Abstract
A composite approximate solution of Michaelis–Menten enzyme kinetic equation, which could describe both transient and slow dynamics, was obtained by ordinary perturbation methods in terms of undetermined gauge functions up to a first-order level. It was found that the zeroth-order perturbation function itself solved the paradox due to steady-state approximation and predicted well the maximum enzyme-substrate complex ([ES]max) and time tm to attain it. Extensive kinetic simulations using a chemical kinetic simulator proved the validity of these results. A comparison between simulated and predicted results showed that error in the prediction of tm was negligible when perturbation parameter falls in the range of (0<ε≪1). Apart from these, also the effect of transient dynamics on the linearity of Lineweaver–Burk plot (especially near the origin) has been explained.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
