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標題: Benzene-di-N-substituted carbamates as conformationally constrained substrate analogs of cholesterol esterase
作者: Chiou, S.Y.
Lin, M.C.
Hwang, M.T.
Chang, H.G.
Lin, G.
關鍵字: cholesterol esterase;inhibitor;carbamate;conformation;salt-activated lipase;inhibition;mechanism;acetylcholinesterase;site
Project: Protein Journal
期刊/報告no:: Protein Journal, Volume 27, Issue 5, Page(s) 276-282.
Benzene-1,2-, 1,3-, and 1,4-di-N-substituted carbamates (1-15) are synthesized as the constrained analogs of gauche, eclipsed, and anti conformations, respectively, for the glycerol backbones of triacylglycerol. Carbamates 1-15 are characterized as the pseudo substrate inhibitors of cholesterol esterase. Long chain carbamates are more potent inhibitors than short chain ones. Comparison of different geometries for benzene-di-substituted carbamates, such as benzene-1,2-di-N-octylcarbamate (3) (ortho-3), benzene-1,3-di-N-octylcarbamate (8) (meta-8), and benzene-1,4-di-N-octylcarbamates (13) (para-13), indicates that inhibitory potencies are as followed: meta-8 > para-13 > ortho-3. Therefore, we suggest that the preferable conformation for the C(sn-1)-O/C(sn-2)-O glycerol backbone in the enzyme-triacylgycerol complex is the eclipsed conformation. Meanwhile, kinetic data indicate that among ortho, meta, and para carbamates, meta carbamates most resemble the substrate cholesterol ester.
ISSN: 1572-3887
DOI: 10.1007/s10930-008-9135-2
Appears in Collections:期刊論文

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