Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Enzyme Kinetics

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...

Introduction to Enzyme Kinetics

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...

Catalytically Perfect Enzymes

Catalytically Perfect Enzymes

The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.

Most enzymes...

You might also read

Related Articles

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

Sort by

Same author

Allosteric Inhibitors of Cell-Cycle-Regulated Methyltransferase for Novel Antibiotic Development.

ACS omega·2025

Same author

Mechanism of non-coding RNA regulation of DNMT3A.

Epigenetics & chromatin·2025

Same author

Structural Investigations of Phthalazinone Derivatives as Allosteric Inhibitors of Human DNA Methyltransferase 3A.

ACS medicinal chemistry letters·2024

Same author

Dynamic correlations in lipid bilayer membranes over finite time intervals.

The Journal of chemical physics·2023

Same author

In silico study of selective inhibition mechanism of S-adenosyl-L-methionine analogs for human DNA methyltransferase 3A.

Computational biology and chemistry·2022

Same author

Correlated diffusion in lipid bilayers.

Proceedings of the National Academy of Sciences of the United States of America·2021

Same journal

Anharmonic phonons via quantum thermal bath simulations.

The Journal of chemical physics·2026

Same journal

Quantum simulation of alignment dependent differential cross sections in co-propagating molecular beams at cold collision energies.

The Journal of chemical physics·2026

Same journal

Non-additive ion effects on the coil-globule equilibrium of a generic polymer in aqueous salt solutions.

The Journal of chemical physics·2026

Same journal

Insights into the unexpected small reduction of the temperature of maximum density of water by lithium chloride addition.

The Journal of chemical physics·2026

Same journal

Optical frequency comb double-resonance spectroscopy of the 9030-9175 cm-1 states of ethylene.

The Journal of chemical physics·2026

Same journal

Time reversal breaking of colloidal particles in cells.

The Journal of chemical physics·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Mar 28, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

Extracting enzyme processivity from kinetic assays.

Itay Barel¹, Norbert O Reich¹, Frank L H Brown¹

¹Department of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106, USA.

The Journal of Chemical Physics

|December 17, 2015

Summary

This summary is machine-generated.

This study introduces a general method to analyze enzyme activity using Markovian dynamics, enabling direct measurement of enzyme processivity from experimental data. The approach is validated with DNA modifying enzymes like EcoRI endonuclease.

More Related Videos

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

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

Published on: August 19, 2013

Kinetics of Lagging-strand DNA Synthesis In Vitro by the Bacteriophage T7 Replication Proteins

Kinetics of Lagging-strand DNA Synthesis In Vitro by the Bacteriophage T7 Replication Proteins

Published on: February 25, 2017

Related Experiment Videos

Last Updated: Mar 28, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

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

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

Published on: August 19, 2013

Kinetics of Lagging-strand DNA Synthesis In Vitro by the Bacteriophage T7 Replication Proteins

Kinetics of Lagging-strand DNA Synthesis In Vitro by the Bacteriophage T7 Replication Proteins

Published on: February 25, 2017

Area of Science:

Biochemistry
Molecular Biology
Enzymology

Background:

DNA modifying enzymes exhibit complex translocation mechanisms like sliding and hopping.
Understanding enzyme processivity is crucial for molecular biology and drug development.

Purpose of the Study:

To develop a general steady-state analysis for catalytic turnover of molecules with dual substrate sites.
To introduce a method for direct and unambiguous extraction of enzyme processivity from experimental data.

Main Methods:

Utilized a broad class of Markovian dynamic models for enzyme action.
Developed a general data analysis method applicable beyond initial velocity regimes.
Validated predictions against numerical models and experimental data of EcoRI endonuclease.

Main Results:

The proposed analysis method allows for direct and unambiguous determination of enzyme processivity.
The method is effective for enzymes with two substrate sites and various translocation mechanisms.
Validated the model's predictions using EcoRI endonuclease data.

Conclusions:

The developed steady-state analysis provides a robust tool for quantifying enzyme processivity.
This method advances the understanding of DNA modifying enzymes and their mechanisms.
Offers a broadly applicable approach for analyzing enzyme kinetics and processivity.