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Related Concept Videos

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...
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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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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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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

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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

Published on: January 16, 2016

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Random-walk enzymes.

Chi H Mak1,2, Phuong Pham3, Samir A Afif3

  • 1Department of Chemistry, University of Southern California, Los Angeles, California 90089, USA.

Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics
|October 15, 2015
PubMed
Summary
This summary is machine-generated.

Enzymes use random walks to find targets, creating complex conversion patterns. Our models show these enzyme processes are tightly coupled, matching experimental DNA deamination data.

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Area of Science:

  • Biochemistry
  • Chemical Physics
  • Molecular Biology

Background:

  • Enzymes using random walks to find substrates create complex spatial conversion profiles.
  • These profiles result from coupled scanning and catalysis stochastic processes.

Purpose of the Study:

  • Develop analytical models to understand enzyme conversion profiles.
  • Compare intrusive and passive models for enzyme-substrate interactions.
  • Analyze DNA deamination by activation-induced deoxycytidine deaminase (AID).

Main Methods:

  • Developed analytical models for enzyme scanning and catalysis.
  • Utilized diagrammatic theory and path-integral solutions.
  • Compared model predictions with experimental data on DNA deamination by AID.

Main Results:

  • Intrusive and passive models yield distinct predictions for enzyme activity.
  • Catalysis and diffusion are strongly intertwined in AID deamination.
  • Conversion profiles show strong contextual dependence on surrounding DNA targets.
  • The intrusive model accurately fits experimental deamination data.

Conclusions:

  • Enzyme scanning and catalysis are tightly coupled, influencing spatial conversion profiles.
  • Contextual DNA sequence strongly affects enzyme catalytic rates.
  • Methods can identify sequence-dependent signatures of DNA modification enzymes.
  • Applications include cancer, gene regulation, and epigenetics research.