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Related Concept Videos

Induced-fit Model01:13

Induced-fit Model

Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon.
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical characteristics of...
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...
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...
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...
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...
Fast Reactions01:27

Fast Reactions

Fast reactions occurring in times shorter than the time needed to mix reactants pose a unique challenge for investigation. In a liquid-phase continuous-flow system, reactants A and B are swiftly pushed into the mixing chamber, where mixing occurs within 1 ms. The reaction mixture then flows through an observation tube, and one measures light absorption to determine species concentrations at various points of the tube. This method is most appropriate when relatively large volumes of reactants...

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Related Experiment Video

Updated: Jul 12, 2026

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

Transient-time analysis of substrate-channelling in interacting enzyme systems.

J Ovádi1, P Tompa, B Vértessy

  • 1Institute of Enzymology, Hungarian Academy of Sciences, Budapest.

The Biochemical Journal
|January 1, 1989
PubMed
Summary

This study examines enzyme kinetics in dynamically interacting systems. We express transient time using intermediate substrate lifetime, revealing insights into enzyme

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Last Updated: Jul 12, 2026

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity
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Published on: August 19, 2013

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Area of Science:

  • Biochemistry and enzymology
  • Chemical kinetics
  • Systems biology

Background:

  • Dynamically interacting enzyme systems are increasingly recognized in vivo.
  • Understanding their kinetics is crucial for elucidating biological pathways.

Purpose of the Study:

  • To analyze the kinetics of dynamically interacting enzyme systems.
  • To express transient time as a function of intermediate substrate lifetime.
  • To investigate enzyme 'channelling' mechanisms.

Main Methods:

  • Mathematical modeling of coupled enzyme reactions.
  • Analysis of transient time and pseudo-first-order rate constants.
  • Extension of kinetic models to N-coupled reactions.

Main Results:

  • Transient time is directly related to intermediate substrate lifetime.
  • Kinetic parameters reveal mechanisms of intermediate transfer (channelling).
  • Parameters for interacting systems are composite functions of individual enzyme processes.

Conclusions:

  • The study provides a kinetic framework for dynamically interacting enzyme systems.
  • The model can be extended to complex, multi-step enzymatic pathways.
  • This work advances the understanding of enzyme organization and function in vivo.