通过使用布里格斯 - 霍尔丹两步不可逆动力学模型所描绘的，k(cat)在最佳酶活性表现中的卓越地位。
The pre-eminence of k(cat) in the manifestation of optimal enzymic activity delineated by using the Briggs-Haldane two-step irreversible kinetic model.
作者信息
Brocklehurst K, Cornish-Bowden A
出版信息
Biochem J. 1976 Oct 1;159(1):165-6. doi: 10.1042/bj1590165.
Abstract
The suggestion by Fersht [(1974) Proc. R. Soc. London Ser. B 187, 397-407] that enzymes that provide maximal rates of catalysis should be characterized by values of Ks, the dissociation constant of the enzyme-substrate complex, greater than 10 times the value of the ambient substrate concentration has been examined. 2. For such enzymes, Ks is not relevant, and attention is best focused on the relative numerical values of k(cat). (in units of s(-1) and the substrate molarity. It is necessary only that the former be about 10(10)-10(11) times the latter to ensure that the rate of product formation be diffusion-limited and thus maximal.
摘要
费什特（1974年，《伦敦皇家学会学报》B辑187卷，397 - 407页）提出，具有最大催化速率的酶应以酶 - 底物复合物解离常数Ks的值来表征，该值应大于环境底物浓度值的10倍，这一观点已得到检验。2. 对于这类酶，Ks并不相关，最好将注意力集中在k(cat)的相对数值上（单位为s(-1)）以及底物摩尔浓度。仅需前者约为后者的10(10) - 10(11)倍，以确保产物形成速率受扩散限制从而达到最大。
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