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Allosteric Regulation01:08

Allosteric Regulation

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Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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Regulation of Metabolism01:19

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Cellular needs and conditions vary from cell to cell and change within individual cells over time. For example, the required enzymes and energetic demands of stomach cells are different from those of fat storage cells, skin cells, blood cells, and nerve cells. Furthermore, a digestive cell works much harder to process and break down nutrients during the time that closely follows a meal compared with many hours after a meal. As these cellular demands and conditions vary, so do the amounts and...
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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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Allosteric Modulation: Dynamics is Double-"E"dged.

Bing Xiong1

  • 1Department of Medicinal Chemistry, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, 555 Zuchongzhi Road, Zhangjiang Hi-Tech Park, Shanghai 201203, P.R. China.

Journal of Medicinal Chemistry
|March 24, 2021
PubMed
Summary
This summary is machine-generated.

Researchers developed the first allosteric inhibitor for Protein Arginine Methyltransferase 6 (PRMT6). This selective inhibitor could help understand PRMT6

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Area of Science:

  • Biochemistry
  • Enzymology
  • Molecular Biology

Background:

  • Protein Arginine Methyltransferase 6 (PRMT6) is a type I enzyme.
  • PRMT6 catalyzes arginine residue methylation.
  • Selective inhibitors are crucial for studying PRMT6 biological functions.

Purpose of the Study:

  • To develop and characterize the first allosteric inhibitor of PRMT6.
  • To understand the mechanism of allosteric inhibition in PRMT6.
  • To compare PRMT6 allosteric inhibition with PRMT5.

Main Methods:

  • Enzyme inhibition assays.
  • Structural analysis of PRMT6.
  • Comparison with PRMT5 allosteric inhibitor data.

Main Results:

  • The first allosteric inhibitor of PRMT6 was identified.
  • Allosteric inhibition is feasible for PRMT6.
  • The dynamics of the double-E loop are critical for allosteric binding.

Conclusions:

  • A novel allosteric inhibitor provides a tool for PRMT6 research.
  • The double-E loop dynamics are key to PRMT6 allosteric inhibition.
  • This work may inform the development of PRMT6-targeted therapeutics.