請用此 Handle URI 來引用此文件: http://hdl.handle.net/11455/34397
標題: Inhibition or activation of Pseudomonas species lipase by 1,2-ethylene-di-N-alkylcarbamates in detergents
作者: Lin, M.C.
林彥甫
Lu, C.P.
Cheng, Y.R.
Lin, Y.F.
Lin, C.S.
Lin, G.
關鍵字: lipase
inhibitor
activator
carbamate
detergent
cholesterol esterase
triacylglycerol lipase
lipolytic enzymes
open
conformation
cepacia lipase
binding site
complex
state
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.
URI: http://hdl.handle.net/11455/34397
ISSN: 0009-3084
文章連結: http://dx.doi.org/10.1016/j.chemphyslip.2006.12.005
顯示於類別:化學系所

文件中的檔案:
沒有與此文件相關的檔案。


在 DSpace 系統中的文件,除了特別指名其著作權條款之外,均受到著作權保護,並且保留所有的權利。