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Related Concept Videos

Introduction to Enzyme Kinetics01:19

Introduction to Enzyme Kinetics

19.7K
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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Enzyme Kinetics01:19

Enzyme Kinetics

96.0K
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...
96.0K
Turnover Number and Catalytic Efficiency01:19

Turnover Number and Catalytic Efficiency

9.9K
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....
9.9K
Determination of Michaelis Constant and Maximum Elimination Rate01:20

Determination of Michaelis Constant and Maximum Elimination Rate

69
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...
69
Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

3.9K
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...
3.9K
One-Compartment Open Model: Wagner-Nelson and Loo Riegelman Method for ka Estimation01:24

One-Compartment Open Model: Wagner-Nelson and Loo Riegelman Method for ka Estimation

399
This lesson introduces two critical methods in pharmacokinetics, the Wagner-Nelson and Loo-Riegelman methods, used for estimating the absorption rate constant (ka) for drugs administered via non-intravenous routes. The Wagner-Nelson method relates ka to the plasma concentration derived from the slope of a semilog percent unabsorbed time plot. However, it is limited to drugs with one-compartment kinetics and can be impacted by factors like gastrointestinal motility or enzymatic degradation.
On...
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Related Experiment Video

Updated: Jun 8, 2025

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
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ENKIE: a package for predicting enzyme kinetic parameter values and their uncertainties.

Mattia G Gollub1, Thierry Backes1, Hans-Michael Kaltenbach1

  • 1Department of Biosystems Science and Engineering and SIB Swiss Institute of Bioinformatics, ETH Zurich, 4056 Basel, Switzerland.

Bioinformatics (Oxford, England)
|November 4, 2024
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Summary

The ENzyme KInetics Estimator (ENKIE) predicts enzyme kinetic parameters like KM and kcat using Bayesian models. This tool provides reliable uncertainty estimates, aiding metabolic modeling.

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Area of Science:

  • Biochemistry
  • Systems Biology
  • Computational Biology

Background:

  • Accurate enzyme kinetics are crucial for metabolic modeling.
  • Limited availability and reliability of experimental kinetic parameters hinder progress.

Purpose of the Study:

  • To develop a computational tool for predicting enzyme kinetic parameters.
  • To estimate the uncertainty associated with these predictions.

Main Methods:

  • Utilized Bayesian Multilevel Models.
  • Incorporated five categorical predictors.
  • Achieved prediction performance comparable to deep learning methods.

Main Results:

  • ENKIE accurately predicts Michaelis constant (KM) and catalytic constant (kcat) values.
  • Provided calibrated uncertainty predictions for kinetic parameters.
  • Identified key sources of uncertainty in predictions.

Conclusions:

  • ENKIE simplifies the creation of priors for Bayesian kinetic models.
  • Offers a reliable method for estimating enzyme kinetic parameters.
  • Facilitates advancements in dynamic and enzyme cost modeling.