一种pH敏感酶变构调节的模型。
A model for the allosteric regulation of pH-sensitive enzymes.
作者信息
Shindler J S, Tipton K F
出版信息
Biochem J. 1977 Nov 1;167(2):479-82. doi: 10.1042/bj1670479.
Abstract
- In an enzyme that has two independent binding sites for a ligand, any inhibitor that binds solely to the free enzyme will give rise to positive co-operativity. 2. A model is considered for the allosteric control of enzymes by effectors in which their effects are mediated by ligand-induced perturbations of the ionization constants of a group or groups involved in the binding of substrate to the active site. 3. The model described offers a plausible explanation for the observation that the sigmoidal initial-rate curves reported for some regulatory enzymes are not expressed at all pH values where the enzyme is catalytically active.
摘要
- 在一种对配体具有两个独立结合位点的酶中，任何仅与游离酶结合的抑制剂都会产生正协同效应。2. 考虑一种效应物对酶进行别构控制的模型，其中效应物的作用是通过配体诱导参与底物与活性位点结合的一个或多个基团的电离常数扰动来介导的。3. 所描述的模型为以下观察结果提供了一个合理的解释：一些调节酶所报道的S形初始速率曲线并非在该酶具有催化活性的所有pH值下都表现出来。
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