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Related Concept Videos

Inhibition of Cdk Activity02:34

Inhibition of Cdk Activity

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The orderly progression of the cell cycle depends on the activation of Cdk protein by binding to its cyclin partner. However, the cell cycle must be restricted when undergoing abnormal changes. Most cancers correlate to the deregulated cell cycle, and since Cdks are a central component of the cell cycle, Cdk inhibitors are extensively studied to develop anticancer agents. For instance, cyclin D associates with several Cdks, such as Cdk 4/6, to form an active complex. The cyclin D-Cdk4/6 complex...
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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
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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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Turnover Number and Catalytic Efficiency01:19

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The turnover number of an enzyme is the maximum number of substrate molecules it can transform per unit time. Turnover numbers for most enzymes range from 1 to 1000 molecules per second. Catalase has the known highest turnover number, capable of converting up to 2.8×106 molecules of hydrogen peroxide into water and oxygen per second. Lysozyme has the lowest known turnover number of half a molecule per second.
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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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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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Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
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Catalytic Protein Inhibitors.

Thomas Kodadek1

  • 1Department of Chemistry, The Herbert Wertheim UF Scripps Institute for Biomedical Innovation & Technology, 120 Scripps Way, Jupiter, FL 33458, USA.

Angewandte Chemie (International Ed. in English)
|December 8, 2023
PubMed
Summary

Developing catalytic protein inhibitors, like protein degraders, offers a novel strategy to overcome challenges in targeting difficult proteins. This approach enhances drug potency beyond traditional affinity improvements.

Keywords:
CatalysisInhibitorMolecular GluePROTACPhoto-Oxidation

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Area of Science:

  • Medicinal Chemistry
  • Drug Discovery
  • Chemical Biology

Background:

  • Difficult-to-drug proteins represent significant challenges in treating various diseases.
  • Traditional small molecule inhibitors often struggle with sufficient affinity and residence time for these targets.
  • There is a need for innovative strategies to enhance the potency of protein inhibitors.

Purpose of the Study:

  • To explore the development of catalytic protein inhibitors as a strategy to overcome limitations of traditional inhibitors.
  • To discuss the rise of protein degraders as a key area within catalytic inhibition.
  • To review the current landscape and future prospects of catalytic inhibitor development.

Main Methods:

  • Review of existing literature and research in catalytic protein inhibition.
  • Analysis of strategies for increasing inhibitor potency beyond affinity.
  • Focus on the mechanisms and applications of protein degraders.

Main Results:

  • Catalytic inhibitors, particularly protein degraders, are emerging as a powerful approach.
  • This strategy offers a route to enhance drug potency by targeting protein destruction.
  • Significant investment and research are driving this burgeoning field.

Conclusions:

  • Catalytic protein inhibitors represent a promising frontier in drug discovery for challenging targets.
  • Protein degraders are at the forefront of this field, catalyzing target protein destruction.
  • Continued innovation in catalytic inhibition holds potential for future therapeutic breakthroughs.