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外文期刊>The biochemical journal
>The pre-eminence of kcat. in the manifestation of optimal enzymic activity delineated by using the Briggs-Haldane two-step irreversible kinetic model
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The pre-eminence of kcat. in the manifestation of optimal enzymic activity delineated by using the Briggs-Haldane two-step irreversible kinetic model
pThe 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./p
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机译:> Fersht的建议[(1974)Proc。 R. Soc。伦敦系列[B 187,397-407]认为提供最大催化速率的酶应以Ks值(酶-底物复合物的解离常数,大于环境底物浓度值的10倍)表征。 2.对于这类酶,Ks无关紧要,最好将注意力集中在k(cat)的相对数值上。 (以s(-1)和底物摩尔浓度为单位。前者仅需约后者的10(10)-10(11)倍即可确保产物形成的速率受到扩散限制,从而达到最大 p>
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