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Studies on the enhancement of the reactivity of the (Cys-25)-S-/(His159)-Im+H ion-pair of papain by deprotonation across pKa 4.

作者信息

Pinitglang S, Noble M, Verma C, Thomas E W, Brocklehurst K

机构信息

Department of Biochemistry, Queen Mary & Westwield College, University of London, U.K.

出版信息

Biochem Soc Trans. 1996 Aug;24(3):468S. doi: 10.1042/bst024468s.

DOI:10.1042/bst024468s
PMID:8879012
Abstract
摘要

相似文献

1
Studies on the enhancement of the reactivity of the (Cys-25)-S-/(His159)-Im+H ion-pair of papain by deprotonation across pKa 4.
Biochem Soc Trans. 1996 Aug;24(3):468S. doi: 10.1042/bst024468s.
2
Ionization characteristics of the Cys-25/His-159 interactive system and of the modulatory group of papain: resolution of ambiguity by electronic perturbation of the quasi-2-mercaptopyridine leaving group in a new pyrimidyl disulphide reactivity probe.半胱氨酸-25/组氨酸-159相互作用系统及木瓜蛋白酶调节基团的电离特性：通过新型嘧啶基二硫化物反应性探针中准2-巯基吡啶离去基团的电子扰动解决歧义问题。
Biochem J. 1993 Feb 15;290 ( Pt 1)(Pt 1):289-96. doi: 10.1042/bj2900289.
3
Structure of chymopapain M the late-eluted chymopapain deduced by comparative modelling techniques and active-centre characteristics determined by pH-dependent kinetics of catalysis and reactions with time-dependent inhibitors: the Cys-25/His-159 ion-pair is insufficient for catalytic competence in both chymopapain M and papain.糜蛋白酶M的结构：通过比较建模技术推导得出的晚期洗脱糜蛋白酶，以及通过pH依赖性催化动力学和与时间依赖性抑制剂反应确定的活性中心特征：半胱氨酸-25/组氨酸-159离子对对于糜蛋白酶M和木瓜蛋白酶的催化活性而言均不充分。
Biochem J. 1994 Jun 15;300 ( Pt 3)(Pt 3):805-20. doi: 10.1042/bj3000805.
4
Identification of interactions involved in the generation of nucleophilic reactivity and of catalytic competence in the catalytic site Cys/His ion pair of papain.鉴定木瓜蛋白酶催化位点半胱氨酸/组氨酸离子对中亲核反应性和催化能力产生所涉及的相互作用。
Biochemistry. 2011 Dec 13;50(49):10732-42. doi: 10.1021/bi201207z. Epub 2011 Nov 17.
5
Challenging a paradigm: theoretical calculations of the protonation state of the Cys25-His159 catalytic diad in free papain.挑战传统观念：游离木瓜蛋白酶中 Cys25-His159 催化二联体质子化状态的理论计算。
Proteins. 2009 Dec;77(4):916-26. doi: 10.1002/prot.22516.
6
Generation of nucleophilic character in the Cys25/His159 ion pair of papain involves Trp177 but not Asp158.木瓜蛋白酶的半胱氨酸25/组氨酸159离子对中亲核特性的产生涉及色氨酸177，而非天冬氨酸158。
Biochemistry. 2008 Feb 19;47(7):2025-35. doi: 10.1021/bi702126p. Epub 2008 Jan 29.
7
Electrostatic properties in the catalytic site of papain: A possible regulatory mechanism for the reactivity of the ion pair.木瓜蛋白酶催化位点的静电性质：离子对反应性的一种可能调控机制。
Proteins. 2003 Aug 1;52(2):236-53. doi: 10.1002/prot.10368.
8
Structure-function relationships in the cysteine proteinases actinidin, papain and papaya proteinase omega. Three-dimensional structure of papaya proteinase omega deduced by knowledge-based modelling and active-centre characteristics determined by two-hydronic-state reactivity probe kinetics and kinetics of catalysis.半胱氨酸蛋白酶肌动蛋白水解酶、木瓜蛋白酶和木瓜蛋白酶ω的结构-功能关系。通过基于知识的建模推导木瓜蛋白酶ω的三维结构，以及通过双水合态反应探针动力学和催化动力学确定其活性中心特征。
Biochem J. 1991 Nov 15;280 ( Pt 1)(Pt 1):79-92. doi: 10.1042/bj2800079.
9
The double catalytic triad, Cys25-His159-Asp158 and Cys25-His159-Asn175, in papain catalysis: role of Asp158 and Asn175.木瓜蛋白酶催化作用中的双催化三联体Cys25-His159-Asp158和Cys25-His159-Asn175：Asp158和Asn175的作用
Protein Eng. 1994 Jan;7(1):75-82. doi: 10.1093/protein/7.1.75.
10
Modulation of the enzymatic activity of papain by interdomain residues remote from the active site.
Protein Eng. 1994 Jun;7(6):769-75. doi: 10.1093/protein/7.6.769.

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