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Related Concept Videos

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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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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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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Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
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Related Experiment Video

Updated: Feb 10, 2026

Rapid, Cost-Efficient, Enzyme-Free Passaging of Human Pluripotent Stem Cells on Feeder Cells by Ethylenediaminetetraacetic Acid-Mediated Dis-Adhesion
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How can enzymes be so efficient?

Dudley H Williams1, Elaine Stephens, Min Zhou

  • 1Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, UK CB2 1EW.

Chemical Communications (Cambridge, England)
|August 26, 2003
PubMed
Summary

Proteins gain binding energy by reducing their movement and becoming more rigid. This structural tightening enhances interactions with ligands and enzyme substrates.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Dynamics

Background:

  • Proteins exhibit dynamic behavior, which is crucial for their function.
  • Ligand-receptor and enzyme-substrate interactions are fundamental in biological processes.
  • Understanding the energetic contributions to molecular binding is key in drug discovery.

Purpose of the Study:

  • To investigate the relationship between protein structural dynamics and binding energy.
  • To explore how changes in protein flexibility influence ligand-receptor and enzyme-substrate interactions.

Main Methods:

  • Analysis of protein structural data.
  • Computational modeling of protein dynamics.
  • Thermodynamic measurements of binding affinities.

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Main Results:

  • Protein structural tightening correlates with increased binding energy for both ligands and substrates.
  • A decrease in protein dynamic behavior was observed upon successful binding.
  • Reduced flexibility enhances the stability of protein-ligand and enzyme-substrate complexes.

Conclusions:

  • Protein structural rigidity plays a significant role in achieving high binding affinity.
  • Modulating protein dynamics offers a potential strategy for designing more effective drugs and enzymes.