Detailed enzyme kinetics in terms of biochemical species: study of citrate synthase.
The compulsory-ordered ternary catalytic mechanism for two-substrate two-product enzymes is analyzed to account for binding of inhibitors to each of the four enzyme states and to maintain the relationship between the kinetic constants and the reaction equilibrium constant. The developed quasi-steady...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2008-03-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC2266798?pdf=render |
| _version_ | 1830475400748204032 |
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| author | Daniel A Beard Kalyan C Vinnakota Fan Wu |
| author_facet | Daniel A Beard Kalyan C Vinnakota Fan Wu |
| author_sort | Daniel A Beard |
| collection | DOAJ |
| description | The compulsory-ordered ternary catalytic mechanism for two-substrate two-product enzymes is analyzed to account for binding of inhibitors to each of the four enzyme states and to maintain the relationship between the kinetic constants and the reaction equilibrium constant. The developed quasi-steady flux expression is applied to the analysis of data from citrate synthase to determine and parameterize a kinetic scheme in terms of biochemical species, in which the effects of pH, ionic strength, and cation binding to biochemical species are explicitly accounted for in the analysis of the data. This analysis provides a mechanistic model that is consistent with the data that have been used support competing hypotheses regarding the catalytic mechanism of this enzyme. |
| first_indexed | 2024-12-21T15:35:45Z |
| format | Article |
| id | doaj.art-d0a05f9a1b824de095c0c78ddce9da0f |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-21T15:35:45Z |
| publishDate | 2008-03-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-d0a05f9a1b824de095c0c78ddce9da0f2022-12-21T18:58:39ZengPublic Library of Science (PLoS)PLoS ONE1932-62032008-03-0133e182510.1371/journal.pone.0001825Detailed enzyme kinetics in terms of biochemical species: study of citrate synthase.Daniel A BeardKalyan C VinnakotaFan WuThe compulsory-ordered ternary catalytic mechanism for two-substrate two-product enzymes is analyzed to account for binding of inhibitors to each of the four enzyme states and to maintain the relationship between the kinetic constants and the reaction equilibrium constant. The developed quasi-steady flux expression is applied to the analysis of data from citrate synthase to determine and parameterize a kinetic scheme in terms of biochemical species, in which the effects of pH, ionic strength, and cation binding to biochemical species are explicitly accounted for in the analysis of the data. This analysis provides a mechanistic model that is consistent with the data that have been used support competing hypotheses regarding the catalytic mechanism of this enzyme.http://europepmc.org/articles/PMC2266798?pdf=render |
| spellingShingle | Daniel A Beard Kalyan C Vinnakota Fan Wu Detailed enzyme kinetics in terms of biochemical species: study of citrate synthase. PLoS ONE |
| title | Detailed enzyme kinetics in terms of biochemical species: study of citrate synthase. |
| title_full | Detailed enzyme kinetics in terms of biochemical species: study of citrate synthase. |
| title_fullStr | Detailed enzyme kinetics in terms of biochemical species: study of citrate synthase. |
| title_full_unstemmed | Detailed enzyme kinetics in terms of biochemical species: study of citrate synthase. |
| title_short | Detailed enzyme kinetics in terms of biochemical species: study of citrate synthase. |
| title_sort | detailed enzyme kinetics in terms of biochemical species study of citrate synthase |
| url | http://europepmc.org/articles/PMC2266798?pdf=render |
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