Literature: Glutathione S-transferase, Mu class (IPR003081)
References used in this entry
The following publications were referred to in the abstract:
X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function.
Dirr H, Reinemer P, Huber R.
Eur. J. Biochem. 220 645-61 1994
PMID: 8143720 Related citations
A basis for differentiating among the multiple human Mu-glutathione S-transferases and molecular cloning of brain GSTM5.
Takahashi Y, Campbell EA, Hirata Y, Takayama T, Listowsky I.
J. Biol. Chem. 268 8893-8 1993
PMID: 8473333 Related citations
Evolution of differential substrate specificities in Mu class glutathione transferases probed by DNA shuffling.
Hansson LO, Bolton-Grob R, Massoud T, Mannervik B.
J. Mol. Biol. 287 265-76 1999
PMID: 10080890 Related citations
The following publications were not referred to in the abstract, but provide useful additional information:
Alternative mutations of a positively selected residue elicit gain or loss of functionalities in enzyme evolution.
Norrgard MA, Ivarsson Y, Tars K, Mannervik B.
Proc. Natl. Acad. Sci. U.S.A. 103 4876-81 2006
PMID: 16549767 Related citations
Local protein dynamics and catalysis: detection of segmental motion associated with rate-limiting product release by a glutathione transferase.
Codreanu SG, Ladner JE, Xiao G, Stourman NV, Hachey DL, Gilliland GL, Armstrong RN.
Biochemistry 41 15161-72 2002
PMID: 12484753 Related citations
Transition state model and mechanism of nucleophilic aromatic substitution reactions catalyzed by human glutathione S-transferase M1a-1a.
Patskovsky Y, Patskovska L, Almo SC, Listowsky I.
Biochemistry 45 3852-62 2006
PMID: 16548513 Related citations
Tyr115, gln165 and trp209 contribute to the 1, 2-epoxy-3-(p-nitrophenoxy)propane-conjugating activity of glutathione S-transferase cGSTM1-1.
Chern MK, Wu TC, Hsieh CH, Chou CC, Liu LF, Kuan IC, Yeh YH, Hsiao CD, Tam MF.
J. Mol. Biol. 300 1257-69 2000
PMID: 10903867 Related citations
The enhanced affinity for thiolate anion and activation of enzyme-bound glutathione is governed by an arginine residue of human Mu class glutathione S-transferases.
Patskovsky YV, Patskovska LN, Listowsky I.
J. Biol. Chem. 275 3296-304 2000
PMID: 10652317 Related citations
Shifting substrate specificity of human glutathione transferase (from class Pi to class alpha) by a single point mutation.
Nuccetelli M, Mazzetti AP, Rossjohn J, Parker MW, Board P, Caccuri AM, Federici G, Ricci G, Lo Bello M.
Biochem. Biophys. Res. Commun. 252 184-9 1998
PMID: 9813167 Related citations