Effectivity of dolichyl phosphates with different chain lengths as acceptors of nucleotide activated sugars.
Chemical synthesis of different S-forms of dolichyl-P was performed in order to investigate the use of these polyprenes in mannosyl, glucosyl and glucosaminyl transferase reactions. Determination of the Vmax values for a series of dolichyl-P demonstrated that the velocities of transferase reactions with all those dolichyl-P derivatives present in animal tissues are largely the same. The apparent Km values for the various dolichyl-P in the transferase system studied differed, but this property does not appear to have physiological importance.
D000818:Animals; D002250:Carbon Radioisotopes; D004288:Dolichol Phosphates / Q000378:metabolism*; D006155:Guanosine Diphosphate Mannose / Q000378:metabolism*; D006602:Hexosyltransferases / Q000378:metabolism*; D007700:Kinetics; D008862:Microsomes, Liver / Q000201:enzymology*; D009702:Nucleoside Diphosphate Sugars / Q000378:metabolism*; D011106:Polyisoprenyl Phosphates / Q000378:metabolism*; D051381:Rats; D013379:Substrate Specificity; D014532:Uridine Diphosphate Glucose / Q000378:metabolism*; D014537:Uridine Diphosphate N-Acetylglucosamine / Q000378:metabolism*; D014539:Uridine Diphosphate Sugars / Q000378:metabolism*
D002250:Carbon Radioisotopes; D004288:Dolichol Phosphates; D009702:Nucleoside Diphosphate Sugars; D011106:Polyisoprenyl Phosphates; D014539:Uridine Diphosphate Sugars; D006155:Guanosine Diphosphate Mannose; D014537:Uridine Diphosphate N-Acetylglucosamine; D006602:Hexosyltransferases; D014532:Uridine Diphosphate Glucose