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| Format: | Preprint |
| Published: |
2024
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| Online Access: | https://arxiv.org/abs/2411.08058 |
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| _version_ | 1866913576768241664 |
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| author | Hatakeyama, Tetsuhiro S. |
| author_facet | Hatakeyama, Tetsuhiro S. |
| contents | Increasing the enzyme concentration generally speeds up enzymatic reactions. However, in this Letter, we show that increasing the enzyme concentration can also slow down the enzymatic reaction. We consider a simple allosteric protein with multiple modification sites, catalyzed by two enzymes with the same catalytic activity, but slightly different affinities. We show that increasing the concentration of one enzyme can slow the relaxation to the equilibrium state. The mechanism for this slowing is similar the Markovian Mpemba effect, and we name this phenomenon as the Enzymatic Mpemba effect. |
| format | Preprint |
| id |
arxiv_https___arxiv_org_abs_2411_08058 |
| institution | arXiv |
| publishDate | 2024 |
| record_format | arxiv |
| spellingShingle | Enzymatic Mpemba Effect: Slowing of biochemical reactions by increasing enzyme concentration Hatakeyama, Tetsuhiro S. Chemical Physics Statistical Mechanics Biomolecules Increasing the enzyme concentration generally speeds up enzymatic reactions. However, in this Letter, we show that increasing the enzyme concentration can also slow down the enzymatic reaction. We consider a simple allosteric protein with multiple modification sites, catalyzed by two enzymes with the same catalytic activity, but slightly different affinities. We show that increasing the concentration of one enzyme can slow the relaxation to the equilibrium state. The mechanism for this slowing is similar the Markovian Mpemba effect, and we name this phenomenon as the Enzymatic Mpemba effect. |
| title | Enzymatic Mpemba Effect: Slowing of biochemical reactions by increasing enzyme concentration |
| topic | Chemical Physics Statistical Mechanics Biomolecules |
| url | https://arxiv.org/abs/2411.08058 |