Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Enzyme kinetics for a two-step enzymic reaction with comparable initial enzyme-substrate ratios.

C L Frenzen1, P K Maini

  • 1Department of Mathematics, Southern Methodist University, Dallas, TX 75275.

Journal of Mathematical Biology
|January 1, 1988
PubMed
Summary

This study expands the quasi-steady state assumption for enzyme-substrate reactions, even when enzyme concentrations are not minimal. New analytical solutions offer accurate predictions for complex reaction kinetics.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Modelling collective invasion with reaction-diffusion equations: When does domain curvature matter?

Applied mathematics letters·2026
Same author

Soliton approximation in continuum models of leader-follower behavior.

Physical review. E·2023
Same author

Structural Features of Microvascular Networks Trigger Blood Flow Oscillations.

Bulletin of mathematical biology·2022
Same author

The role of mechanics in the growth and homeostasis of the intestinal crypt.

Biomechanics and modeling in mechanobiology·2020
Same author

A theoretical framework for transitioning from patient-level to population-scale epidemiological dynamics: influenza A as a case study.

Journal of the Royal Society, Interface·2020
Same author

A simple mechanochemical model for calcium signalling in embryonic epithelial cells.

Journal of mathematical biology·2019

Area of Science:

  • Biochemistry
  • Chemical Kinetics
  • Enzyme Kinetics

Background:

  • The quasi-steady state assumption (QSSA) is crucial for simplifying complex reaction mechanisms in enzyme kinetics.
  • Traditional QSSA often requires the initial enzyme concentration to be significantly lower than the substrate concentration.
  • Extending QSSA validity broadens its applicability to a wider range of biochemical reactions.

Purpose of the Study:

  • To extend the validity of the quasi-steady state assumption (QSSA) for a model double intermediate enzyme-substrate reaction.
  • To include scenarios where the ratio of initial enzyme to substrate concentration is not necessarily small.
  • To develop and validate new analytical solutions for enzyme kinetics under these extended conditions.

Main Methods:

Related Experiment Videos

  • Development of analytical solutions for a double intermediate enzyme-substrate reaction model.
  • Comparison of analytical solutions with numerical solutions of the full system of differential equations.
  • Investigation of conditions under which the extended QSSA is applicable.

    • Main Results:

    • Simple analytical solutions were obtained under specific conditions relating reaction rates and initial substrate concentration.
    • These analytical solutions demonstrated favorable agreement with numerical solutions of the complete reaction model.
    • The study provides a theoretical basis for applying QSSA in previously challenging enzyme kinetic scenarios.

    Conclusions:

    • The quasi-steady state assumption can be validly extended to enzyme-substrate reactions with higher initial enzyme concentrations.
    • The derived analytical solutions offer a computationally efficient and accurate method for analyzing such reactions.
    • Suggested experimental methods could enable the application of QSSA in broader reaction contexts, enhancing kinetic analysis.