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猕猴桃蛋白酶的特异性及其与酶结构的关系。

The specificity of actinidin and its relationship to the structure of the enzyme.

作者信息

Baker E N, Boland M J, Calder P C, Hardman M J

出版信息

Biochim Biophys Acta. 1980 Nov 6;616(1):30-4. doi: 10.1016/0005-2744(80)90260-0.

DOI:10.1016/0005-2744(80)90260-0
PMID:7002215
Abstract

The kinetic parameters kcat, Km and kcat/Km, have been determined for the actinidin-catalysed hydrolyses of N-substituted amino acid esters and amides and compared to the corresponding values for papain (EC 3.4.22.2). Substrates with aromatic N-substituents have lower kcat/Km values for actinidin (EC 3.4.22.14); the difference is much smaller for substrates with aliphatic substituents. The lower kcat/Km values for actinidin generally correspond to higher Km values suggesting that the strength of substrate binding differs between the two enzymes. This difference is explained in terms of the differences in the substrate binding sites found in X-ray crystallographic studies.

摘要

已测定了肌动蛋白酶催化的N-取代氨基酸酯和酰胺水解反应的动力学参数kcat、Km和kcat/Km，并与木瓜蛋白酶（EC 3.4.22.2）的相应值进行了比较。对于肌动蛋白酶（EC 3.4.22.14），具有芳香族N-取代基的底物的kcat/Km值较低；对于具有脂肪族取代基的底物，差异要小得多。肌动蛋白酶较低的kcat/Km值通常对应较高的Km值，这表明两种酶之间底物结合强度不同。根据X射线晶体学研究中发现的底物结合位点的差异来解释这种差异。

相似文献

1
The specificity of actinidin and its relationship to the structure of the enzyme.猕猴桃蛋白酶的特异性及其与酶结构的关系。
Biochim Biophys Acta. 1980 Nov 6;616(1):30-4. doi: 10.1016/0005-2744(80)90260-0.
2
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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3
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4
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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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7
Characterization by rapid-kinetic and equilibrium methods of the interaction between N-terminally truncated forms of chicken cystatin and the cysteine proteinases papain and actinidin.通过快速动力学和平衡方法对鸡半胱氨酸蛋白酶抑制剂N端截短形式与半胱氨酸蛋白酶木瓜蛋白酶和猕猴桃蛋白酶之间相互作用的表征。
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8
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J Med Chem. 1984 Nov;27(11):1427-31. doi: 10.1021/jm00377a009.

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