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J. Biol. Chem., Vol. 259, Issue 17, 10857-10862, Sep, 1984
MS Bae-Lee and GM Carman
Membrane-associated phosphatidylserine synthase (CDP-diacylglycerol:L-
serine O-phosphatidyltransferase, EC 2.7.8.8) was purified from the
microsomal fraction of Saccharomyces cerevisiae strains S288C and
VAL2C(YEpCHO1). VAL2C(YEpCHO1) contains a hybrid plasmid bearing the
structural gene for phosphatidylserine synthase and overproduces the enzyme
6-7 fold (Letts, V. A., Klig, L. S., Bae-Lee, M., Carman, G. M., and Henry,
S. A. (1983) Proc. Natl. Acad. Sci. U. S. A. 80, 7279-7283) compared to
wild-type S288C. The purification procedure included Triton X-100
extraction of the microsomal membranes, CDP-diacylglycerol- Sepharose
affinity chromatography, and DE-53 chromatography. The procedure yielded a
preparation from each strain containing a major peptide band (Mr = 23,000)
upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
Phosphatidylserine synthase was dependent on manganese and Triton X-100 for
maximum activity at pH 8.0. The apparent Km values for serine and
CDP-diacylglycerol were 0.58 mM and 60 microM, respectively. Thioreactive
agents inhibited enzyme activity. The enzyme was thermally labile above 40
degrees C. Results of isotopic exchange reactions between substrates and
products suggest that the enzyme catalyzes a sequential Bi Bi reaction.
Phosphatidylserine synthesis in Saccharomyces cerevisiae. Purification and characterization of membrane-associated phosphatidylserine synthase
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