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Related Concept Videos

Enzyme Kinetics01:19

Enzyme Kinetics

105.7K
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...
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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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Enzymes02:34

Enzymes

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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.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
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Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

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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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Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

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Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

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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.
 
Most enzymes...
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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

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Complex Media and Enzymatic Kinetics.

Evangelos Bakalis1, Alice Soldà1, Marios Kosmas2

  • 1Dipartimento di Chimica "G. Ciamician", Università di Bologna , V. F. Selmi 2, 40126, Bologna, Italy.

Analytical Chemistry
|May 6, 2016
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Summary
This summary is machine-generated.

This study presents a generalized enzymatic kinetic model applicable to complex biological environments, moving beyond standard Michaelis-Menten conditions. The new model accurately describes enzyme behavior even when enzyme and substrate concentrations are similar, crucial for cellular and biosensing applications.

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Area of Science:

  • Biochemistry
  • Chemical Engineering
  • Materials Science

Background:

  • Enzymatic reactions in biological systems often occur at enzyme and substrate concentrations that deviate from standard in vitro Michaelis-Menten conditions.
  • These non-standard conditions are prevalent in cellular environments and biosensing applications, necessitating a generalized kinetic model.

Purpose of the Study:

  • To generalize the classical Michaelis-Menten reaction scheme for application in complex biological environments.
  • To develop and validate a new kinetic model that accounts for high enzyme concentrations relative to substrates.

Main Methods:

  • Fabrication of a permeable, micrometrically structured hydrogel matrix via protein cross-linking.
  • Immobilization of glucose oxidase (GOx) enzyme within the hydrogel matrix as a model system.
  • Monitoring hydrogen peroxide (H2O2) production over time and fitting the data to an accurate solution of the generalized enzymatic kinetic scheme.

Main Results:

  • The developed kinetic model accurately describes enzymatic reactions under conditions where enzyme and substrate concentrations are comparable.
  • The model's solution is expressed in terms of simple, applicable functions.
  • Demonstrated the successful application of the generalized model using immobilized glucose oxidase.

Conclusions:

  • The generalized enzymatic kinetic model extends the applicability of Michaelis-Menten kinetics to complex biological systems.
  • This approach is valuable for applications in digital microfluidics and systems biology, particularly where linear kinetic regimes are insufficient.
  • The study provides a framework for understanding enzyme kinetics in non-ideal, biologically relevant conditions.