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Active site architecture of polymorphic forms of human glutathione S-transferase P1-1 accounts for their enantioselectivity and disparate activity in the glutathione conjugation of 7beta,8alpha-dihydroxy-9alpha,10alpha-ox y-7,8,9,10-tetrahydrobenzo(a)pyrene.
Hu X, O'Donnell R, Srivastava SK, Xia H, Zimniak P, Nanduri B, Bleicher RJ, Awasthi S, Awasthi YC, Ji X, Singh SV. Hu X, et al. Among authors: ji x. Biochem Biophys Res Commun. 1997 Jun 18;235(2):424-8. doi: 10.1006/bbrc.1997.6777. Biochem Biophys Res Commun. 1997. PMID: 9199210
Structure and function of residue 104 and water molecules in the xenobiotic substrate-binding site in human glutathione S-transferase P1-1.
Ji X, Blaszczyk J, Xiao B, O'Donnell R, Hu X, Herzog C, Singh SV, Zimniak P. Ji X, et al. Biochemistry. 1999 Aug 10;38(32):10231-8. doi: 10.1021/bi990668u. Biochemistry. 1999. PMID: 10441116
Third, in the hydrophilic portion of the H-site of the I104 complex, five H-site water molecules [Ji, X., et al. (1997) Biochemistry 36, 9690-9702] are observed, whereas in the V104 complex, two of the five have been displaced by the Bpd moiety of GSBpd. ...
Third, in the hydrophilic portion of the H-site of the I104 complex, five H-site water molecules [Ji, X., et al. (1997) Bioche …
9,903 results