請用此 Handle URI 來引用此文件: http://hdl.handle.net/11455/70190
標題: Probing conformations of the glycerol backbones of triacyglycerols in the active site of lipase by 1,2-cyclopentane-carbamates: The meso effect for the enzyme inhibition
作者: Lin, G.
Lai, F.H.
Tsai, B.I.
Hsieh, C.W.
Tsai, H.J.
關鍵字: lipase
enzyme inhibitor
carbamate
cyclopentanediol
conformation
pseudomonas-species lipase
cholesterol esterase
interfacial
activation
binding site
complex
selectivity
mechanism
期刊/報告no:: Journal of Molecular Catalysis B-Enzymatic, Volume 40, Issue 3-4, Page(s) 86-92.
摘要: The aim of this study is to probe the glycerol backbone conformation of the substrate (or inhibitor) in the active site of Pseudomonas species lipase by the 1,2-cyclopentandiol analogues of the ethylene glycerol carbamate inhibitors. Cyclopentane-carbamates, cis-1,2-di-Nn- butylcarbamyl-cyclopentane (1) and trans-1,2-di-N-n-butylcarbamyl-cyclopentane (2), are the conformationally constrained analogues of 1,2-di-N-n-butylcarbamyl ethane (3). All carbamates are synthesized and characterized as the pseudo-substrate inhibitors of the enzyme. Cis-cyclopentane-di-carbamate (1) is a more potent inhibitor than both ethane-di-carbamate (3) and trans-cyclopentane-di-carbamate (2) probably because the glycerol backbone conformations of cis-cyclopentane-di-carbamate (1) are constrained by the cyclopentane ring and cis-cyclopentane-di-cabamate (1) is a meso compound but trans-cyclopentane-di-carbamate (2) is a racemate. (c) 2006 Elsevier B.V. All rights reserved.
URI: http://hdl.handle.net/11455/70190
ISSN: 1381-1177
文章連結: http://dx.doi.org/10.1016/j.molcatb.2006.02.007
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