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KMID : 0614019990150010251
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Journal of Pharmaceutical Sciences (C.N.U.)
1999 Volume.15 No. 1 p.251 ~ p.258
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A structural Feature of the Active Site of Acetylcholinesterase using Thiocholine ester Substrates
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Lee Chun-Bae
Chu Eun-Hui
Choi Su-La
Sok Dai-Eun
Myung Pyung-Keun
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Abstract
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The inhibition pattern of three inhibitors(tacrine, decamethonium and propidium) on the hydrolysis of various thiocholine ester substrates by eel acetylcholinesterase was comparatively examined. When the substrate was acetylthiocholine, it showed a similar competitive inhibition by tacrine inhibitor, and a mixed type inhibition by decamethonium and propidium inhibitors. When the substrate was pentanoylthiocholine, it showed an uncompetitive inhibition by tacrine, and a noncompetitive inhibition by decamethonium. When the substrate was laurylthiocholine, it showed mixed type and uncompetitive inhibition by tacrine, and a competitive inhibition by decamethonium and propidium. Those results suggest that the active of acetylcholinesterase has the existence of hydorphobic site besides the anionic and esteratic site.
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