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J. Biol. Chem., Vol. 265, Issue 13, 7221-7226, May, 1990
M Bae-Lee and GM Carman
The regulation of purified yeast membrane-associated phosphatidylserine
synthase (CDP-diacylglycerol:L-serine O-phosphatidyltransferase, EC
2.7.8.8) and phosphatidylinositol synthase (CDP-diacylglycerol:myo-
inositol 3-phosphatidyltransferase, EC 2.7.8.11) activities by
phospholipids was examined using Triton X-100/phospholipid mixed micelles.
Phosphatidate, phosphatidylcholine, and phosphatidylinositol stimulated
phosphatidylserine synthase activity, whereas cardiolipin and the neutral
lipid diacylglycerol inhibited enzyme activity. Phosphatidate was a potent
activator of phosphatidylserine synthase activity with an apparent
activation constant (0.033 mol %) 88-fold lower than the apparent Km (2.9
mol %) for the surface concentration of CDP-diacylglycerol. Phosphatidate
caused an increase in the apparent Vmax and a decrease in the apparent Km
for the enzyme with respect to the surface concentration of
CDP-diacylglycerol. Phosphatidylcholine and phosphatidylinositol caused an
increase in the apparent Vmax for phosphatidylserine synthase with respect
to CDP-diacylglycerol with apparent activation constants of 3.4 and 3.2 mol
%, respectively. Cardiolipin and diacylglycerol were competitive inhibitors
of phosphatidylserine synthase activity with respect to CDP-
diacylglycerol. The apparent Ki value for cardiolipin (0.7 mol %) was 4-
fold lower than the apparent Km for CDP-diacylglycerol, whereas the
apparent Ki for diacylglycerol (7 mol %) was 2.4-fold higher than the
apparent Km for CDP-diacylglycerol. Phosphatidylethanolamine and
phosphatidylglycerol did not affect phosphatidylserine synthase activity.
Phosphatidylinositol synthase activity was not significantly effected by
lipids. The role of lipid activators and inhibitors on phosphatidylserine
synthase activity is discussed in relation to overall lipid metabolism.
Regulation of yeast phosphatidylserine synthase and phosphatidylinositol synthase activities by phospholipids in Triton X- 100/phospholipid mixed micelles
Department of Food Science, Cook College, New Jersey Agricultural Experiment Station, Rutgers University, New Brunswick 08903.
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