Calmodulin-dependent enzymic phosphorylation of dolichol in Tetrahymena pyriformis.

The Protozoan, Tetrahymena pyriformis, is capable of phosphorylating dolichol in the presence of CTP. Other nucleotides (ATP, UTP and GTP) were ineffective. The enzyme was activated independently by the bivalent cations Mg2+, Mn2+ and Ca2+. The Ca2+ stimulation of the enzyme activity was calmodulin-dependent. A substantial increase in the enzyme activity was seen in the presence of UTP. The apparent Km values for CTP and dolichol, as calculated from the Lineweaver-Burk plot, were 3 mM and 70 microM respectively. Although the presence of detergent was essential, at higher concentrations there was a decrease in the enzyme activity. The enzyme had two pH optima (pH 7.4 and 9.0) and at both the activity was Ca2+-calmodulin-dependent.