Schnell, S. and Maini, P. K. (2003) A century of enzyme kinetics. Should we believe in the Km and vmax estimates? Comments in Theoretical Biology, 8 (2-3). pp. 169-187.
The application of the quasi-steady-state approximation (QSSA) in biochemical kinetics allows the reduction of a complex biochemical system with an initial fast transient into a simpler system. The simplified system yields insights into the behavior of the biochemical reaction, and analytical approximations can be obtained to determine its kinetic parameters. However, this process can lead to inaccuracies due to the inappropriate application of the QSSA. Here we present a number of approximate solutions and determine in which regions of the initial enzyme and substrate concentration parameter space they are valid. In particular, this illustrates that experimentalists must be careful to use the correct approximation appropriate to the initial conditions within the parameter space.
|Uncontrolled Keywords:||Enzyme Kinetics, Michaelis-Menten, Quasi-steady-state Approximation, Fitting Procedures, Progress Curves|
|Subjects:||A - C > Biology and other natural sciences|
|Research Groups:||Centre for Mathematical Biology|
|Deposited By:||Philip Maini|
|Deposited On:||17 Nov 2006|
|Last Modified:||20 Jul 2009 14:20|
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