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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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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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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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Networks of Dynamic Allostery Regulate Enzyme Function.

Michael Joseph Holliday1, Carlo Camilloni2, Geoffrey Stuart Armstrong3

  • 1Department of Biochemistry and Molecular Genetics, University of Colorado Denver, 12801 East 17th Avenue, MS 8101, Aurora, CO 80045, USA.

Structure (London, England : 1993)
|January 17, 2017
PubMed
Summary
This summary is machine-generated.

Researchers identified dynamic networks in cyclophilin A using a novel method. Key residues were found to modulate enzyme activity, revealing insights into dynamic allostery for enzyme engineering.

Keywords:
allosterycyclophilin Adynamicsisomerizationnuclear magnetic resonanceprotein engineering

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Area of Science:

  • Biochemistry and enzymology
  • Protein dynamics and allostery
  • Molecular biophysics

Background:

  • Protein allostery is crucial for function, but analyzing non-coherently dynamic systems is challenging.
  • Understanding communication mechanisms in these systems is key to enzyme engineering.

Purpose of the Study:

  • To develop and apply a novel methodology for analyzing allosterically coupled dynamic networks in enzymes.
  • To identify key residues and communication pathways involved in enzyme regulation.
  • To explore the link between enzyme dynamics and catalytic function.

Main Methods:

  • Development of the RASSMM (Relaxation and Single-Site Multiple Mutation) technique.
  • Application of RASSMM to study cyclophilin A dynamics.
  • Utilizing nuclear magnetic resonance relaxation and site-directed mutagenesis.
  • Employing molecular dynamics simulations to elucidate coupling mechanisms.

Main Results:

  • Identification of two allosterically coupled dynamic networks in cyclophilin A.
  • Discovery of hotspot residues Val6 and Val29 mediating communication.
  • Demonstration that mutations at hotspots alter active-site dynamics and substrate turnover.
  • Elucidation of the coupling mechanism of a hotspot to dynamic networks via simulations.

Conclusions:

  • Enzyme dynamics are intrinsically linked to the catalytic cycle of cyclophilin A.
  • The RASSMM methodology is effective for dissecting complex allosteric networks.
  • Dynamic allostery can be engineered to precisely tune enzyme function.