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J Biol Chem, Vol. 274, Issue 14, 9531-9538, April 2, 1999
From the Department of Food Science, Cook College, New Jersey
Agricultural Experiment Station, Rutgers University,
New Brunswick, New Jersey 08901
The CKI1-encoded choline kinase
(ATP:choline phosphotransferase, EC 2.7.1.32) from Saccharomyces
cerevisiae was phosphorylated in vivo on multiple
serine residues. Activation of protein kinase A activity in
vivo resulted in a transient increase in the phosphorylation of
choline kinase. This phosphorylation was accompanied by a stimulation in choline kinase activity. In vitro, protein kinase A
phosphorylated choline kinase on a serine residue with a stoichiometry
(0.44 mol of phosphate/mol of choline kinase) consistent with one
phosphorylation site/choline kinase subunit. The major phosphopeptide
derived from the enzyme phosphorylated in vitro by protein
kinase A was common to one of the major phosphopeptides derived from
the enzyme phosphorylated in vivo. Protein kinase A
activity was dose- and time-dependent and dependent on the
concentrations of ATP (Km 2.1 µM)
and choline kinase (Km 0.12 µM).
Phosphorylation of choline kinase with protein kinase A resulted in a
stimulation (1.9-fold) in choline kinase activity whereas alkaline
phosphatase treatment of choline kinase resulted in a 60% decrease in
choline kinase activity. The mechanism of the protein kinase A-mediated
stimulation in choline kinase activity involved an increase in the
apparent Vmax values with respect to ATP
(2.6-fold) and choline (2.7-fold). Overall, the results reported here
were consistent with the conclusion that choline kinase was regulated
by protein kinase A phosphorylation.
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