Mechanism and binding specificity of beta-glucosidase-catalyzed hydrolysis of cellobiose analogues studied by competition enzyme kinetics monitored by 1H-NMR spectroscopy.
Mechanism and binding specificity of beta-glucosidase-catalyzed hydrolysis of cellobiose analogues studied by competition enzyme kinetics monitored by 1H-NMR spectroscopy.
复制标题
通过 1 H-NMR 光谱监测竞争酶动力学研究 β-葡萄糖苷酶催化纤维二糖类似物水解的机制和结合特异性。
DOI：
10.1111/j.1432-1033.1989.tb14502.x
复制
发表时间：
1989
期刊：
影响因子：
--
通讯作者：
B. W. Sigurskjold
中科院分区：
文献类型：
--
作者：
K. Bock;B. W. Sigurskjold
应用高分辨率1H-NMR光谱监测底物和产品的时间依赖性的进展曲线酶动力学与β-葡萄糖苷酶催化水解的纤维二糖类似物作为例子。它表明，抑制模式，相对结合特异性和催化速率可以推断从竞争实验与两个或两个以上的基板。从竞争实验中可以得出结论，由于催化步骤中较低的活化能，形成比甲基β-纤维二糖苷更不稳定的酶-底物复合物的底物在作为唯一底物时比该参比底物水解得更快，但是在直接竞争中它们水解得比参比化合物更慢，这是因为在结合步骤中形成了较不稳定的酶-底物复合物。
The application of high-resolution 1H-NMR spectroscopy to monitor substrate and product time dependencies in progress curve enzyme kinetics is described with beta-glucosidase-catalyzed hydrolyses of cellobiose analogues as examples. It is demonstrated that inhibition patterns, relative binding specificities and catalytic rates can be inferred from competition experiments with two or more substrates. It could be concluded from competition experiments that substrates which form less stable enzyme-substrate complexes than methyl beta-cellobioside are hydrolyzed faster than this reference substrate when they are the sole substrate, due to a lower activation energy in the catalytic step, but that they are hydrolyzed slower than the reference compound in direct competition, due to the formation of the less stable enzyme-substrate complex in the binding step.
从进度曲线进行酶动力学研究。
影响因子：
4.1
作者：
E. Canela;R. Franco
通讯作者：
R. Franco