Evolution of functional diversity as observed through structural studies of glutathione transferases

Michael W. Parker, William J. McKinstry, Aaron J. Oakley, Galina Polekhina, Jamie Rossjohn, Gareth Chelvanayagam, Philip G. Board, Carmine Di Ilio, Anna Maria Caccuri, Giorgio Ricci, Mario Lo Bello

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2 Citations (Scopus)


Most enzymes bind specifically to one or to a few closely related substrates. However, this is not the case for the enzyme superfamily of glutathione S-transferases (GSTs). The enzyme's ability to recognise a diverse range of substrates is due, in part, to the existence of isoforms. We have determined the crystal structures of GSTs from four classes and from a diverse range of organisms ranging from bacteria to human. These studies are revealing the molecular basis and evolutionary development of how GSTs recognise and react with a structurally diverse array of toxins.

Original languageEnglish
Pages (from-to)8-12
Number of pages5
JournalChemico-Biological Interactions
Issue number1-3
Publication statusPublished - 28 Feb 2001
Externally publishedYes


  • Crystallography
  • Evolution
  • Glutathione transferase
  • Structure

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