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Allosteric Regulation01:08

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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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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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A flexible, allosteric loop regulates protein activity and rewires electrostatics.

Darex J Vera-Rodríguez1, Paul J Sapienza2, Konstantin I Popov1,2

  • 1Department of Biochemistry and Biophysics, School of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA.

Protein Science : a Publication of the Protein Society
|September 24, 2025
PubMed
Summary

Flexible loops in proteins can control enzyme activity. A study on chorismate mutase shows a distal loop, previously unseen, influences enzyme function by interacting with the active site, revealing new allosteric regulation mechanisms.

Keywords:
NMRallosteryloopsparamagnetic relaxation enhancementprotein dynamicsprotein electrostatics

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Allosteric regulation is crucial for protein function, traditionally linked to structured regions.
  • The role of distal, flexible loops in allostery is poorly understood.
  • Chorismate mutase (CM) is essential for aromatic amino acid biosynthesis and differentially regulated.

Purpose of the Study:

  • Investigate the allosteric mechanism of chorismate mutase (CM).
  • Explore the function of distal, flexible loops in protein regulation.
  • Elucidate how effector binding influences enzyme activity through remote elements.

Main Methods:

  • Investigated chorismate mutase (CM) using mutagenesis and NMR spectroscopy.
  • Employed paramagnetic labeling to study loop dynamics.
  • Utilized a novel NMR approach to analyze electrostatic modulation.

Main Results:

  • A mutation in the flexible loop 11-12 significantly altered CM's activity.
  • Loop 11-12 transiently interacts with the active site upon tryptophan (Trp) binding.
  • Loop 11-12 modulates enzyme electrostatics, influencing activity.

Conclusions:

  • Flexible, distal loops can be functionally coupled to effector binding sites and active sites.
  • This study reveals a sophisticated allosteric mechanism involving remote loop dynamics and electrostatics.
  • Findings provide new insights into protein allosteric regulation and the function of flexible regions.