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| Format: | Recurso digital |
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Zenodo
2025
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| Online Access: | https://doi.org/10.5281/zenodo.17659182 |
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Table of Contents:
- <p>We develop the first biological extension of the Conservative Motion Theory (CMT),<br>showing that enzymatic catalysis can be interpreted as a conservative flow network acting<br>on the reaction coordinate. Traditional Michaelis–Menten kinetics explain turnover rates but<br>fail to account for enzymes that operate near or seemingly beyond the diffusion limit. In the<br>CMT framework, a folded protein creates a low–dimensional, reflection–positive Fredholm<br>kernel that continuously compresses information along a restricted reaction manifold. The<br>transition state is stabilized via real–zero persistence of the kernel, and dimensional reduction<br>of substrate motion naturally yields apparent diffusion–limit breaking. This unified analytic<br>structure explains the efficiency of ultrafast enzymes (SOD, AChE, TIM) and suggests a<br>principled route toward rational design of artificial biocatalysts.</p>