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Thioltransferases

W W Wells1, Y Yang, T L Deits

  • 1Department of Biochemistry, Michigan State University, East Lansing.

Advances in Enzymology and Related Areas of Molecular Biology
|January 1, 1993
PubMed
Summary
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Thioltransferases, also known as glutaredoxins, are crucial proteins found across many species. Research confirms their universal distribution and highlights a key amino acid sequence critical for their function in thiol-disulfide exchange.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Thioltransferases (glutaredoxins) are small proteins with thiol-disulfide exchange activity found widely in E. coli and mammalian systems.
  • While not previously reported in plants, dehydroascorbate reductase from peas exhibits similar catalytic activity, suggesting universal distribution.

Purpose of the Study:

  • To investigate the critical structural features and universal distribution of thioltransferases (glutaredoxins).
  • To clarify the relationship between thioltransferase and glutaredoxin nomenclature.
  • To explore the functional significance of conserved amino acid sequences in enzyme activity.

Main Methods:

  • Analysis of mutagenesis studies to identify critical amino acid sequences.
  • Comparison of protein sequences and properties across different species (E. coli, yeast, mammals, plants).

Related Experiment Videos

  • Enzyme activity assays, including dehydroascorbate reductase and thiol-disulfide exchange.

    • Main Results:

    • A conserved sequence (Cys-Pro-Tyr(Phe)-Cys- followed by Arg-Lys- or Lys) is essential for both thiol-disulfide exchange and dehydroascorbate reductase activity.
    • The N-terminal cysteine in this motif has a low pKa, enhancing S-nucleophilicity.
    • Mammalian and yeast thioltransferases show variations in N- and C-terminal extensions and cysteine pairs compared to E. coli glutaredoxin.

    Conclusions:

    • Thioltransferase and glutaredoxin are synonymous, based on sequence, immunological, and enzymatic similarities.
    • The identified conserved sequence is critical for the enzymatic function of these proteins.
    • Further research is needed to explain the inability of some mammalian thioltransferases to act as electron carriers in ribonucleotide reductase systems.