[Interactions of phosphorylethanolamine analogs with phosphorylethanolamine-citidylyltransferase].
Kinetic studies of ethanolaminephosphate-cytidylyltransferase (E.C. 2.7.7.14) 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++.
D000615:Aminoethylphosphonic Acid / Q000378:metabolism / Q000494:pharmacology; D000818:Animals; D003568:Cytidine Monophosphate / Q000378:metabolism; D004983:Ethanolamines / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008274:Magnesium / Q000494:pharmacology; D009713:Nucleotidyltransferases / Q000037:antagonists & inhibitors*; D063065:Organophosphonates / Q000494:pharmacology*; D009943:Organophosphorus Compounds / Q000494:pharmacology; D011437:Propylamines / Q000494:pharmacology; D051381:Rats
D004983:Ethanolamines; D063065:Organophosphonates; D009943:Organophosphorus Compounds; D011437:Propylamines; D000615:Aminoethylphosphonic Acid; D009713:Nucleotidyltransferases; D003568:Cytidine Monophosphate; D008274:Magnesium
Interactions d'analogues de la phosphoryléthanolamine avec la phosphoryléthanolamine-cytidylyltransférase