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Glutathione S-transferase, N-terminal domain
This family is closely related to Pfam:PF02798. (from Pfam)
glutathione S-transferase N-terminal domain-containing protein
Function: conjugation of reduced glutathione to a variety of targets. Also included in the alignment, but not GSTs: S-crystallins from squid (similarity to GST previously noted); eukaryotic elongation factors 1-gamma (not known to have GST activity and similarity not previously recognised); HSP26 family of stress-related proteins including auxin-regulated proteins in plants and stringent starvation proteins in E. coli (not known to have GST activity and similarity not previously recognised). The glutathione molecule binds in a cleft between the N- and C-terminal domains - the catalytically important residues are proposed to reside in the N-terminal domain [1]. [1]. 9680481. Three-dimensional structure of Escherichia coli glutathione. S-transferase complexed with glutathione sulfonate: catalytic. roles of Cys10 and His106.. Nishida M, Harada S, Noguchi S, Satow Y, Inoue H, Takahashi K;. J Mol Biol 1998;281:135-147. (from Pfam)
glutathione S-transferase
glutathione S-transferase (GST) catalyzes the conjugation of reduced glutathione to a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress
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