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The elusive roles of bacterial glutathione S-transferases: new lessons from genomes

Abstract.

Glutathione S-transferases constitute a large family of enzymes which catalyze the addition of glutathione to endogenous or xenobiotic, often toxic electrophilic chemicals. Eukaryotic glutathione S-transferases usually promote the inactivation, degradation or excretion of a wide range of compounds by formation of the corresponding glutathione conjugates. In bacteria, by contrast, the few glutathione S-transferases for which substrates are known, such as dichloromethane dehalogenase, 1,2-dichloroepoxyethane epoxidase and tetrachlorohydroquinone reductase, are catabolic enzymes with an essential role for growth on recalcitrant chemicals. Glutathione S-transferase genes have also been found in bacterial operons and gene clusters involved in the degradation of aromatic compounds. Information from bacterial genome sequencing projects now suggests that glutathione S-transferases are present in large numbers in proteobacteria. In particular, the genomes of three Pseudomonas species each include at least ten different glutathione S-transferase genes. Several of the corresponding proteins define new classes of the glutathione S-transferase family and may also have novel functions that remain to be elucidated.

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Similar content being viewed by others Explore related subjectsDiscover the latest articles and news from researchers in related subjects, suggested using machine learning. Author information Authors and Affiliations
  1. Institut für Mikrobiologie, ETH Zürich, Schmelzbergstrasse 7, 8092 Zürich, Switzerland, , , , ,

    S. Vuilleumier

  2. Swiss Institute of Bioinformatics, Chemin des Boveresses 155, 1066 Épalinges, Switzerland, , , , ,

    M. Pagni

Authors
  1. S. Vuilleumier
  2. M. Pagni
Additional information

Received revision: 3 September 2001

Electronic Publication

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Vuilleumier, .S., Pagni, .M. The elusive roles of bacterial glutathione S-transferases: new lessons from genomes. Appl Microbiol Biotechnol 58, 138–146 (2002). https://doi.org/10.1007/s00253-001-0836-0

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