Glutathione S-transferase, C-terminal QuickView

Description:: In eukaryotes, glutathione S-transferases (GSTs) participate in thedetoxification of reactive electrophillic compounds by catalysing theirconjugation to glutathione. The GST domain is also found in S-crystallins from squid, and proteins with no known GST activity, such as eukaryotic elongation factors 1-gamma and the HSP26 family of stress-related proteins, which include auxin-regulated proteins in plants and stringent starvation proteins in Escherichia coli. The major lens polypeptide of cephalopods is also a GST.Bacterial GSTs of known function often have a specific, growth-supporting role in biodegradative metabolism: epoxide ring opening and tetrachlorohydroquinone reductive dehalogenation are two examples of the reactions catalysed by these bacterial GSTs. Some regulatory proteins, like the stringent starvation proteins, also belong to the GST family. GST seems to be absent from Archaea in which gamma-glutamylcysteine substitute to glutathione as major thiol.Glutathione S-transferases form homodimers, but in eukaryotes can also form heterodimers of the A1 and A2 or YC1 and YC2 subunits. The homodimeric enzymes display a conserved structuralfold. Each monomer is composed of a distinct N-terminal sub-domain,which adopts the thioredoxin fold, and a C-terminal all-helicalsub-domain. This entry is the C-terminal domain.
Taxonomy/Path:: InterPro : Glutathione S-transferase, C-terminal-like / Glutathione S-transferase, C-terminal