The interplay of electrostatic and binding interactions determining active centre chemistry and catalytic activity in actinidin and papain.
作者信息
Brocklehurst K, O'Driscoll M, Kowlessur D, Phillips I R, Templeton W, Thomas E W, Topham C M, Wharton C W
出版信息
Biochem J. 1989 Jan 1;257(1):309-10. doi: 10.1042/bj2570309.
Abstract
摘要
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1
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.
2
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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3
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。
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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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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 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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Sensitivities of transition state geometries to P1-P2 binding in reactions of papain and actinidin.
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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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Effects of the quality of the P2-S2 hydrophobic contacts on the catalytic activities of papain, caricain and ficin and their generation by electrostatic switches.P2-S2疏水接触的质量对木瓜蛋白酶、木菠萝蛋白酶和无花果蛋白酶催化活性及其通过静电开关产生的影响。
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Actinidin and chymopapain B provide variation in the common electrostatic environment of Glu50 in papain and caricain.
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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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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.
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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.
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.
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
Effects of conformational selectivity and of overlapping kinetically influential ionizations on the characteristics of pH-dependent enzyme kinetics. Implications of free-enzyme pKa variability in reactions of papain for its catalytic mechanism.构象选择性和重叠动力学影响电离对pH依赖性酶动力学特征的影响。木瓜蛋白酶反应中游离酶pKa变异性对其催化机制的影响。
Biochem J. 1983 Jun 1;211(3):701-8. doi: 10.1042/bj2110701.
3
Calculation of the electric potential in the active site cleft due to alpha-helix dipoles.由于α-螺旋偶极子导致的活性位点裂隙中电势的计算。
J Mol Biol. 1982 Jun 5;157(4):671-9. doi: 10.1016/0022-2836(82)90505-8.
4
Ionization behavior of the catalytic carboxyls of lysozyme.
Biochem Biophys Res Commun. 1970 Oct 9;41(1):45-9. doi: 10.1016/0006-291x(70)90466-3.
5
pH-dependence and structure-activity relationships in the papain-catalysed hydrolysis of anilides.木瓜蛋白酶催化酰苯胺水解反应中的pH依赖性及构效关系
Biochem J. 1971 Aug;124(1):117-22. doi: 10.1042/bj1240117.
6
Kinetics of papain-catalyzed hydrolysis of -N-benzoyl-L-arginine-p-nitroanilide.木瓜蛋白酶催化水解-N-苯甲酰-L-精氨酸对硝基苯胺的动力学
Biochemistry. 1973 Feb 27;12(5):816-22. doi: 10.1021/bi00729a005.
7
Thiol proteases. Comparative studies based on the high-resolution structures of papain and actinidin, and on amino acid sequence information for cathepsins B and H, and stem bromelain.硫醇蛋白酶。基于木瓜蛋白酶和猕猴桃蛋白酶的高分辨率结构，以及组织蛋白酶B和H及菠萝蛋白酶的氨基酸序列信息进行的比较研究。
J Mol Biol. 1985 Mar 20;182(2):317-29. doi: 10.1016/0022-2836(85)90348-1.
8
Chemical evidence for the pH-dependent control of ion-pair geometry in cathepsin B. Benzofuroxan as a reactivity probe sensitive to differences in the mutual disposition of the thiolate and imidazolium components of cysteine proteinase catalytic sites.组织蛋白酶B中离子对几何结构pH依赖性控制的化学证据。苯并呋咱作为一种对半胱氨酸蛋白酶催化位点硫醇盐和咪唑𬭩组分相互位置差异敏感的反应性探针。
Biochem J. 1986 Aug 15;238(1):103-7. doi: 10.1042/bj2380103.
9
Substrate-derived two-protonic-state electrophiles as sensitive kinetic specificity probes for cysteine proteinases. Activation of 2-pyridyl disulphides by hydrogen-bonding.作为半胱氨酸蛋白酶敏感动力学特异性探针的底物衍生双质子态亲电试剂。通过氢键作用激活2-吡啶基二硫化物。
Biochem J. 1987 May 15;244(1):173-81. doi: 10.1042/bj2440173.
10
Chromophoric and fluorophoric peptide substrates cleaved through the dipeptidyl carboxypeptidase activity of cathepsin B.
Anal Biochem. 1987 Aug 15;165(1):96-101. doi: 10.1016/0003-2697(87)90205-3.
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