Lin G, Chen G H, Ho H C
Department of Chemistry, National Chung-Hsing University, Taichung, Taiwan.
Bioorg Med Chem Lett. 1998 Oct 6;8(19):2747-50. doi: 10.1016/s0960-894x(98)00484-3.
Conformationally restricted carbamate inhibitors, exo-2-norbornyl-N-butylcarbamate (1), endo-2-norbornyl-N-butylcarbamate (2), l-adamantyl-N-butylcarbamate (3), and 2-adamantyl-N-butylcarbamate (4) as active site-directed irreversible inhibitors of horse serum butyrylcholinesterase are investigated for values of the dissociation constant (KI), the carbamylation constant (k2), and the bimolecular rate constant (ki). Compound 1 is the most potent inhibitor of the enzyme and the values of KI and ki are 20 nM and 1.1 x 10(5) M-1sec-1, respectively.
构象受限的氨基甲酸酯抑制剂，外型-2-降冰片基-N-丁基氨基甲酸酯（1）、内型-2-降冰片基-N-丁基氨基甲酸酯（2）、1-金刚烷基-N-丁基氨基甲酸酯（3）和2-金刚烷基-N-丁基氨基甲酸酯（4）作为马血清丁酰胆碱酯酶活性位点导向的不可逆抑制剂，对其解离常数（KI）、氨甲酰化常数（k2）和双分子速率常数（ki）进行了研究。化合物1是该酶最有效的抑制剂，KI和ki值分别为20 nM和1.1×10⁵ M⁻¹秒⁻¹。
