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| Content Provider | Springer Nature Link |
|---|---|
| Author | Vuilleumier, S. Pagni, M. |
| Copyright Year | 2001 |
| 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. |
| Starting Page | 138 |
| Ending Page | 146 |
| Page Count | 9 |
| File Format | |
| ISSN | 01757598 |
| Journal | Applied Microbiology and Biotechnology |
| Volume Number | 58 |
| Issue Number | 2 |
| e-ISSN | 14320614 |
| Language | English |
| Publisher | Springer-Verlag |
| Publisher Date | 2001-11-29 |
| Publisher Place | Berlin, Heidelberg |
| Access Restriction | Subscribed |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Applied Microbiology and Biotechnology Biotechnology |
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