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Related Concept Videos

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.
 
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Enzyme Kinetics01:19

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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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Cofactors and Coenzymes01:24

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Enzymes are proteins made of amino acids. The functional group of each constituent amino acid catalyzes a wide variety of chemical reactions via ionic interactions or acid-base reactions. However, amino acids cannot catalyze oxidation-reduction and group transfer reactions and need to be aided by non-protein components called cofactors. Cofactors are also referred to as the chemical teeth of an enzyme.
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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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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.
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Enzyme Inhibition01:30

Enzyme Inhibition

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Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.
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Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
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Evolution of enzyme functionality in the flavin-containing monooxygenases.

Gautier Bailleul1, Guang Yang1, Callum R Nicoll2

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|February 23, 2023
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This summary is machine-generated.

Enzyme functional diversification allows animals to adapt to new environments. A few key amino acid changes transformed an ancestral flavin-containing monooxygenase (FMO) into a specialized enzyme, highlighting critical residues beyond the active site.

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Area of Science:

  • Molecular biology
  • Biochemistry
  • Evolutionary biology

Background:

  • Enzyme functional diversification is a key molecular mechanism for biological adaptation.
  • Flavin-containing monooxygenases (FMOs) are crucial for detoxifying foreign substances (xenobiotics) in animals.
  • Understanding enzyme evolution is vital for comprehending how organisms adapt to new environments.

Purpose of the Study:

  • To investigate the historical amino acid substitutions driving flavin-containing monooxygenase (FMO) functional diversification in tetrapods.
  • To elucidate how a few key substitutions can alter enzyme function and specificity.
  • To explore the role of specific amino acid residues in modulating enzyme activity.

Main Methods:

  • Paleobiochemistry approach to reconstruct ancestral enzyme functions.
  • Enzymology techniques to characterize enzyme activity and specificity.
  • Comparative analysis of FMO gene families across tetrapod lineages.

Main Results:

  • Identified a specific set of historical amino acid substitutions responsible for FMO functional diversification in tetrapods.
  • Demonstrated that a small number of amino acid replacements can convert a multi-tasking ancestral FMO into a specialized monooxygenase.
  • Showcased how these substitutions modulate the oxygenating flavin intermediate, altering enzyme function.
  • Highlighted the importance of residues outside the active site core in determining enzymatic function.

Conclusions:

  • Enzymatic function is critically dependent on a limited set of amino acid residues, not solely confined to the active site.
  • The evolution of FMOs in tetrapods provides a model for understanding enzyme adaptation and specialization.
  • This study underscores the power of paleobiochemistry in revealing the evolutionary trajectory of enzyme function.