Plantavid M, Maget-Dana R, Douste-Blazy L
Biochimie. 1975;57(8):951-7. doi: 10.1016/s0300-9084(75)80217-3.
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++.
对大鼠肝脏中的乙醇胺磷酸胞苷酰转移酶（E.C. 2.7.7.14）进行了动力学研究，研究是在磷酸乙醇胺的结构类似物存在的情况下进行的：这些化合物作为该酶的抑制剂：- 2-氨基乙基膦酸酯表现为底物和磷酸乙醇胺的竞争性抑制剂：在pH = 5.5时，2-氨基乙基膦酸酯的Km值与其Ki值几乎相同（分别为30×10⁻³ M和24×10⁻³ M）。- 3-氨基丙基膦酸酯也是竞争性抑制剂。在最适pH（pH = 7.7）时，它似乎是最佳抑制剂。- 1-氨基乙基膦酸酯表现为非竞争性抑制剂。然而，胞苷酰转移酶具有相对特异性，抑制作用总是较弱。Mg²⁺增强了膦酸酯的抑制能力。
