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Plant Physiology 53:171-175 (1974)
© 1974 American Society of Plant Biologists

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Biosynthesis of Phosphatidylethanolamine by Enzyme Preparations from Plant Tissues

B. A. Macher and J. B. Mudd

Department of Biochemistry and Statewide Air Pollution Research Center, University of California, Riverside, California 92502

The enzymic utilization of cytidine diphosphoethanolamine in the synthesis of phosphatidylethanolamine is localized in the microsomal fraction of spinach (Spinacia oleracea) leaves. The metal ion requirement can be satisfied by Mn2+ (saturation approximately 0.6 mM) or Mg2+ (saturation approximately 25 mM). The enzyme has a pH optimum of 8.0 in the presence of Mn2+ and 7.5 in the presence of Mg2+. A Michaelis constant of 20 µM was determined for cytidinediphos-phoethanolamine. Enzyme activity was stimulated by thiol compounds and inhibited by thiol reagents. No inhibition was obtained with cytidine monophosphate and Tween 80.

The in vitro biosynthesis of phosphatidylethanolamine was inhibited by cytidine diphosphocholine and the biosynthesis of phosphatidylcholine was inhibited by cytidine diphosphoethanolamine. Activities of the two synthetic systems were indistinguishable on the basis of susceptibility to lyophilization and inhibition by thiol reagents.




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Copyright © 1974 by the American Society of Plant Biologists