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Thiolsubtilisin acts as an acetyltransferase in organic solvents
Author(s) -
Tai Dar-Fu,
Liaw Wen-Chen
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02562-0
Subject(s) - acetyltransferase , histone acetyltransferase , acyltransferases , catalytic triad , chemistry , acetyltransferases , amine gas treating , histone acetyltransferases , enzyme , catalysis , n acetyltransferase , acetylation , biochemistry , amino acid , stereochemistry , transferase , organic chemistry , active site , biosynthesis , gene
The catalytic mechanism of arylamine N ‐acetyltransferase has been proposed to involve Cys‐His‐Asp as its catalytic triad. Thiolsubtilisin, a chemically modified enzyme that has a catalytic triad of Cys‐His‐Asp at the active site, mimics the catalysis of arylamine N ‐acetyltransferase, serotonin N ‐acetyltransferase, histone N ‐acetyltransferase and amino acid N ‐acetyltransferase. Thiolsubtilisin not only can catalyze amino acid transacetylation, but is also able to catalyze amine transacetylation. Ethyl acetate was used as the acylating reagent to form N ‐acetyl amino acids and amines in organic solvents with moderate yield. Hence, these findings broaden our understanding of the structural features required for N ‐acetyltransferases activity as well as provide a structural relationship between cysteine protease and other N ‐acyltransferases.