Electrostatic effects in the alpha-chymotrypsin-catalyzed acyl transfer. II. Efficiency of nucleophiles bearing charged groups in various locations.
作者信息
Schellenberger V, Jakubke H D, Kasche V
机构信息
Department of Biochemistry, Leipzig University, F.R.G.
出版信息
Biochim Biophys Acta. 1991 May 30;1078(1):8-11. doi: 10.1016/0167-4838(91)90084-d.
PMID:2049385
Abstract
We investigated the alpha-chymotrypsin-catalyzed acyl transfer to a series of glycine oligomers. It could be established that the electrostatic interactions between the carboxylate group of the nucleophiles and the S'-subsites of the enzyme fall off with the length of the nucleophile molecule. Additional negatively charged residues in the nucleophile lead to a considerable reduction of the acyl transfer efficiency. An arginine residue in P'1- or P'3-position, but not in P'2-position, makes favourable interactions with the appropriate S'-subsites of the enzyme.
摘要
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