Title | Influence of substrate unbinding on kinetics of enzymatic catalysis |
Publication Type | Journal Article |
Year of Publication | 2019 |
Authors | Christophorov, LN |
Abbreviated Key Title | Dopov. Nac. akad. nauk Ukr. |
DOI | 10.15407/dopovidi2019.01.040 |
Issue | 1 |
Section | Physics |
Pagination | 40-46 |
Date Published | 01/2019 |
Language | Ukrainian |
Abstract | In a minimal kinetic scheme with two conformational states of the enzyme-substrate complex, which differ in their catalytic activity, it is shown that the backward process of substrate unbinding does not always play an inhibitory role. On the contrary, increasing the unbinding rate constant up to certain values can only accelerate the enzyme turnover. Substrate concentration values necessary for making this effect possible are determined. The conclusions are equally applicable to the analysis of either ensemble or single-enzyme experimental data. |
Keywords | conformational states, enzymatic reaction velocity, enzyme-substrate interaction, single macromolecules |
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