Jan 1, 1975

Interactions of phosphorylethanolamine analogs with phosphorylethanolamine-citidylyltransferase

M PlantavidL Douste-Blazy


Kinetic studies of ethanolaminephosphate-cytidylyltransferase (E.C. from rat liver have been carried out in presence of structural analogues of ethanolaminephosphate : these compounds acted as inhibitors of the enzyme: - 2-aminoethylphosphonate behaved as a substrate and a competitive inhibitor to phosphorylethanolamine: the Km value of 2-aminoethylphosphonate was nearly the same as its Ki value, at pH = 5,5 (30 X 10(-3) M and 24 x 10(-3) M, respectively). - 3-aminopropylphosphonate was also a competitive inhibitor. It appeared to be the best inhibitor at pH optimum (pH = 7,7). - 1-aminoethylphosphonate behaved as a noncompetitive inhibitor. However, cytidylyltransferase was relatively specific, inhibitions being always weak. Inhibitory power of phosphonates was stimulated by Mg++.

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Mentioned in this Paper

Aminoethylphosphonic Acid
Analogs & derivatives
Organopyrophosphorus Compounds

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