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Journal of Lipid Research, Vol. 11, 394-403, September 1970
Copyright © 1970 by Lipid Research, Inc.

Enzymatic synthesis and decarboxylation of phosphatidylserine in Tetrahymena pyriformis

Edward A. Dennis and Eugene P. Kennedy

Department of Biological Chemistry, Harvard Medical School, Boston, Massachusetts 02115

Cell-free extracts of the protozoan Tetrahymena pyriformis have been found to catalyze the following reactions:

Phosphatidylethanolamine + l-Serine Phosphatidylserine + Ethanolamine

Phosphatidylserine Phosphatidylethanolamine + CO₂ / Net: l-Serine Ethanolamine + CO₂

The biosynthesis of phosphatidylserine in this organism resembles that found in higher animals. In contrast, phosphatidylserine is formed in bacteria in a reaction between CDP-diglyceride and l-serine. A detailed description is presented of the enzyme that catalyzes the synthesis of phosphatidylserine in Tetrahymena by the exchange reaction, together with some properties of the phosphatidylserine decarboxylase in this organism.

Supplementary key words biosynthesis • exchange enzyme • mechanism • phosphatidylethanolamine • phosphatidylserine decarboxylase • phospholipids

Submitted on January 28, 1970
Accepted on April 29, 1970

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