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反应基团并列时的灵活性以及酶反应的上限。

The flexibility during the juxtaposition of reacting groups and the upper limits of enzyme reactions.

作者信息

Zhou G P, Li T T, Chou K C

出版信息

Biophys Chem. 1981 Nov;14(3):277-81. doi: 10.1016/0301-4622(81)85028-4.

DOI:10.1016/0301-4622(81)85028-4
PMID:7326350
Abstract

The combination between enzymes and substrates occur only after their reacting groups are in juxtaposition with each other. This will greatly reduce the probability of their effective encounters. However, the results calculated with the finite elements method show that the reaction limits will not decrease substantially if van der Waal's forces and a reasonable flexibility during such a juxtaposition are taken into account.

摘要

酶与底物只有在它们的反应基团相互并列后才会发生结合。这将大大降低它们有效相遇的概率。然而,用有限元方法计算的结果表明,如果考虑范德华力以及在这种并列过程中的合理柔韧性,反应限度不会大幅降低。

相似文献

1
The flexibility during the juxtaposition of reacting groups and the upper limits of enzyme reactions.反应基团并列时的灵活性以及酶反应的上限。
Biophys Chem. 1981 Nov;14(3):277-81. doi: 10.1016/0301-4622(81)85028-4.
2
A theoretical model for calculation of the rate constant of enzyme-substrate complex formation. 3. Effect of intermolecular forces and diffusion motion of the enzyme molecule on the rate constant.酶-底物复合物形成速率常数计算的理论模型。3. 分子间作用力和酶分子扩散运动对速率常数的影响。
Acta Biochim Biophys Acad Sci Hung. 1974;9(3):185-96.
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Diffusion-controlled reactions of enzymes. A comparison between Chou's model and Alberty-Hammes-Eigen's model.酶的扩散控制反应。周氏模型与阿尔伯蒂-哈姆斯-艾根模型的比较。
Eur J Biochem. 1982 Nov 15;128(2-3):383-7.
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Subunit interactions in enzyme catalysis. Kinetic models for one-substrate polymeric enzymes.酶催化中的亚基相互作用。单底物聚合酶的动力学模型。
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Finite fluctuations and multiple steady states far from equilibrium.远离平衡态的有限涨落和多重稳态。
Bull Math Biol. 1974 Apr;36(2):205-13. doi: 10.1007/BF02458604.
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Diffusion-controlled reactions of enzymes. An approximate analytic solution of Chou's model.
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A theoretical model for calculation of the rate constant of enzyme-substrate complex formation. I. Calculation of rate constant in the case of motionless enzyme molecule without nonspecific intermolecular forces.一种用于计算酶 - 底物复合物形成速率常数的理论模型。I. 无非特异性分子间力的静止酶分子情况下速率常数的计算。
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A theoretical model for calculation of the rate constant of enzyme-substrate complex formation. II. Effect of intermolecular forces on the parameters describing the translational diffusion motion of a particle.酶 - 底物复合物形成速率常数计算的理论模型。II. 分子间力对描述粒子平动扩散运动参数的影响。
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Biophys Chem. 1975 Apr;3(2):153-60. doi: 10.1016/0301-4622(75)80005-6.

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