Lanks K W, Lieske C N, Papirmeister B
Biochim Biophys Acta. 1977 Aug 11;483(2):320-30. doi: 10.1016/0005-2744(77)90060-2.
Repeated cycles of inhibition by a variety of organophosphates followed by spontaneous reactivation reveal a component of electric eel acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7) which preferentially reactivates. That the observed enzymatic activity truly resides in acetylcholinesterase is indicated by its sensitivity to a specific inhibitor and by molecular weights for subunits and native enzyme which are approximately the same as those for the major fraction of enzymatic activity which behaves in the classical manner. The Km values for phenyl acetate of the two components are similar but the rate constant for covalent bond formation, k2, with isopropyl m-nitrophenyl methylphosphonate is greatly reduced in the spontaneously reactivating species. The molecular basis for these observations is discussed.
多种有机磷酸酯反复抑制电鳗乙酰胆碱酯酶（乙酰胆碱水解酶，EC 3.1.1.7），随后自发重新激活，这揭示了电鳗乙酰胆碱酯酶中一种优先重新激活的成分。观察到的酶活性真正存在于乙酰胆碱酯酶中，这一点可通过其对特定抑制剂的敏感性以及亚基和天然酶的分子量来表明，这些分子量与以经典方式表现的主要酶活性部分的分子量大致相同。两种成分的乙酸苯酯的Km值相似，但与间硝基苯基甲基膦酸异丙酯形成共价键的速率常数k2在自发重新激活的物种中大大降低。讨论了这些观察结果的分子基础。
