作者: Jose R. Tormos , Kenneth L. Wiley , Yi Wang , Didier Fournier , Patrick Masson
DOI: 10.1021/JA104496Q
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摘要: In a previous communication, kinetic β-deuterium secondary isotope effects were reported that support mechanism for substrate-activated turnover of acetylthiocholine by human butyrylcholinesterase (BuChE) wherein the accumulating reactant state is tetrahedral intermediate (Tormos, J. R.; et al. Am. Chem. Soc. 2005, 127, 14538−14539). this contribution additional effect experiments are described with acetyl-labeled acetylthiocholines (CL3COSCH2CH2N+Me3; L = H or D) also accumulation in Drosophila melanogaster acetylcholinesterase (DmAChE) catalysis. contrast to aforementioned BuChE-catalyzed reaction, reaction dependence initial rates on substrate concentration marked pronounced inhibition at high concentrations. Moreover, depended concentration, and gave following: D3kcat/Km 0.95 ± 0.03, D3kcat 1...