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 Concept Videos

Introduction to Enzyme Kinetics01:19

Introduction to Enzyme Kinetics

Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate concentrations. Additional trials with inhibitors or other molecules that affect the reaction rate may also be performed.
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...
Enzyme Kinetics01:19

Enzyme Kinetics

Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
Transition State Theory01:25

Transition State Theory

Transition-state theory, also known as activated-complex theory, provides a molecular-level explanation of reaction rates in both gas-phase and solution-phase reactions. It extends earlier kinetic models by considering the formation of a short-lived, high-energy configuration during a reaction.The progress of a chemical reaction can be represented using a reaction profile, which plots potential energy against the reaction coordinate. As two reactant molecules approach one another, their...
Nonlinear Pharmacokinetics: Michaelis-Menten Equation01:18

Nonlinear Pharmacokinetics: Michaelis-Menten Equation

The Michaelis–Menten equation is a fundamental model for describing capacity-limited kinetics in drug metabolism. It offers insights into the rate of decline of plasma drug concentration Cp over time, with Vmax and KM as pivotal parameters.
Vmax represents the maximum achievable process rate, while KM, known as the Michaelis constant, signifies the drug concentration at which the process rate reaches half its maximum. This relationship between Vmax, KM, and Cp gives rise to three distinct...
Fundamental Mathematical Principles in Pharmacokinetics: Rate and Order of Reaction01:15

Fundamental Mathematical Principles in Pharmacokinetics: Rate and Order of Reaction

In pharmacokinetics, the rates and order of reactions play a crucial role in understanding how the body processes drugs and help us comprehend drug absorption, distribution, metabolism, and elimination. A critical concept in pharmacokinetics is the rate constant, which quantifies the speed of a reaction. It provides valuable information about the kinetics of drug elimination. The rate constant allows us to determine the rate at which drugs are eliminated from the body.
Pharmacokinetic reactions...
Arrhenius Plots02:34

Arrhenius Plots

The Arrhenius equation relates the activation energy and the rate constant, k, for chemical reactions. In the Arrhenius equation, k = Ae−Ea/RT, R is the ideal gas constant, which has a value of 8.314 J/mol·K, T is the temperature on the kelvin scale, Ea is the activation energy in J/mole, e is the constant 2.7183, and A is a constant called the frequency factor, which is related to the frequency of collisions and the orientation of the reacting molecules.
The Arrhenius equation can be used to...

You might also read

Related Articles

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

Sort by
Same author

Hysteresis of butyrylcholinesterase in the approach to steady-state kinetics.

Chemico-biological interactions·2005
Same author

What makes biochemical networks tick?

European journal of biochemistry·2004
Same author

Damped oscillatory hysteretic behaviour of butyrylcholinesterase with benzoylcholine as substrate.

European journal of biochemistry·2003
Same author

Critical switch of the metabolic fluxes by phosphofructo-2-kinase:fructose-2,6-bisphosphatase. A kinetic model.

FEBS letters·2002
Same journal

NMR-based serum metabolomic signatures distinguish active tuberculosis from latent tuberculosis infection.

Biophysical chemistry·2026
Same journal

Machine learning-driven identification of pan-PI3K inhibitors: A hybrid virtual screening approach combining naïve Bayesian classification, pharmacophore modeling, and consensus scoring-based molecular docking.

Biophysical chemistry·2026
Same journal

Optimizing grid preparation methods for TEM imaging of amyloid-forming proteins.

Biophysical chemistry·2026
Same journal

Biogenic reduction mechanisms in iron oxide nanoparticle synthesis: Strategies to mitigate microbial resistance.

Biophysical chemistry·2026
Same journal

Novel Pennisetum Alopecuroides-derived activated carbon for high-efficiency Tartrazine Removal: Box-Behnken optimization and DFT-assisted mechanistic insights.

Biophysical chemistry·2026
Same journal

Reactive molecular dynamics investigation of the first steps of coronavirus (COVID-19) viral-protein ligands fragment (SARS-CoV-2).

Biophysical chemistry·2026
See all related articles

Related Experiment Video

Updated: Jun 25, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

Transient enzyme kinetics: graph-theoretic approach.

Boris N Goldstein1

  • 1Institute of Theoretical and Experimental Biophysics Russian Academy of Sciences, 142290, Pushchino, Moscow Region, Russia. goldstein@iteb.ru

Biophysical Chemistry
|February 24, 2009
PubMed
Summary
This summary is machine-generated.

A novel graph-theoretic method simplifies enzyme kinetics analysis. This approach aids in understanding complex reactions like lactate dehydrogenase inhibition and non-monotonous kinetics for accurate parameter estimation.

More Related Videos

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity
14:27

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity

Published on: August 19, 2013

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions
13:00

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions

Published on: April 4, 2014

Related Experiment Videos

Last Updated: Jun 25, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity
14:27

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity

Published on: August 19, 2013

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions
13:00

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions

Published on: April 4, 2014

Area of Science:

  • Biochemistry
  • Chemical Kinetics
  • Systems Biology

Background:

  • Transient enzyme kinetics analysis is complex.
  • Understanding enzyme mechanisms requires accurate kinetic parameter estimation.
  • Lactate dehydrogenase (LDH) inhibition is pH-dependent and involves substrate inhibition.

Purpose of the Study:

  • To introduce a graph-theoretic approach for simplifying transient enzyme kinetics analysis.
  • To demonstrate the application of this method to substrate-inhibited enzymatic reactions, specifically pH-dependent LDH inhibition.
  • To highlight the utility of non-monotonous transient kinetics in parameter estimation.

Main Methods:

  • Utilizing graph theory to construct directed trees and sub-trees from kinetic schemes.
  • Deriving coefficients of the characteristic polynomial for kinetic equations through graphical construction.
  • Applying the method to a model of substrate-inhibited enzymatic reactions, including LDH.

Main Results:

  • The graph-theoretic approach simplifies the analysis of transient enzyme kinetics.
  • A simple time-dependent analytical solution was obtained for a substrate-inhibited enzymatic reaction.
  • Non-monotonous transient kinetics were observed for enzyme pre-incubation with a product, aiding parameter estimation.

Conclusions:

  • Graph-theoretic analysis offers a powerful tool for studying complex enzyme kinetics.
  • Substrate inhibition in LDH may play a role in regulating glycolytic fluxes.
  • The method facilitates accurate kinetic parameter estimation and understanding of enzyme mechanisms.