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木瓜蛋白酶的催化活性对两个酸性基团电离的依赖性。

Dependence of the catalytic activity of papain on the ionization of two acidic groups.

作者信息

Lewis S D, Johnson F A, Ohno A K, Shafer J A

出版信息

J Biol Chem. 1978 Jul 25;253(14):5080-6.

PMID:27512
Abstract

The pH dependence of kcat/Km for the papain-catalyzed hydrolysis of ethyl hippurate, N-alpha-benzoyl-L-citrulline methyl ester, and the p-nitroanilide, amide, and ethyl ester derivatives of N-alpha-benzoyl-L-arginine was determined below pH 6.4. The value of kcat/Km was observed to be modulated by two acid ionizations rather than a single ionization as previously believed. For the five substrates studied, the average pK values for the two ionizations are 3.78 +/- 0.2 and 3.95 +/- 0.1 at T/2 0.3, 25 degrees C. The observation that similar pK values were obtained with different substrates was taken as evidence that the kinetically determined pK values are close in value to true macroscopic ionization constants for ionization of groups on the free enzyme.

摘要

在pH 6.4以下测定了木瓜蛋白酶催化马尿酸乙酯、N-α-苯甲酰-L-瓜氨酸甲酯以及N-α-苯甲酰-L-精氨酸的对硝基苯胺、酰胺和乙酯衍生物水解反应的kcat/Km与pH的关系。结果发现，kcat/Km的值受两个酸电离的调节，而非如之前所认为的受单个电离调节。对于所研究的五种底物，在T/2为0.3、25℃时，这两个电离的平均pK值分别为3.78±0.2和3.95±0.1。不同底物获得相似pK值这一观察结果被视为动力学测定的pK值在数值上接近游离酶上基团电离的真实宏观电离常数的证据。

相似文献

1
Dependence of the catalytic activity of papain on the ionization of two acidic groups.木瓜蛋白酶的催化活性对两个酸性基团电离的依赖性。
J Biol Chem. 1978 Jul 25;253(14):5080-6.
2
Kinetics of the hydrolysis of N-benzoyl-L-serine methyl ester catalysed by bromelain and by papain. Analysis of modifier mechanisms by lattice nomography, computational methods of parameter evaluation for substrate-activated catalyses and consequences of postulated non-productive binding in bromelain- and papain-catalysed hydrolyses.菠萝蛋白酶和木瓜蛋白酶催化N-苯甲酰-L-丝氨酸甲酯水解的动力学。通过晶格列线图分析修饰机制、底物活化催化的参数评估计算方法以及菠萝蛋白酶和木瓜蛋白酶催化水解中假定的非生产性结合的后果。
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The pH dependence of pre-steady-state and steady-state kinetics for the papain-catalyzed hydrolysis of N-alpha-carbobenzoxyglycine p-nitrophenyl ester.木瓜蛋白酶催化N-α-苄氧羰基甘氨酸对硝基苯酯水解的前稳态和稳态动力学的pH依赖性。
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引用本文的文献

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Biochem J. 1993 Feb 15;290 ( Pt 1)(Pt 1):289-96. doi: 10.1042/bj2900289.
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Clarification of the pH-dependent kinetic behaviour of papain by using reactivity probes and analysis of alkylation and catalysed acylation reactions in terms of multihydronic state models: implications for electrostatics calculations and interpretation of the consequences of site-specific mutations such as Asp-158-Asn and Asp-158-Glu.利用反应性探针阐明木瓜蛋白酶的pH依赖性动力学行为，并根据多质子态模型分析烷基化和催化酰化反应：对静电计算以及对位点特异性突变（如Asp-158-Asn和Asp-158-Glu）后果的解释的意义。
Biochem J. 1993 Aug 15;294 ( Pt 1)(Pt 1):201-10. doi: 10.1042/bj2940201.
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Current problems in mechanistic studies of serine and cysteine proteinases.丝氨酸蛋白酶和半胱氨酸蛋白酶机制研究中的当前问题。
Biochem J. 1982 Oct 1;207(1):1-10. doi: 10.1042/bj2070001.
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