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|標題:||Inhibition or activation of Pseudomonas species lipase by 1,2-ethylene-di-N-alkylcarbamates in detergents||作者:||Lin, M.C.
|關鍵字:||lipase;inhibitor;activator;carbamate;detergent;cholesterol esterase;triacylglycerol lipase;lipolytic enzymes;open;conformation;cepacia lipase;binding site;complex;state||Project:||Chemistry and Physics of Lipids||期刊/報告no：:||Chemistry and Physics of Lipids, Volume 146, Issue 2, Page(s) 85-93.||摘要:||
1,2-Ethylene-di-N-n-propyicarbamate (1) is characterized as an essential activator of Pseudomonas species lipase while 1,2ethylene-di-N-n-butyl-, t-butyl-, n-heptyl-, and n-octyl-carbamates (2-5) are characterized as the pseudo substrate inhibitors of the enzyme in the presence of the detergent taurocholate or triton X-100. The inhibition and activation reactions are more sensitive in taurocholate than in triton X-100. From CD studies, the enzyme changes conformations in the presence of the detergent and further alters conformations by addition of the carbamate activator or inhibitor into the enzyme-detergent adduct. Therefore, this study suggests that the conformational change of lipase during interfacial activation is a continuous process to expose the active site of the enzyme to substrate. From 600 MHz H-1 NMR studies, the conformations of the alpha- and beta-methylene moieties of the activator 1,2-ethylene-di-N-n-propylcarbamate in the presence of substrate change after adding taurocholate into the mixture, and the conformations of the beta-methylene moieties of the inhibitor 1,2-ethylene-di-N-n-butylcarbamate in the presence of substrate alter after adding taurocholate into the mixture. (c) 2007 Elsevier Ireland Ltd. All rights reserved.
|Appears in Collections:||化學系所|
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