English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Analytical solutions of a simple enzyme kinetic problem by a perturbative procedure

MPS-Authors
/persons/resource/persons258792

Seshadri,  M.S.
Department of Physical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137659

Fritzsch,  Günter
Department of Physical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Seshadri, M., & Fritzsch, G. (1980). Analytical solutions of a simple enzyme kinetic problem by a perturbative procedure. Biophysics of structure and mechanism, 6(2), 111-123. doi:10.1007/BF00535748.


Cite as: http://hdl.handle.net/21.11116/0000-0009-158B-3
Abstract
A systematic perturbative procedure (the method of singular perturbation) is developed to follow the time evolution of an enzyme catalyzed reaction with one intermediate product over the entire time domain of interest. The perturbation parameter is the ratio of the enzyme concentration to the Michaelis-Menten constant. The treatment leads to a meaningful definition of the so-called quasi-steady state often invoked in the description of enzyme catalyzed reactions. The legitimacy and the domain of validity of this assumption are examined in the context of both the reversible and irreversible Michaelis-Menten kinetics.