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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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Enzyme Allostery: Now Controllable by Light.

Taylor M Courtney1, Alexander Deiters1

  • 1Department of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260, USA.

Cell Chemical Biology
|November 23, 2019
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Summary
This summary is machine-generated.

Researchers used photoswitchable unnatural amino acids to control protein allostery in imidazole glycerol phosphate synthase. Light-induced changes in an azobenzene amino acid isomer dramatically altered enzyme activity.

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Area of Science:

  • Biochemistry
  • Chemical Biology
  • Enzymology

Background:

  • Protein allostery is crucial for regulating enzyme activity.
  • Controlling allosteric regulation using external stimuli remains a challenge.
  • Photoswitchable unnatural amino acids offer a potential mechanism for external control.

Purpose of the Study:

  • To investigate the application of photoswitchable unnatural amino acids for controlling protein allostery.
  • To demonstrate light-induced switching of enzyme activity in a specific enzyme complex.

Main Methods:

  • Incorporation of photoswitchable unnatural amino acids, specifically an azobenzene derivative, into the imidazole glycerol phosphate synthase enzyme complex.
  • Utilizing photoisomerization of the azobenzene moiety to induce conformational changes.
  • Measuring changes in enzyme activity upon light exposure.

Main Results:

  • Successful incorporation of the photoswitchable unnatural amino acid into the enzyme complex.
  • Demonstration of light-induced photoisomerization of the azobenzene amino acid.
  • Significant switching in imidazole glycerol phosphate synthase activity was observed upon photoisomerization.

Conclusions:

  • Photoswitchable unnatural amino acids can be effectively employed to control protein allostery.
  • Light-induced modulation of enzyme activity is achievable through this method.
  • This approach provides a novel tool for studying and manipulating enzyme function.