Про швидкість ферментативних реакцій у міхаеліс–ментен-подібних схемах (ансамблева та одномолекулярна версії)

In searching non-standard ways of conformational regulation, various Michaelis–Menten-like schemes attract relentless attention, resulting in sometimes too sophisticated considerations. With the example of monomeric enzymes possessing an only binding site, we define the minimal schemes capable of be...

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Bibliographic Details
Date:2020
Main Author: Christophorov, L. N.
Format: Article
Language:English
Published: Publishing house "Academperiodika" 2020
Online Access:https://ujp.bitp.kiev.ua/index.php/ujp/article/view/2019615
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Journal Title:Ukrainian Journal of Physics

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Ukrainian Journal of Physics
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Summary:In searching non-standard ways of conformational regulation, various Michaelis–Menten-like schemes attract relentless attention, resulting in sometimes too sophisticated considerations. With the example of monomeric enzymes possessing an only binding site, we define the minimal schemes capable of bearing peculiar regulatory properties like “cooperativity” or substrate inhibition. The simplest ways of calculating the enzymatic reaction velocity are exemplified, either in the ensemble or single-molecule case.