In eukaryotes, glutathione S-transferases (GSTs) participate in the detoxification of reactive electrophilic compounds by catalyzing their conjugation to glutathione [1]. The C-terminal GST domain is also found in S-crystallins from squid, and proteins with no known GST activity, such as eukaryotic elongation factors 1 and the Hsp26 family of stress-related proteins. Bacterial GSTs of known function often have a specific, growth-supporting role in biodegradative metabolism. GSTs are composed of an N-terminal domain, which adopts the thioredoxin fold, and a C-terminal all-helical domain.
Allergenic members of this family include allergens from mites (group 8) [2] and cockroaches (group 5) [3] as well as few minor allergens from fungi and plants.
Family-defining Pfam domains (at least one of these domains is present in each family member):
| Pfam domain | Pfam clan | ||
| PF00043 | Glutathione S-transferase, C-terminal domain | CL0497 | Glutathione S-transferase, C-terminal domain |
| PF02798 | Glutathione S-transferase, N-terminal domain | CL0172 | Thioredoxin-like |
| PF13410 | Glutathione S-transferase, C-terminal domain | CL0497 | Glutathione S-transferase, C-terminal domain |
| PF13417 | Glutathione S-transferase, N-terminal domain | CL0172 | Thioredoxin-like |
| PF14497 | Glutathione S-transferase, C-terminal domain | CL0497 | Glutathione S-transferase, C-terminal domain |
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