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Related Concept Videos

Introduction to Enzyme Kinetics01:19

Introduction to Enzyme Kinetics

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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...
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Turnover Number and Catalytic Efficiency01:19

Turnover Number and Catalytic Efficiency

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The turnover number of an enzyme is the maximum number of substrate molecules it can transform per unit time. Turnover numbers for most enzymes range from 1 to 1000 molecules per second. Catalase has the known highest turnover number, capable of converting up to 2.8×106 molecules of hydrogen peroxide into water and oxygen per second. Lysozyme has the lowest known turnover number of half a molecule per second.
Chymotrypsin is a pancreatic enzyme that breaks down proteins during digestion....
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Enzyme Kinetics01:19

Enzyme Kinetics

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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...
97.0K
Determination of Michaelis Constant and Maximum Elimination Rate01:20

Determination of Michaelis Constant and Maximum Elimination Rate

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The Michaelis constant (KM) and the theoretical maximum process rate (Vmax) are vital parameters in the Michaelis-Menten equation, central to many biochemical reactions. They provide essential insights into enzyme kinetics and drug metabolism.
These parameters can be estimated by analyzing plasma concentration data post-drug administration. A notable example of this application is phenytoin, a drug with capacity-limited kinetics. It's recommended that phenytoin should be administered at two...
118
Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

4.0K
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...
4.0K
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

8.2K
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...
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Related Experiment Video

Updated: Jul 12, 2025

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions
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Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions

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Analysis of continuous enzyme kinetic data using ICEKAT.

Karina L Bursch1, Michael D Olp2, Brian C Smith3

  • 1Department of Biochemistry, Medical College of Wisconsin, Watertown Plank Road, Milwaukee, WI, United States.

Methods in Enzymology
|October 20, 2023
PubMed
Summary
This summary is machine-generated.

ICEKAT is a free online tool for analyzing enzyme kinetic assay data. It helps researchers accurately calculate initial rates and kinetic parameters, improving assay reliability and reproducibility.

Keywords:
Computer modelingEC(50)Enzyme activatorEnzyme catalysisEnzyme inhibitorEnzyme kineticsIC(50)Initial rateMichaelis–MentenSteady-state kinetics

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The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis
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Last Updated: Jul 12, 2025

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Area of Science:

  • Biochemistry
  • Enzymology
  • Computational Biology

Background:

  • Enzyme kinetics analysis is crucial for understanding enzyme function.
  • Accurate calculation of kinetic parameters (Vmax, Km, etc.) requires robust tools.
  • Existing methods may lack consistency or ease of use for continuous assays.

Purpose of the Study:

  • To provide an updated guide and highlight new features for the Interactive Continuous Enzyme Analysis Tool (ICEKAT).
  • To ensure rapid, reliable, and repeatable analysis of continuous enzyme kinetic data.
  • To support educational and research settings with a free, accessible software solution.

Main Methods:

  • ICEKAT is a web-based interactive program.
  • It calculates initial rates and kinetic parameters from continuous enzyme kinetic assay data.
  • The tool adheres to Michaelis-Menten and steady-state kinetic assumptions.

Main Results:

  • ICEKAT has been cited in over 26 publications since its 2020 debut.
  • The initial publication has seen nearly 9000 accesses.
  • The tool is freely available online with source code provided.

Conclusions:

  • ICEKAT enhances the veracity and reproducibility of enzyme kinetic studies.
  • The software facilitates more efficient and dependable data analysis for scientists globally.
  • ICEKAT is a valuable, free resource for the scientific community.