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Related Concept Videos

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

Determination of Michaelis Constant and Maximum Elimination Rate

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

Nonlinear Pharmacokinetics: Michaelis-Menten Equation

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...
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...

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Related Experiment Video

Updated: Jun 9, 2026

Kinetic Screening of Nuclease Activity using Nucleic Acid Probes
06:52

Kinetic Screening of Nuclease Activity using Nucleic Acid Probes

Published on: November 1, 2019

Enzyme kinetics informatics: from instrument to browser.

Neil Swainston1, Martin Golebiewski, Hanan L Messiha

  • 1Manchester Centre for Integrative Systems Biology, University of Manchester, Manchester, UK. neil.swainston@manchester.ac.uk

The FEBS Journal
|August 27, 2010
PubMed
Summary
This summary is machine-generated.

A new system integrates enzyme kinetics data, linking raw experimental results with curated parameters. This enhances data reliability and accessibility for researchers by connecting SABIO-RK and MeMo-RK databases.

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Area of Science:

  • Biochemistry
  • Bioinformatics
  • Scientific Data Management

Background:

  • Limited public resources exist for enzyme kinetic parameters.
  • Current resources rely on manual data mining, lacking raw experimental data.
  • Lack of standardized software hinders experimental data management.

Purpose of the Study:

  • To introduce an integrative system for managing experimental enzyme kinetics data.
  • To link raw experimental data with curated kinetic parameters.
  • To improve confidence and accessibility of enzyme kinetic data.

Main Methods:

  • Developed an integrative system with two databases: SABIO-RK (kinetic data) and MeMo-RK (raw data).
  • Implemented web browser and web service interfaces for public access.
  • Created a data analysis and submission tool, kineticswizard.

Main Results:

  • The system enables viewing of both kinetic parameters and underlying raw experimental data.
  • Publicly accessible databases (SABIO-RK, MeMo-RK) are now interconnected.
  • The kineticswizard facilitates data collection, analysis, and submission.

Conclusions:

  • The integrative system enhances the reliability and accessibility of enzyme kinetic data.
  • It provides a comprehensive solution from experimental data capture to browser dissemination.
  • The system is extensible for integration with various analytical instruments.