglucosamine