Marquis J K, Lerrick A J
Biochem Pharmacol. 1982 Apr 1;31(7):1437-40. doi: 10.1016/0006-2952(82)90040-5.
Measurements of altered activity of soluble acetylcholinesterase from E. electricus electric organ by the inorganic cations aluminum, scandium and yttrium demonstrate that these ions are noncompetitive enzyme inhibitors. Al3+ inhibited enzyme activity at all substrate and inhibitor concentrations studied. Inhibition by Al3+ did not appear to be sensitive to the active site-specific, competitive ligand physostigmine or to calcium, a peripheral site-binding activator cation. Inhibition by another peripheral site-binding noncompetitive inhibitor, decamethonium, was not altered by Al3+. Al3+ appears thus to have interacted with a class of peripheral anionic sites on AChE distinct from the beta- or P1 peripheral anionic sites that bind Ca2+ and C-10 and may be a useful probe of a subclass of gamma- or P2-4 peripheral anionic sites. A possible mechanism for Al3+ neurotoxicity, via alterations of the enzymes of cholinergic neurotransmission, is also suggested.
对电鳗（E. electricus）电器官中可溶性乙酰胆碱酯酶活性变化的测量表明，无机阳离子铝、钪和钇是该酶的非竞争性抑制剂。在所有研究的底物和抑制剂浓度下，Al3+ 均抑制酶活性。Al3+ 的抑制作用似乎对活性位点特异性竞争性配体毒扁豆碱或对钙（一种外周位点结合激活阳离子）不敏感。另一种外周位点结合非竞争性抑制剂十烃季铵的抑制作用不受 Al3+ 影响。因此，Al3+ 似乎与乙酰胆碱酯酶上一类不同于结合 Ca2+ 和 C-10 的β或P1外周阴离子位点的外周阴离子位点相互作用，可能是γ或P2-4外周阴离子位点亚类的有用探针。还提出了通过改变胆碱能神经传递酶导致Al3+ 神经毒性的可能机制。
