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

Introduction to Mechanisms of Enzyme Catalysis

Introduction to Mechanisms of Enzyme Catalysis

For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes...

Enzymes

Enzymes

Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...

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...

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...

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 Enzymes

Introduction to Enzymes

The use of enzymes by humans dates to 7000 BCE. Humans first used enzymes to ferment sugars and produce alcohol without knowing that this was an enzyme-catalyzed reaction. Wilhelm Kuhne coined the term 'enzyme' in 1877 from the Greek words ‘en’ meaning ‘in’ or ‘within’ and ‘zyme’ meaning ‘yeast.’
Most enzymes are proteins that speed up biochemical reactions without being consumed. Enzymes contain one or more active sites that...

You might also read

Related Articles

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

Sort by

Same author

Metabolic thermodynamics: pertinent reference state and energy potentials.

The FEBS journal·2026

Same author

Simulated digestions of free oligosaccharides and mucin-type O-glycans reveal a potential role for Clostridium perfringens.

Scientific reports·2024

Same author

In silico analysis of the human milk oligosaccharide glycome reveals key enzymes of their biosynthesis.

Scientific reports·2022

Same author

Enzyme nomenclature and classification: the state of the art.

The FEBS journal·2021

Same author

Simulating the enzymes of ganglioside biosynthesis with Glycologue.

Beilstein journal of organic chemistry·2021

Same author

Degradation of thymic humoral factor γ2 in human, rat and mouse blood: An experimental and theoretical study.

Biochimica et biophysica acta. Proteins and proteomics·2020

Search research articles

Related Experiment Video

Updated: Oct 7, 2025

Measuring Enzymatic Stability by Isothermal Titration Calorimetry

Measuring Enzymatic Stability by Isothermal Titration Calorimetry

Published on: March 26, 2019

Parameter Reliability and Understanding Enzyme Function.

Andrew G McDonald¹, Keith F Tipton¹

¹School of Biochemistry and Immunology, Trinity Biomedical Sciences Institute, Trinity College Dublin, D02 PN40 Dublin, Ireland.

Molecules (Basel, Switzerland)

|January 11, 2022

Summary

This summary is machine-generated.

Understanding Michaelis-Menten parameters is crucial for enzyme studies. This review focuses on evaluating the validity and appropriateness of published enzyme kinetic data for specific research applications.

Keywords:

Michaelis constant bisubstrate kinetics cooperativity enzyme inhibition enzyme kinetics maximal velocity parameter uncertainties substrate competition

More Related Videos

Defining Substrate Specificities for Lipase and Phospholipase Candidates

Defining Substrate Specificities for Lipase and Phospholipase Candidates

Published on: November 23, 2016

High-throughput Fluorometric Measurement of Potential Soil Extracellular Enzyme Activities

High-throughput Fluorometric Measurement of Potential Soil Extracellular Enzyme Activities

Published on: November 15, 2013

Related Experiment Videos

Last Updated: Oct 7, 2025

Measuring Enzymatic Stability by Isothermal Titration Calorimetry

Measuring Enzymatic Stability by Isothermal Titration Calorimetry

Published on: March 26, 2019

Defining Substrate Specificities for Lipase and Phospholipase Candidates

Defining Substrate Specificities for Lipase and Phospholipase Candidates

Published on: November 23, 2016

High-throughput Fluorometric Measurement of Potential Soil Extracellular Enzyme Activities

High-throughput Fluorometric Measurement of Potential Soil Extracellular Enzyme Activities

Published on: November 15, 2013

Area of Science:

Biochemistry
Enzyme kinetics

Background:

Michaelis-Menten parameters are fundamental to understanding enzyme kinetics.
Numerous enzyme kinetic values are available in scientific literature.

Purpose of the Study:

To review methods for evaluating the appropriateness and validity of published enzyme kinetic data.
To emphasize assessing the fitness of published data for specific research purposes.

Main Methods:

Literature review of methods for data evaluation.
Focus on 'fitness for purpose' assessment criteria.

Main Results:

The review highlights the critical need for rigorous evaluation of published enzyme kinetic data.
Established criteria for assessing data validity are discussed.

Conclusions:

Researchers must critically assess published Michaelis-Menten parameters.
Ensuring data 'fitness for purpose' is essential for reliable enzyme behavior studies.