Theoretical studies on the possible reaction pathway for the deacylation of the AChE-catalyzed reaction
文献类型：期刊论文
| 作者 | Wang, QM; Jiang, HL ; Chen, KX; Ji, RY; Ye, YJ
|
| 刊名 | INTERNATIONAL JOURNAL OF QUANTUM CHEMISTRY
 |
| 出版日期 | 1999-08-15 |
| 卷号 | 74期号:3页码:315-325 |
| 关键词 | acetylcholinesterase deacylation process transition state catalytic mechanism stepwise mechanism cooperative mechanism |
| ISSN号 | 0020-7608 |
| DOI | 10.1002/(SICI)1097-461X(1999)74:3<315::AID-QUA4>3.0.CO;2-Y |
| 文献子类 | Article |
| 英文摘要 | Acetylcholinesterase (AChE)-catalyzed hydrolysis of the neurotransmitter, acetylcholine (ACh), occurs via an acylation and deacylation process. The deacylation process was studied theoretically by the semiempirical quantum chemical method AM1 using the model molecules. To investigate the micro features of the deacylation process, two types of possible reaction mechanisms, the stepwise mechanism and the cooperative mechanism, were proposed and studied. All optimized structures of the model molecules for the possible reactants, intermediates, transition states, and products in the reaction pathway of the two possible mechanisms were obtained. Energy profiles and the structural properties of the transition states indicated that the deacylation process proceeds through the cooperative mechanism, that is, the proton transfer from H2O to His440 occurs simultaneously with the nucleophilic attack of the oxygen atom of the H2O to the carbonyl carbon of the acylenzyme. Considering the reaction mechanism of acylation, the first process in AChE-catalyzed hydrolysis of ACh, studied in our previous article, we can conclude that both the acylation and deacylation process limit the rate of the entire AChE-catalyzed reaction. Four transition states exist in the whole pathway of the AChE-catalyzed reaction. The rehybridization of the transition state was found. These results are in agreement with the kinetics data and the secondary isotope effects of AChE-catalyzed reactions. (C) 1999 John Wiley & Sons, Inc. |
| WOS关键词 | TRANSITION-STATE STRUCTURE ; ACETYLCHOLINESTERASE ; HYDROLYSIS ; SIMULATION ; ACYLATION ; DYNAMICS |
| WOS研究方向 | Chemistry ; Mathematics ; Physics |
| 语种 | 英语 |
| WOS记录号 | WOS:000081626900004 |
| 出版者 | JOHN WILEY & SONS INC |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/274708]  |
| 专题 | 中国科学院上海药物研究所 |
| 通讯作者 | Jiang, HL |
| 作者单位 | 1.Chinese Acad Sci, Shanghai Inst Mat Med, State Key Lab New Drug Res, Shanghai 200031, Peoples R China 2.Chinese Acad Sci, Inst Biophys, Dept Prot Engn, Beijing 100101, Peoples R China |
| 推荐引用方式 GB/T 7714 | Wang, QM,Jiang, HL,Chen, KX,et al. Theoretical studies on the possible reaction pathway for the deacylation of the AChE-catalyzed reaction[J]. INTERNATIONAL JOURNAL OF QUANTUM CHEMISTRY,1999,74(3):315-325. |
| APA | Wang, QM,Jiang, HL,Chen, KX,Ji, RY,&Ye, YJ.(1999).Theoretical studies on the possible reaction pathway for the deacylation of the AChE-catalyzed reaction.INTERNATIONAL JOURNAL OF QUANTUM CHEMISTRY,74(3),315-325. |
| MLA | Wang, QM,et al."Theoretical studies on the possible reaction pathway for the deacylation of the AChE-catalyzed reaction".INTERNATIONAL JOURNAL OF QUANTUM CHEMISTRY 74.3(1999):315-325. |
入库方式： OAI收割
来源：上海药物研究所
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