Role of cytoplasmic thioltransferase in cellular regulation by thiol-disulphide interchange

Biochem J. 1980 Jul 15;190(1):125-30. doi: 10.1042/bj1900125.

Abstract

Cytoplasmic thioltransferase purified from rat liver [Axelsson, Eriksson & Mannervik (1978) Biochemistry 17, 2978--2984] catalyses the formation and decomposition of mixed disulphides of proteins and glutathione. The enzyme was found to catalyse the reversible thiol-disulphide interchange between glutathione disulphide and a crude thiol-containing protein fraction from rat liver. This finding indicates a role of the thioltransferase in the regulation of the 'glutathione status' of the cell. Specifically, it was found that thioltransferase catalyses the reactivation of pyruvate kinase from rat liver that had previously been inactivated by glutathione disulphide. It is suggested that thioltransferase may have a general role in regulatory processes involving thiol-disulphide interchange.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cytoplasm / enzymology
  • Disulfides / metabolism*
  • Enzyme Activation / drug effects
  • Glutaredoxins
  • Glutathione / metabolism
  • Glutathione / pharmacology
  • In Vitro Techniques
  • Liver / enzymology*
  • Oxidoreductases / metabolism*
  • Protein Disulfide Reductase (Glutathione)*
  • Proteins / metabolism
  • Pyruvate Kinase / metabolism
  • Rats
  • Sulfhydryl Compounds / metabolism*
  • Transferases / pharmacology

Substances

  • Disulfides
  • Glutaredoxins
  • Proteins
  • Sulfhydryl Compounds
  • Oxidoreductases
  • Protein Disulfide Reductase (Glutathione)
  • Transferases
  • Pyruvate Kinase
  • Glutathione