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The Pseudouridine Synthases Proceed through a Glycal Intermediate.

Govardhan Reddy Veerareddygari1, Sanjay K Singh1, Eugene G Mueller1

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This summary is machine-generated.

Pseudouridine synthases convert uridine (U) to pseudouridine (Ψ) via a glycal intermediate. This mechanism, involving C2

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Pseudouridine synthases catalyze the isomerization of uridine (U) to pseudouridine (Ψ) in RNA.
  • The precise catalytic mechanism of these enzymes has been a long-standing question in molecular biology.

Purpose of the Study:

  • To elucidate the reaction mechanism employed by pseudouridine synthases.
  • To investigate the potential role of a glycal intermediate in pseudouridine formation.

Main Methods:

  • Mechanistic studies using a probe molecule, 5-fluorouridine.
  • Kinetic isotope effect analysis using deuterated substrate at the C2' position.

Main Results:

  • Evidence suggests a glycal intermediate formed by deprotonation at the C2' position.
  • A primary kinetic isotope effect was observed when C2' of uridine was deuterated.
  • This observation confirms deprotonation at C2' as a key step in the isomerization process.

Conclusions:

  • The findings establish the mechanism of pseudouridine synthases.
  • The reaction proceeds through a deprotonation at C2' to form a glycal intermediate, followed by isomerization to pseudouridine.