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Phosphatidylinositol Synthesis by a Mn2+-Dependent Exchange Enzyme in Castor Bean Endosperm
Author(s) -
James C. Sexton,
Thomas Moore
Publication year - 1981
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.68.1.18
Subject(s) - phosphatidylinositol , inositol , endosperm , cytidine , chemistry , pi , transferase , enzyme , biochemistry , signal transduction , receptor
myo-Inositol is incorporated into phosphatidylinositol by an exchange reaction associated with the endoplasmic reticulum fraction isolated from post-germination castor bean endosperm. The reaction requires Mn(2+), has a pH optimum of 8.0, an apparent K(m) for myo-inositol of 26 micromolar, and is stimulated about 15-fold by certain cytidine derivatives. The cytidine derivatives appear to be converted to CMP, which may be the only active stimulator. These optimal exchange reaction conditions, both with and without CMP, differ from those for cytidine-5' -diphosphodiglyceride: myo-inositol transferase (EC 2.7.8), so the exchange does not appear to be a reversal of the transferase. This conclusion is augmented by the low rates of CDP-diglyceride formation from cytidine derivatives when compared to the high rate of myo-inositol incorporation into phosphatidylinositol in the presence of the same cytidine derivatives and identical reaction conditions.

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