Structural and electrostatic differences between actinidin and papain account for differences in activity.
作者信息
Pickersgill R W, Sumner I G, Collins M E, Goodenough P W
出版信息
Biochem J. 1989 Jan 1;257(1):310-2. doi: 10.1042/bj2570310.
Abstract
摘要
相似文献
1
Structural and electrostatic differences between actinidin and papain account for differences in activity.猕猴桃蛋白酶和木瓜蛋白酶之间的结构和静电差异导致了活性差异。
Biochem J. 1989 Jan 1;257(1):310-2. doi: 10.1042/bj2570310.
2
The interplay of electrostatic and binding interactions determining active centre chemistry and catalytic activity in actinidin and papain.静电相互作用与结合相互作用之间的相互影响决定了猕猴桃蛋白酶和木瓜蛋白酶的活性中心化学性质及催化活性。
Biochem J. 1989 Jan 1;257(1):309-10. doi: 10.1042/bj2570309.
3
The interplay of electrostatic fields and binding interactions determining catalytic-site reactivity in actinidin. A possible origin of differences in the behaviour of actinidin and papain.静电场与结合相互作用的相互影响决定了猕猴桃蛋白酶催化位点的反应活性。猕猴桃蛋白酶和木瓜蛋白酶行为差异的一个可能来源。
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4
Actinidin and chymopapain B provide variation in the common electrostatic environment of Glu50 in papain and caricain.
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Variation in the P2-S2 stereochemical selectivity towards the enantiomeric N-acetylphenylalanylglycine 4-nitroanilides among the cysteine proteinases papain, ficin and actinidin.半胱氨酸蛋白酶木瓜蛋白酶、无花果蛋白酶和猕猴桃蛋白酶对映体N-乙酰苯丙氨酰甘氨酸4-硝基苯胺的P2-S2立体化学选择性差异。
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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。
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Sensitivities of transition state geometries to P1-P2 binding in reactions of papain and actinidin.
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Variation in aspects of cysteine proteinase catalytic mechanism deduced by spectroscopic observation of dithioester intermediates, kinetic analysis and molecular dynamics simulations.通过二硫酯中间体的光谱观察、动力学分析和分子动力学模拟推导的半胱氨酸蛋白酶催化机制各方面的变化。
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Variation in the pH-dependent pre-steady-state and steady-state kinetic characteristics of cysteine-proteinase mechanism: evidence for electrostatic modulation of catalytic-site function by the neighbouring carboxylate anion.半胱氨酸蛋白酶机制中pH依赖性预稳态和稳态动力学特征的变化：相邻羧酸根阴离子对催化位点功能进行静电调节的证据
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Milk Protein Hydrolysis by Actinidin-Kinetic and Thermodynamic Characterisation and Comparison to Bromelain and Papain.奇异果蛋白酶对乳蛋白的水解作用——动力学和热力学表征以及与菠萝蛋白酶和木瓜蛋白酶的比较
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Ionization characteristics and chemical influences of aspartic acid residue 158 of papain and caricain determined by structure-related kinetic and computational techniques: multiple electrostatic modulators of active-centre chemistry.通过与结构相关的动力学和计算技术确定木瓜蛋白酶和木瓜凝乳蛋白酶中天冬氨酸残基158的电离特性和化学影响：活性中心化学的多种静电调节剂
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Catalytic-site characteristics of the porcine calpain II 80 kDa/18 kDa heterodimer revealed by selective reaction of its essential thiol group with two-hydronic-state time-dependent inhibitors: evidence for a catalytic site Cys/His interactive system and an ionizing modulatory group.通过猪钙蛋白酶II 80 kDa/18 kDa异二聚体的必需巯基与双水合态时间依赖性抑制剂的选择性反应揭示的催化位点特征：催化位点半胱氨酸/组氨酸相互作用系统和电离调节基团的证据。
Biochem J. 1993 Feb 15;290 ( Pt 1)(Pt 1):75-83. doi: 10.1042/bj2900075.
4
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.
5
The interplay of electrostatic fields and binding interactions determining catalytic-site reactivity in actinidin. A possible origin of differences in the behaviour of actinidin and papain.静电场与结合相互作用的相互影响决定了猕猴桃蛋白酶催化位点的反应活性。猕猴桃蛋白酶和木瓜蛋白酶行为差异的一个可能来源。
Biochem J. 1989 Apr 15;259(2):443-52. doi: 10.1042/bj2590443.
6
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.
本文引用的文献
1
Structure of actinidin, after refinement at 1.7 A resolution.经1.7埃分辨率精修后的猕猴桃蛋白酶结构。
J Mol Biol. 1980 Aug 25;141(4):441-84. doi: 10.1016/0022-2836(80)90255-7.
2
Structure of papain refined at 1.65 A resolution.木瓜蛋白酶结构在1.65埃分辨率下的精修。
J Mol Biol. 1984 Oct 25;179(2):233-56. doi: 10.1016/0022-2836(84)90467-4.
3
A rapid method of calculating charge-charge interaction energies in proteins.
Protein Eng. 1988 Sep;2(3):247-8. doi: 10.1093/protein/2.3.247.
4
The electrostatic fields in the active-site clefts of actinidin and papain.猕猴桃蛋白酶和木瓜蛋白酶活性位点裂隙中的静电场。
Biochem J. 1988 Aug 15;254(1):235-8. doi: 10.1042/bj2540235.
5
The interplay of electrostatic and binding interactions determining active centre chemistry and catalytic activity in actinidin and papain.静电相互作用与结合相互作用之间的相互影响决定了猕猴桃蛋白酶和木瓜蛋白酶的活性中心化学性质及催化活性。
Biochem J. 1989 Jan 1;257(1):309-10. doi: 10.1042/bj2570309.
6
Cloning and sequencing of papain-encoding cDNA.木瓜蛋白酶编码cDNA的克隆与测序
Gene. 1986;48(2-3):219-27. doi: 10.1016/0378-1119(86)90080-6.
7
Differences in the chemical and catalytic characteristics of two crystallographically 'identical' enzyme catalytic sites. Characterization of actinidin and papain by a combination of pH-dependent substrate catalysis kinetics and reactivity probe studies targeted on the catalytic-site thiol group and its immediate microenvironment.两个晶体学上“相同”的酶催化位点在化学和催化特性上的差异。通过结合pH依赖性底物催化动力学以及针对催化位点硫醇基团及其紧邻微环境的反应性探针研究，对猕猴桃蛋白酶和木瓜蛋白酶进行表征。
Biochem J. 1987 Oct 1;247(1):181-93. doi: 10.1042/bj2470181.
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