| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5371575 | Biophysical Chemistry | 2009 | 5 Pages |
Abstract
A graphical analysis demonstrates the ability of slow substrate activation and certain types of cooperativity between the two enzyme active sites to generate sustained oscillations. The analysis allows us to estimate kinetic parameter values for which oscillations exist. The scheme analyzed can explain the cyclical changes in functioning of various motor enzymes. Moreover, this scheme does not generate bistability for any parameter values. The graphical analysis presented is simple and visually clarifies the regulatory role of the details in the kinetic schemes.
Related Topics
Physical Sciences and Engineering
Chemistry
Physical and Theoretical Chemistry
Authors
B.N. Goldstein, A.M. Aksirov, D.T. Zakrjevskaya,