Mammalian cytosolic glutathione transferases

Curr Protein Pept Sci. 2008 Aug;9(4):325-37. doi: 10.2174/138920308785132677.


Glutathione Transferases (GSTs) are crucial enzymes in the cell detoxification process catalyzing the nucleophilic attack of glutathione (GSH) on toxic electrophilic substrates and producing a less dangerous compound. GSTs studies are of great importance since they have been implicated in the development of drug resistance in tumoral cells and are related to human diseases such as Parkinson's, Alzheimer's, atherosclerois, liver cirrhosis, aging and cataract formation. In this review we start by providing an evolutionary perspective of the mammalian cytosolic GSTs known to date. Later on we focus on the more abundant classes alpha, mu and pi and their structure, catalysis, metabolic associated functions, drug resistance relation and inhibition methods. Finally, we introduce the recent insights on the GST class zeta from a metabolic perspective.

Publication types

  • Review

MeSH terms

  • Aldehydes / chemistry
  • Aldehydes / metabolism
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Evolution, Molecular
  • Glutathione Transferase / chemistry*
  • Glutathione Transferase / classification
  • Glutathione Transferase / genetics
  • Glutathione Transferase / metabolism*
  • Humans
  • JNK Mitogen-Activated Protein Kinases / metabolism
  • Mammals*
  • Models, Molecular
  • Molecular Sequence Data
  • Phylogeny
  • Prostaglandins / chemistry
  • Prostaglandins / metabolism
  • Protein Conformation
  • Sequence Alignment
  • Steroids / chemistry
  • Steroids / metabolism


  • Aldehydes
  • Prostaglandins
  • Steroids
  • Glutathione Transferase
  • JNK Mitogen-Activated Protein Kinases
  • 4-hydroxy-2-nonenal