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. 1981 May;67(5):922–925. doi: 10.1104/pp.67.5.922

Phosphatidylethanolamine Synthesis in Castor Bean Endosperm 1

Salvatore A Sparace 1,2, Leslie K Wagner 1, Thomas S Moore Jr 1
PMCID: PMC425801  PMID: 16661793

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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