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alpha-Chymotrypsin deacylation: temperature dependence of hydrolysis and transesterification reactions.

作者信息

Wang C L, Calvo K C, Klapper M H

出版信息

Biochemistry. 1981 Mar 3;20(5):1401-8. doi: 10.1021/bi00508a057.

DOI:10.1021/bi00508a057
PMID:7225338
Abstract

The hydrolysis and transesterification reactions of furoyl-chymotrypsins display nonlinear Arrhenius plots with no apparent discontinuities. Of a number of models considered, the best explanation assumes a temperature-dependent rapid equilibrium between two forms of acyl-enzyme with differing reactivities. Rate constants for the transesterification of alpha-chymotrypsinyl 2-(5-n-propyl)furoate, after normalization for this equilibrium, display a linear free energy correlation with the Taft polarity constants sigma* and volumes of the attacking alcohols.

摘要

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引用本文的文献

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The kinetics of acylation and deacylation of penicillin acylase from Escherichia coli ATCC 11105: evidence for lowered pKa values of groups near the catalytic centre.来自大肠杆菌ATCC 11105的青霉素酰化酶的酰化和去酰化动力学:催化中心附近基团pKa值降低的证据。
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Interpretation of thermodynamic compensation plots for acyl alpha-chymotrypsin systems.酰基α-胰凝乳蛋白酶系统热力学补偿图的解读。
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3
Chymotrypsin compensation plots: a cautionary note.
胰凝乳蛋白酶补偿图:一则警示
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