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首页> 外文期刊>Biochemistry >Kinetics of inactivation of aminoacylase by 2-chloromercuri-4-nitrophenol: a new type of complexing inhibitor.
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Kinetics of inactivation of aminoacylase by 2-chloromercuri-4-nitrophenol: a new type of complexing inhibitor.

机译：2-氯巯基-4-硝基苯酚灭活氨酰酶的动力学：一种新型的络合抑制剂。

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摘要

The kinetic theory of the substrate reaction during modification of enzyme activity previously described [Tsou (1988) Adv. Enzymol. 61, 381-436] has been applied to a study of the inactivation kinetics of aminoacylase by 2-chloromercuri-4-nitrophenol (MNP). The results indicate that the mechanism of reaction between MNP and aminoacylase is a special type of irreversible inhibition. The main features of this type of inhibitor are as follows: (i) the reaction kinetics of inhibitor with enzyme is a single exponential process; (ii) inhibition shows a noncompetitive, complexing behavior; (iii) the first inhibitor-enzyme complex, EI, still has some enzyme activity, and hence the plot of [P]infinity versus the reciprocal of inhibitor concentration gives a straight line with a positive intercept at the ordinate. On the basis of the kinetic equation of substrate reaction in the presence of the inhibitor, a plotting method has been developed for determining the inhibition kinetic constants. As an example, all reaction kinetic constants of aminoacylase with 2-chloromercuri-4-nitrophenol have been determined. The results of the present study suggest that the essential thiol group at the active site of aminoacylase may have a significant effect on the catalytic step but is not involved in substrate binding.
机译：先前描述的酶活性修饰过程中底物反应的动力学理论[Tsou（1988）Adv。酵素61，381-436]已被用于研究2-氯巯基-4-硝基苯酚（MNP）氨酰酶的失活动力学。结果表明，MNP与氨酰酶之间的反应机理是一种不可逆的抑制作用。这种抑制剂的主要特征如下：（i）抑制剂与酶的反应动力学是一个单一的指数过程; （ii）抑制显示出非竞争性的复杂行为; （iii）第一种抑制剂-酶复合物EI仍然具有一定的酶活性，因此[P]无穷大与抑制剂浓度倒数的曲线给出了一条直线，纵坐标为正截距。基于在抑制剂存在下底物反应的动力学方程，开发了一种绘制方法来确定抑制动力学常数。例如，已经确定了氨酰酶与2-氯巯基-4-硝基苯酚的所有反应动力学常数。本研究的结果表明，氨酰酶活性位点上的必需巯基可能对催化步骤有重大影响，但不参与底物结合。

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