首页> 外文期刊>Bulletin of Mathematical Biology >KINETIC STUDY OF AN ENZYME-CATALYSED REACTION IN THE PRESENCE OF NOVEL IRREVERSIBLE-TYPE INHIBITORS THAT REACT WITH THE PRODUCT OF ENZYMATIC CATALYSIS
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KINETIC STUDY OF AN ENZYME-CATALYSED REACTION IN THE PRESENCE OF NOVEL IRREVERSIBLE-TYPE INHIBITORS THAT REACT WITH THE PRODUCT OF ENZYMATIC CATALYSIS

机译:存在与酶催化产物发生反应的新型不可逆型抑制剂的酶催化反应动力学研究

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摘要

In the present paper a kinetic study is made of the behaviour of a Michaelis-Menten enzyme-catalysed reaction in the presence of irreversible inhibitors rendered unstable in the medium by their reaction with the product of enzymatic catalysis. A general mechanism involving competitive, non-competitive, uncompetitive and mixed irreversible inhibition with one or two steps has been analysed. The differential equation that describes the kinetics of the reaction is non-linear and computer simulations of its dynamic behaviour are presented. The results obtained show that the systems studied here present kinetic co-operativity for a target enzyme that follows the simple Michaelis-Menten mechanism in its action on the substrate, except in the case of an uncompetitive-type inhibitor.
机译:在本文中,动力学研究了Michaelis-Menten酶催化的反应在不可逆抑制剂存在下的行为,该抑制剂在介质中因与酶催化产物的反应而变得不稳定。已经分析了涉及竞争性,非竞争性,非竞争性和混合不可逆抑制的一个或两个步骤的一般机制。描述反应动力学的微分方程是非线性的,并给出了其动力学行为的计算机模拟。获得的结果表明,本文研究的系统具有针对目标酶的动力学协同作用,该目标酶在作用于底物上遵循简单的Michaelis-Menten机理,除了非竞争性抑制剂外。

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