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

Enzyme Kinetics01:19

Enzyme Kinetics

106.4K
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...
106.4K
Introduction to Enzyme Kinetics01:19

Introduction to Enzyme Kinetics

36.1K
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...
36.1K
SN1 Reaction: Kinetics02:05

SN1 Reaction: Kinetics

10.6K
In an SN2 reaction, the reaction rate depends on both the type of nucleophile and the substrate. A hindered tertiary alkyl halide is practically inert to the SN2 mechanism despite using a strong nucleophile.
However, Sir Christopher Ingold and Edward D. Hughes, who studied the kinetics of various nucleophilic substitution reactions, noticed that a tertiary alkyl halide does undergo a nucleophilic substitution reaction in the presence of a weak nucleophile. While studying the substitution...
10.6K
Enzymes02:34

Enzymes

97.5K
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...
97.5K
Nonlinear Pharmacokinetics: Michaelis-Menten Equation01:18

Nonlinear Pharmacokinetics: Michaelis-Menten Equation

1.4K
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...
1.4K
Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

5.5K
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...
5.5K

You might also read

Related Articles

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

Sort by
Same author

A Miniaturized Enzymatic Lactate Sensor for Continuous Monitoring in Oxygen-Depleted Tissue Microenvironments.

IEEE transactions on bio-medical engineering·2026
Same author

In vitro modeling of nutritional and mitochondria-targeted therapies for osteosarcoma.

bioRxiv : the preprint server for biology·2026
Same author

Cognate amino acid therapies provide preclinical benefit in 19 <i>C. elegans</i> models of ARS2 deficiency.

bioRxiv : the preprint server for biology·2026
Same author

ndufs2<sup>-/-</sup> zebrafish have impaired survival, neuromuscular activity, morphology, and one-carbon metabolism treatable with folic acid.

bioRxiv : the preprint server for biology·2025
Same author

Zagociguat prevented stressor-induced neuromuscular dysfunction, improved mitochondrial physiology, and increased exercise capacity in diverse mitochondrial respiratory chain disease zebrafish models.

Frontiers in pharmacology·2025
Same author

Interpreting the clinical significance of multiple large-scale mitochondrial DNA deletions (MLSMD) in skeletal muscle tissue in the diagnostic evaluation of primary mitochondrial disease.

Frontiers in pharmacology·2025
Same journal

Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

Molecular Basis of Disease Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

General Subjects Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

Erratum to 'on the role of exchangeable hydrogen bonds for the kinetics of P680<sup>+·</sup> Q<sub>A</sub> <sup>-·</sup> formation and P680<sup>+·</sup> Pheo<sup>-·</sup> recombination in photosystem II' [Biochim. Biophys. Acta 1276 (1996) 35-44].

Biochimica et biophysica acta·2019
Same journal

Oligomeric state of the light-harvesting complexes B800-850 and B875 from purple bacterium Rubrivivax gelatinosus in detergent solution.

Biochimica et biophysica acta·2019
Same journal

Regulation of pigment content and enzyme activity in the cyanobacterium Nostoc sp. Mac grown in continuous light, a light-dark photoperiod, or darkness.

Biochimica et biophysica acta·2019
See all related articles

Related Experiment Video

Updated: Apr 11, 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

9.5K

Multiple alternative substrate kinetics.

Vernon E Anderson1

  • 112803 Theresa Drive, Silver Spring, MD 20892, USA.

Biochimica Et Biophysica Acta
|June 9, 2015
PubMed
Summary
This summary is machine-generated.

This study expands enzyme kinetics theory to measure specificity constants for numerous substrates simultaneously. It also advances the measurement of kinetic isotope effects for multiple isotopologs in a single reaction.

Keywords:
Alternate substrateAlternative substrateCombinatorial libraryEnzyme kineticsEnzyme specificityInternal competitionKinetic isotope effectsSpecificity constant

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

20.1K
Defining Substrate Specificities for Lipase and Phospholipase Candidates
08:59

Defining Substrate Specificities for Lipase and Phospholipase Candidates

Published on: November 23, 2016

15.7K

Related Experiment Videos

Last Updated: Apr 11, 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

9.5K
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

20.1K
Defining Substrate Specificities for Lipase and Phospholipase Candidates
08:59

Defining Substrate Specificities for Lipase and Phospholipase Candidates

Published on: November 23, 2016

15.7K

Area of Science:

  • Biochemistry
  • Chemical Kinetics
  • Enzyme Mechanisms

Background:

  • Enzyme specificity is crucial in understanding metabolic pathways.
  • The specificity constant (kcat/Km) is a standard metric for enzyme-substrate interactions.
  • Existing methods often analyze substrates or isotopologs individually.

Purpose of the Study:

  • To develop theoretical frameworks for determining relative specificity constants among a large number of competing substrates.
  • To extend the theory of kinetic isotope effects for internal competition involving three isotopologs.
  • To enable precise kinetic analysis in complex reaction mixtures.

Main Methods:

  • Theoretical expansion of enzyme kinetics principles.
  • Application of internal competition experiments for kinetic measurements.
  • Analysis of Michaelis-Menten kinetics for multiple substrates and isotopologs.

Main Results:

  • A theoretical framework for assessing relative specificity constants of numerous substrates in a single reaction.
  • An extension of kinetic isotope effect theory to three competing isotopologs at non-tracer concentrations.
  • Demonstration of precise kinetic measurements in complex mixtures.

Conclusions:

  • The developed theories enable more efficient and comprehensive analysis of enzyme specificity.
  • These advancements facilitate mechanistic enzymology and the study of enzyme transition states.
  • The methods are applicable to complex biological systems and combinatorial libraries.