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

Kinetic barriers under steady-state conditions.

J Südi1

  • 1Abteilung Toxikologie, Christian-Albrechts-Universität, Kiel, Federal Republic of Germany.

The Biochemical Journal
|May 15, 1992
PubMed
Summary
This summary is machine-generated.

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

How to derive steady-state rate laws for enzyme-catalyzed reactions from macroscopic probabilities.

Die Naturwissenschaften·1997
Same author

Control analysis of enzyme mechanisms in terms of the classical steady-state description.

Biochimica et biophysica acta·1997
Same author

[Gluten enteropathy].

Medicinski arhiv·1997
Same author

How to derive flux control coefficients from the rate equations of classical enzyme kinetics.

Mathematical biosciences·1996
Same author

Control analysis of single enzyme sequences with abortive complexes and random substrate binding.

Journal of theoretical biology·1996
Same author

How to draw kinetic barrier diagrams for enzyme-catalysed reactions.

The Biochemical journal·1991
Same journal

Nanobodies against Plasmodium adhesins that block receptor engagement and malaria parasite invasion.

The Biochemical journal·2026
Same journal

Persistence without turnover: the RhoG G12E mutant highlights the role of nucleotide cycling in RhoG signaling.

The Biochemical journal·2026
Same journal

Alternative Splicing of Rice Chloroplastic CuZn Superoxide Dismutase, OsCSD2: Impact on expression and protein characteristics.

The Biochemical journal·2026
Same journal

Difference and similarity between the ubiquitous secretory pathway Ca2+-ATPases, SERCA2b, and SPCA1a.

The Biochemical journal·2026
Same journal

A molecular perspective on dimethylarginine dimethylaminohydrolases structure and function.

The Biochemical journal·2026
Same journal

Proteolytic coordination of the OXPHOS Life Cycle.

The Biochemical journal·2026
See all related articles

Kinetic barrier diagrams reveal a new additivity rule for enzymic reactions under steady-state conditions. This rule equates initial steady-state net fluxes with the overall flux in equilibrium systems, simplifying resistance analysis.

Area of Science:

  • Biochemistry
  • Chemical Kinetics
  • Enzyme Catalysis

Background:

  • Kinetic barrier diagrams are established tools for analyzing enzyme kinetics.
  • Understanding phenomenological resistance to net chemical fluxes under steady-state conditions is crucial for enzymology.

Purpose of the Study:

  • To demonstrate the utility of kinetic barrier diagrams for assessing enzymic turnover resistance.
  • To uncover and elucidate a novel additivity rule governing net flux profiles in enzymatic reactions.

Main Methods:

  • Analysis of a numerical example involving enzymic turnover.
  • Examination of net flux profiles under steady-state and equilibrium conditions.
  • Application of kinetic barrier diagrams to visualize phenomenological resistance.

Related Experiment Videos

Main Results:

  • Kinetic barrier diagrams effectively display the phenomenological resistance of enzymic turnover to net fluxes.
  • A new additivity rule for net flux profiles under limiting conditions was identified.
  • Net fluxes under initial steady-state conditions were found to be identical to the overall flux at equilibrium.

Conclusions:

  • The identified additivity rule provides a direct link between unidirectional and net fluxes.
  • The equality of 'one-way flux resistance' at equilibrium and 'net flux resistance' under steady-state is explained.
  • The findings are applicable to consecutive chemical reactions.