Enzymatic activities in cultured human lymphocytes that dephosphorylate dolichyl pyrophosphate and dolichyl phosphate.
Enzymatic activities which dephosphorylate dolichyl phosphate (Dol-P) and dolichyl pyrophosphate (Dol-P-P) have been observed in membranes from cultured human lymphocytes. Neither activity requires divalent metals. Dol-P phosphatase is inhibited by inorganic phosphate but not by other phosphate-containing compounds. Dol-P-P phosphatase is inhibited by bacitracin but not by phosphate-containing compounds including the methylene analogue of pyrophosphate. These reactions are similar to those previously found in the cycle of bacterial wall peptidoglycan biosynthesis. A chemical synthesis of [32P]Dol-P and [32P]Dol-P-P is reported.
D001414:Bacitracin / Q000494:pharmacology; D002478:Cells, Cultured; D004288:Dolichol Phosphates / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008214:Lymphocytes / Q000201:enzymology*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D010761:Phosphorus Radioisotopes; D011106:Polyisoprenyl Phosphates / Q000378:metabolism*
D004288:Dolichol Phosphates; D010761:Phosphorus Radioisotopes; D011106:Polyisoprenyl Phosphates; D001414:Bacitracin; D010744:Phosphoric Monoester Hydrolases