对一种酶不稳定的米氏（Michaelis-Menten）机制的动力学分析。
Kinetic analysis of a Michaelis-Menten mechanism in which the enzyme is unstable.
作者信息
Garrido-del Solo C, García-Cánovas F, Havsteen B H, Varón-Castellanos R
机构信息
Departamento de Química-Física, Escuela Universitaria Politécnica, Universidad de Castilla-La Mancha, Albacete, Spain.
出版信息
Biochem J. 1993 Sep 1;294 ( Pt 2)(Pt 2):459-64. doi: 10.1042/bj2940459.
Abstract
A kinetic analysis of the Michaelis-Menten mechanism is made for the cases in which the free enzyme, or the enzyme-substrate complex, or both, are unstable, either spontaneously or as a result of the addition of a reagent. The explicit time-course equations of all of the species involved has been derived under conditions of limiting enzyme concentration. The validity of these equations has been checked by using numerical simulations. An experimental design and a kinetic data analysis allowing the evaluation of the parameters and kinetic constants are recommended.
摘要
针对游离酶、酶-底物复合物或两者自发地或因添加试剂而不稳定的情况，对米氏机制进行了动力学分析。在酶浓度受限的条件下，推导了所有相关物种的明确时间进程方程。通过数值模拟检验了这些方程的有效性。推荐了一种允许评估参数和动力学常数的实验设计和动力学数据分析方法。
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本文引用的文献
1
Kinetics of suicide substrates.自杀底物的动力学
Biochem J. 1980 Mar 1;185(3):771-3. doi: 10.1042/bj1850771.
2
An easy method for the determination of initial rates.一种测定初始速率的简便方法。
Biochem J. 1981 Mar 1;193(3):1009-12. doi: 10.1042/bj1931009.
3
Determination of the rate constant of enzyme modification by measuring the substrate reaction in the presence of the modifier.通过在修饰剂存在的情况下测量底物反应来测定酶修饰的速率常数。
Biochemistry. 1982 Mar 2;21(5):1028-32. doi: 10.1021/bi00534a031.
4
Kinetics of suicide substrates. Practical procedures for determining parameters.自杀底物的动力学。确定参数的实用程序。
Biochem J. 1985 May 1;227(3):843-9. doi: 10.1042/bj2270843.
5
Progress curves of reactions catalyzed by unstable enzymes. A theoretical approach.不稳定酶催化反应的进程曲线。一种理论方法。
J Theor Biol. 1986 Nov 7;123(1):67-80. doi: 10.1016/s0022-5193(86)80236-3.
6
Transient-phase kinetics of enzyme inactivation induced by suicide substrates.自杀底物诱导的酶失活的瞬态动力学
Biochim Biophys Acta. 1987 Apr 30;912(3):408-16. doi: 10.1016/0167-4838(87)90046-x.
7
Kinetics of substrate reaction during irreversible modification of enzyme activity.酶活性不可逆修饰过程中底物反应的动力学
Adv Enzymol Relat Areas Mol Biol. 1988;61:381-436. doi: 10.1002/9780470123072.ch7.
8
Resistance to inactivation by EGTA of the enzyme-substrate and enzyme-phosphate complexes of alkaline phosphatase.碱性磷酸酶的酶 - 底物复合物和酶 - 磷酸复合物对乙二醇双（2-氨基乙基醚）四乙酸（EGTA）失活作用的抗性。
Biochem J. 1987 Jun 15;244(3):781-5. doi: 10.1042/bj2440781.
9
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Biochem J. 1989 Jan 15;257(2):419-24. doi: 10.1042/bj2570419.
10
Analysis of residuals: criteria for determining goodness-of-fit.残差分析：确定拟合优度的标准。
Methods Enzymol. 1992;210:87-105. doi: 10.1016/0076-6879(92)10007-z.
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