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|標題:||Probing structure-function relationships of serine hydrolases and proteases with carbamate and thiocarbamate inhibitors||作者:||Lin, G.
|關鍵字:||structure-function relationship;serine hydrolase;serine protease;enzyme inhibition;carbamate and thiocarbamate;pancreatic cholesterol esterase;structure-reactivity relationships;free-energy relationships;crystal-structure;acetylcholinesterase;butyrylcholinesterase;mechanism;lipase;cholinesterases;recognition||Project:||Protein Journal||期刊/報告no：:||Protein Journal, Volume 25, Issue 1, Page(s) 33-43.||摘要:||
Benzene-1,3-di-N-n-octylcarbamate (1), benzene-1-hydroxyl-3-N-n-octylcarbamate (2), benzene-1,3-di-N-n-ocztylthiocarbamate (3), and benzene-1-hydroxyl-3-N-n-octylthiocarbamate (4) are synthesized from 1,3-benzene-diol and are characterized as the pseudo-substrate inhibitors of acetylcholinesterase, butyrylcholinesterase, cholesterol esterase, lipase, trypsin, and chymotrypsin. For these six enzyme inhibitions by 1-4, the pK(i) values are linearly correlated with their log k(i) values - Bronsted plots. Therefore, 1-4 inhibit these enzymes through a common mechanism. Moreover, both pK(i) and log k(i) values for the inhibitions by 1,3, and 4 are linearly correlated with both pK(i) and log k(i) values for the inhibitions by 2, respectively. Thus, the pK(i) values for the inhibitions by 2 are defined as the nucleophilicity constants of these enzymes (n(enzyme)). The log k(2) values for the inhibitions by 1-4 are also linearly correlated with the n(enzyme) values. Therefore, the nucleophilicity for serine hydrolases and proteases toward 1-4 also applies the Swain-Scott correlations.
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