Glutathione S-transferase Mu 2 is an enzyme that in humans is encoded by the GSTM2gene.[5][6][7]
Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta.
This gene encodes a glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are organized in a gene cluster on chromosome 1p13.3 and are known to be highly polymorphic. These genetic variations can change an individual's susceptibility to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs.[7]
Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID1602151.
Raghunathan S, Chandross RJ, Kretsinger RH, et al. (1994). "Crystal structure of human class mu glutathione transferase GSTM2-2. Effects of lattice packing on conformational heterogeneity". J. Mol. Biol. 238 (5): 815–32. doi:10.1006/jmbi.1994.1336. PMID8182750.
Anttila S, Hirvonen A, Vainio H, et al. (1994). "Immunohistochemical localization of glutathione S-transferases in human lung". Cancer Res. 53 (23): 5643–8. PMID8242618.
Patskovska LN, Fedorov AA, Patskovsky YV, et al. (1998). "Expression, crystallization and preliminary X-ray analysis of ligand-free human glutathione S-transferase M2-2". Acta Crystallogr. D. 54 (Pt 3): 458–60. Bibcode:1998AcCrD..54..458P. doi:10.1107/S0907444997011190. PMID9761928.
Coles BF, Anderson KE, Doerge DR, et al. (2000). "Quantitative analysis of interindividual variation of glutathione S-transferase expression in human pancreas and the ambiguity of correlating genotype with phenotype". Cancer Res. 60 (3): 573–9. PMID10676639.
Weng MW, Hsiao YM, Chiou HL, et al. (2005). "Alleviation of benzo[a]pyrene-diolepoxide-DNA damage in human lung carcinoma by glutathione S-transferase M2". DNA Repair (Amst.). 4 (4): 493–502. doi:10.1016/j.dnarep.2004.12.006. PMID15725629.
PDB gallery
1hna: CRYSTAL STRUCTURE OF HUMAN CLASS MU GLUTATHIONE TRANSFERASE GSTM2-2: EFFECTS OF LATTICE PACKING ON CONFORMATIONAL HETEROGENEITY
1hnb: CRYSTAL STRUCTURE OF HUMAN CLASS MU GLUTATHIONE TRANSFERASE GSTM2-2: EFFECTS OF LATTICE PACKING ON CONFORMATIONAL HETEROGENEITY
1hnc: CRYSTAL STRUCTURE OF HUMAN CLASS MU GLUTATHIONE TRANSFERASE GSTM2-2: EFFECTS OF LATTICE PACKING ON CONFORMATIONAL HETEROGENEITY
1xw5: Human glutathione s-transferase M2-2 (E.C.2.5.1.18)complexed with glutathione, monoclinic crystal form
1ykc: human glutathione S-transferase m2-2 (E.C.2.5.1.18) complexed with glutathione-disulfide
2ab6: HUMAN GLUTATHIONE S-TRANSFERASE M2-2 (E.C.2.5.1.18) complexed with S-METHYLGLUTATHIONE
2c4j: HUMAN GLUTATHIONE-S-TRANSFERASE M2-2 T210S MUTANT IN COMPLEX WITH GLUTATHIONE-STYRENE OXIDE CONJUGATE
2gtu: LIGAND-FREE HUMAN GLUTATHIONE S-TRANSFERASE M2-2 (E.C.2.5.1.18), MONOCLINIC CRYSTAL FORM
3gtu: LIGAND-FREE HETERODIMERIC HUMAN GLUTATHIONE S-TRANSFERASE M2-3 (EC 2.5.1.18), MONOCLINIC CRYSTAL FORM