Enzyme kinetics far from the standard quasi-steady-state and equilibrium approximations
<p>Analytic approximations of the time-evolution of the single enzyme-substrate reaction are valid for all but a small region of parameter space in the positive initial enzyme-initial substrate concentration plane. We find velocity equations for the substrate decomposition and product formatio...
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| Format: | Journal article |
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Elsevier
2002
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| _version_ | 1826275526127386624 |
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| author | Schnell, S Maini, P |
| author_facet | Schnell, S Maini, P |
| author_sort | Schnell, S |
| collection | OXFORD |
| description | <p>Analytic approximations of the time-evolution of the single enzyme-substrate reaction are valid for all but a small region of parameter space in the positive initial enzyme-initial substrate concentration plane. We find velocity equations for the substrate decomposition and product formation with the aid of the total quasi-steady-state approximation and an aggregation technique for cases where neither the more normally employed standard nor reverse quasi-steady-state approximations are valid. Applications to determining reaction kinetic parameters are discussed.</p> |
| first_indexed | 2024-03-06T23:00:03Z |
| format | Journal article |
| id | oxford-uuid:61cb40b8-0f07-4a3e-a5e4-269193024ae1 |
| institution | University of Oxford |
| last_indexed | 2024-03-06T23:00:03Z |
| publishDate | 2002 |
| publisher | Elsevier |
| record_format | dspace |
| spelling | oxford-uuid:61cb40b8-0f07-4a3e-a5e4-269193024ae12022-03-26T18:02:10ZEnzyme kinetics far from the standard quasi-steady-state and equilibrium approximationsJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:61cb40b8-0f07-4a3e-a5e4-269193024ae1biology and other natural sciencesSymplectic Elements at OxfordElsevier2002Schnell, SMaini, P<p>Analytic approximations of the time-evolution of the single enzyme-substrate reaction are valid for all but a small region of parameter space in the positive initial enzyme-initial substrate concentration plane. We find velocity equations for the substrate decomposition and product formation with the aid of the total quasi-steady-state approximation and an aggregation technique for cases where neither the more normally employed standard nor reverse quasi-steady-state approximations are valid. Applications to determining reaction kinetic parameters are discussed.</p> |
| spellingShingle | biology and other natural sciences Schnell, S Maini, P Enzyme kinetics far from the standard quasi-steady-state and equilibrium approximations |
| title | Enzyme kinetics far from the standard quasi-steady-state and equilibrium approximations |
| title_full | Enzyme kinetics far from the standard quasi-steady-state and equilibrium approximations |
| title_fullStr | Enzyme kinetics far from the standard quasi-steady-state and equilibrium approximations |
| title_full_unstemmed | Enzyme kinetics far from the standard quasi-steady-state and equilibrium approximations |
| title_short | Enzyme kinetics far from the standard quasi-steady-state and equilibrium approximations |
| title_sort | enzyme kinetics far from the standard quasi steady state and equilibrium approximations |
| topic | biology and other natural sciences |
| work_keys_str_mv | AT schnells enzymekineticsfarfromthestandardquasisteadystateandequilibriumapproximations AT mainip enzymekineticsfarfromthestandardquasisteadystateandequilibriumapproximations |