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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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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.
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Introduction to Mechanisms of Enzyme Catalysis01:13

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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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Catalytically Perfect Enzymes01:07

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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.
 
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Induced-fit Model01:13

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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.
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Enzymes02:34

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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.
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Modeling an Enzyme Active Site using Molecular Visualization Freeware
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A model for single-substrate trimolecular enzymatic kinetics.

Wei Chen1, Cheng Zhu

  • 1Woodruff School of Mechanical Engineering, Georgia Institute of Technology, Atlanta, Georgia, USA.

Biophysical Journal
|May 6, 2010
PubMed
Summary
This summary is machine-generated.

We created a kinetic model for complex enzymatic reactions involving receptors and enzymes. This model simplifies to Michaelis-Menten kinetics under specific conditions, accurately predicting experimental data for blood clotting systems.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Biophysics

Background:

  • Enzymatic reactions are often modeled using Michaelis-Menten kinetics.
  • Trimolecular enzymatic systems, involving a receptor, substrate, and enzyme, exhibit complex kinetics.
  • Understanding these complex systems is crucial for biological processes like hemostasis.

Purpose of the Study:

  • To develop a kinetic model for a single-substrate trimolecular enzymatic system.
  • To analyze the conditions under which trimolecular kinetics simplify to Michaelis-Menten kinetics.
  • To apply the model to the von Willebrand factor-glycoprotein Ibalpha-ADAMTS13 system.

Main Methods:

  • Developed a theoretical kinetic model for a trimolecular enzymatic system.
  • Analyzed limiting cases of fast equilibrium and slow dissociation.
  • Applied the model to the von Willebrand factor (vWF)/glycoprotein Ibalpha (GPIbα)/ADAMTS13 system.
  • Validated the model using published single-molecule and ensemble experimental data.

Main Results:

  • The general kinetics of the trimolecular system are more complex than Michaelis-Menten kinetics.
  • Under fast enzyme-substrate equilibrium, kinetics reduce to Michaelis-Menten.
  • Under slow receptor dissociation, the system simplifies to bimolecular kinetics.
  • The model accurately predicted and fitted experimental data for the vWF/GPIbα/ADAMTS13 system.

Conclusions:

  • The developed kinetic model provides a more comprehensive understanding of trimolecular enzymatic systems.
  • The model accurately describes the kinetics of the vWF/GPIbα/ADAMTS13 system, relevant to hemostasis and thrombosis.
  • This framework can be applied to other similar complex enzymatic systems.