Enzyme kinetics at high enzyme concentrations
We re-visit previous analyses of the classical Michaelis-Menten substrate-enzyme reaction and, with the aid of the reverse quasi-steady-state assumption, we challenge the approximation d[C]/dt ≈ 0 for the basic enzyme reaction at high enzyme concentration. For the first time, an approximate solution...
| Main Authors: | , |
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| Format: | Journal article |
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2000
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| _version_ | 1797082590238212096 |
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| author | Schnell, S Maini, P |
| author_facet | Schnell, S Maini, P |
| author_sort | Schnell, S |
| collection | OXFORD |
| description | We re-visit previous analyses of the classical Michaelis-Menten substrate-enzyme reaction and, with the aid of the reverse quasi-steady-state assumption, we challenge the approximation d[C]/dt ≈ 0 for the basic enzyme reaction at high enzyme concentration. For the first time, an approximate solution for the concentrations of the reactants uniformly valid in time is reported. Numerical simulations are presented to verify this solution. We show that an analytical approximation can be found for the reactants for each initial condition using the appropriate quasi-steady-state assumption. An advantage of the present formalism is that it provides a new procedure for fitting experimental data to determine reaction constants. Finally, a new necessary criterion is found that ensures the validity of the reverse quasi-steady-state assumption. This is verified numerically. |
| first_indexed | 2024-03-07T01:30:00Z |
| format | Journal article |
| id | oxford-uuid:934a526b-0d68-474b-ba2d-30cd692384d6 |
| institution | University of Oxford |
| last_indexed | 2024-03-07T01:30:00Z |
| publishDate | 2000 |
| record_format | dspace |
| spelling | oxford-uuid:934a526b-0d68-474b-ba2d-30cd692384d62022-03-26T23:31:11ZEnzyme kinetics at high enzyme concentrationsJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:934a526b-0d68-474b-ba2d-30cd692384d6Mathematical Institute - ePrints2000Schnell, SMaini, PWe re-visit previous analyses of the classical Michaelis-Menten substrate-enzyme reaction and, with the aid of the reverse quasi-steady-state assumption, we challenge the approximation d[C]/dt ≈ 0 for the basic enzyme reaction at high enzyme concentration. For the first time, an approximate solution for the concentrations of the reactants uniformly valid in time is reported. Numerical simulations are presented to verify this solution. We show that an analytical approximation can be found for the reactants for each initial condition using the appropriate quasi-steady-state assumption. An advantage of the present formalism is that it provides a new procedure for fitting experimental data to determine reaction constants. Finally, a new necessary criterion is found that ensures the validity of the reverse quasi-steady-state assumption. This is verified numerically. |
| spellingShingle | Schnell, S Maini, P Enzyme kinetics at high enzyme concentrations |
| title | Enzyme kinetics at high enzyme concentrations |
| title_full | Enzyme kinetics at high enzyme concentrations |
| title_fullStr | Enzyme kinetics at high enzyme concentrations |
| title_full_unstemmed | Enzyme kinetics at high enzyme concentrations |
| title_short | Enzyme kinetics at high enzyme concentrations |
| title_sort | enzyme kinetics at high enzyme concentrations |
| work_keys_str_mv | AT schnells enzymekineticsathighenzymeconcentrations AT mainip enzymekineticsathighenzymeconcentrations |