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Related Concept Videos

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...
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...
Reaction Rate02:53

Reaction Rate

The rate of reaction is the change in the amount of a reactant or product per unit time. Reaction rates are therefore determined by measuring the time dependence of some property that can be related to reactant or product amounts. Rates of reactions that consume or produce gaseous substances, for example, are conveniently determined by measuring changes in volume or pressure.
The mathematical representation of the change in the concentration of reactants and products, over time, is the rate...
Introduction to Mechanisms of Enzyme Catalysis01:13

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 a mild...
Introduction to Mechanisms of Enzyme Catalysis01:13

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 a mild...
Enzymes02:34

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...

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Related Experiment Video

Updated: Jun 19, 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

ON THE RATE OF REACTION BETWEEN ENZYME AND SUBSTRATE.

J Berkson1, L B Flexner

  • 1Department of Pediatrics of The Johns Hopkins University School of Medicine, Baltimore.

The Journal of General Physiology
|October 30, 2009
PubMed
Summary

A novel equation accurately describes viscosity changes in enzyme-substrate reactions, specifically observed in gelatin and pancreatin mixtures. This finding, derived from bimolecular reaction principles, offers a new model for enzyme kinetics.

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

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Related Experiment Videos

Last Updated: Jun 19, 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

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

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

Area of Science:

  • Biochemistry
  • Chemical Kinetics

Background:

  • Enzyme kinetics are crucial for understanding biochemical processes.
  • Accurate modeling of enzyme-substrate interactions is essential for predicting reaction rates and outcomes.

Purpose of the Study:

  • To develop and validate a mathematical equation describing the change in viscosity during enzyme-substrate reactions.
  • To theoretically derive this equation from fundamental principles of chemical kinetics.

Main Methods:

  • Empirical observation of viscosity changes in a gelatin and pancreatin mixture over time.
  • Mathematical modeling to fit the observed viscosity data to a proposed equation.
  • Theoretical derivation of the equation based on the mass action law for bimolecular reactions.

Main Results:

  • An equation accurately models the time-dependent viscosity changes in a gelatin-pancreatin mixture.
  • The same equation form was applicable to other enzyme-substrate systems.
  • The equation can be theoretically derived from a bimolecular reaction model.

Conclusions:

  • A new equation provides an accurate description of viscosity changes in enzyme-substrate reactions.
  • The derived equation is based on the fundamental principles of bimolecular reactions and the mass action law.
  • This model has broad applicability to various enzyme-substrate interactions.