Identification, characterization, and crystal structure of the Omega class glutathione transferases

J Biol Chem. 2000 Aug 11;275(32):24798-806. doi: 10.1074/jbc.M001706200.


A new class of glutathione transferases has been discovered by analysis of the expressed sequence tag data base and sequence alignment. Glutathione S-transferases (GSTs) of the new class, named Omega, exist in several mammalian species and Caenorhabditis elegans. In humans, GSTO 1-1 is expressed in most tissues and exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities characteristic of the glutaredoxins. The structure of GSTO 1-1 has been determined at 2.0-A resolution and has a characteristic GST fold (Protein Data Bank entry code ). The Omega class GSTs exhibit an unusual N-terminal extension that abuts the C terminus to form a novel structural unit. Unlike other mammalian GSTs, GSTO 1-1 appears to have an active site cysteine that can form a disulfide bond with glutathione.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Caenorhabditis elegans / enzymology
  • Crystallography, X-Ray
  • Female
  • Glutathione Transferase / chemistry*
  • Glutathione Transferase / genetics
  • Glutathione Transferase / metabolism*
  • Humans
  • Isoenzymes / chemistry
  • Isoenzymes / genetics
  • Isoenzymes / metabolism
  • Kinetics
  • Male
  • Mammals
  • Models, Molecular
  • Molecular Sequence Data
  • Phylogeny
  • Protein Conformation
  • Protein Structure, Secondary
  • Sequence Tagged Sites
  • Substrate Specificity
  • Transcription, Genetic


  • Isoenzymes
  • Glutathione Transferase

Associated data

  • GENBANK/AF212303
  • PDB/1EEM