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Glutathione transferases--structure and catalytic activity.

B Mannervik1, U H Danielson

  • 1Department of Biochemistry, University of Uppsala, Sweden.

CRC Critical Reviews in Biochemistry
|January 1, 1988
PubMed
Summary

Glutathione transferases (GSTs) are key enzymes in detoxifying harmful substances. Research classifies these enzymes into distinct classes, revealing their evolutionary origins and catalytic mechanisms.

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Role of the glutamyl alpha-carboxylate of the substrate glutathione in the catalytic mechanism of human glutathione transferase A1-1.

Biochemistry·2001

Area of Science:

  • Biochemistry
  • Enzymology
  • Molecular Biology

Background:

  • Glutathione transferases (GSTs) are crucial enzymes involved in the biotransformation of xenobiotics, including drugs and environmental pollutants.
  • Multiple GST forms exist across various species (mammals, insects, plants) and have been isolated and characterized.
  • Classification of GSTs relies on enzymatic properties, antibody reactions, and structural characteristics.

Purpose of the Study:

  • To classify glutathione transferases based on their enzymatic, immunological, and structural properties.
  • To investigate the evolutionary relationships among different GST classes.
  • To elucidate the substrate specificities and catalytic mechanisms of GSTs.

Main Methods:

  • Isolation and characterization of numerous transferases from mammalian tissues, insects, and plants.
  • Enzymatic assays, antibody cross-reactivity studies, and primary structure comparisons.
  • Analysis of substrate binding sites using homologous series and chiral substrates, coupled with steady-state kinetics.

Main Results:

  • Cytosolic mammalian GSTs are grouped into Alpha, Mu, and Pi classes; microsomal GST differs significantly.
  • Homologous GST enzyme classes are found in human, rat, and mouse tissues.
  • Primary structure comparisons suggest divergent evolution from a common precursor.
  • Organic hydroperoxides, epoxides, quinones, and activated alkenes are identified as potential natural substrates, with 4-hydroxyalkenals being particularly effective.
  • Kinetic studies support a sequential catalytic mechanism.

Conclusions:

  • Glutathione transferases represent a diverse enzyme superfamily with conserved structural and functional roles in xenobiotic metabolism.
  • The classification into distinct classes aids in understanding their specific functions and evolutionary history.
  • Further research into GSTs can inform strategies for managing drug metabolism and environmental pollutant detoxification.

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