A note on the kinetics of enzyme action.
A note on the kinetics of enzyme action.
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DOI：
10.1042/bj0190338
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发表时间：
1925-01-01
影响因子：
4.1
通讯作者：
Haldane, JBS
中科院分区：
文献类型：
--
作者：
Briggs, GE;Haldane, JBS
Kuhn [1924] 和其他人已将 Michaelis 和 Menten [1913] 的方程成功应用于许多酶作用的案例。因此，有必要研究其理论基础。考虑不可逆反应 A-+ B，就 A 而言是单分子的，并且由酶催化。假设A的一分子与一种酶可逆地结合，该化合物然后不可逆地变成游离的酶和B，其中B可以代表几个分子。我们可以将其表示为： A+ E= AE B+ E.(ax)(ep) px 现在令 a 为 A 的初始浓度，e 为酶的总浓度，x 为时间 t 后产生的 B 的浓度，p 为时间 t 时酶与底物结合的浓度。我们假设 e 和 p 与 a 和 x 相比小得可以忽略不计。然后根据质量作用定律 dP= k1 (a-x)(e-p)-k2p-k3p，其中 k1、k2、k3 是反应的速度常数
THE equation of Michaelis and Menten [1913] has been applied with success by Kuhn [1924] and others to numerous cases of enzyme action. It is therefore desirable to examine its theoretical basis. Consider the irreversible reaction A-+ B, unimolecular as regards A, and catalysed by an enzyme. Suppose one molecule of A to combine reversibly with one of enzyme, the compound then changing irreversibly into free enzyme and B, where B may represent several molecules. We may represent this as: A+ E= AE B+ E.(ax)(ep) px Now let a be the initial concentration of A, e the total concentration of entyme, x the concentration of B produced after time t, and p the concentration of enzyme combined with substrate at time t. We suppose e and p to be negligibly small compared with a and x. Then by the laws of mass action dP= k1 (a-x)(e-p)-k2p-k3p, where k1, k2, k3 are the velocity constants of the reactions