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Plant Physiology 67:922-925 (1981)
© 1981 American Society of Plant Biologists

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Articles

Phosphatidylethanolamine Synthesis in Castor Bean Endosperm 1

Salvatore A. Sparace2, Leslie K. Wagner and Thomas S. Moore, Jr.

Department of Botany, University of Wyoming, Laramie, Wyoming 82071

Phosphatidylethanolamine synthesis by CDP-ethanolamine:1,2-diacylglycerol ethanolaminephosphotransferase (EC 2.7.8.1) from the endoplasmic reticulum of castor bean (Ricinus communis L. var. Hale) endosperm was characterized. The Michaelis-Menten constant of the enzyme for CDP-ethanolamine was approximately 8.0 micromolar. The pH optimum was 6.5 and a divalent cation was an absolute requirement for activity, with Mg2+ giving the greatest stimulation at 3 millimolar. Sulfhydryl reagents variously affected enzyme activity. No discernible differences were detected between the responses of the ethanolaminephosphotransferase and CDP-choline:1,2-diacylglycerol cholinephosphotransferase (EC 2.7.8.2) to a variety of treatments. CDP-choline and CDP-ethanolamine were competitive inhibitors of the ethanolaminephosphotransferase and cholinephosphotransferase reactions, respectively.

2 Present address: Department of Biochemistry, University of California, Riverside, CA 92521.

1 This investigation was supported by National Science Foundation Grant PCM78-061817.




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Y. H. Choi, J. K. Lee, C.-H. Lee, and S. H. Cho
cDNA Cloning and Expression of an Aminoalcoholphosphotransferase Isoform in Chinese Cabbage
Plant Cell Physiol., September 1, 2000; 41(9): 1080 - 1084.
[Abstract] [Full Text] [PDF]


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Copyright © 1981 by the American Society of Plant Biologists