Human glutathione S-transferases

Seminars in Liver Disease

Volumn 18, Issue 4, 1998, Pages 345-358

  Whalen, Richard ^a   Boyer, Thomas D ^a  

^a EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Enzyme induction; Glutathione S transferases; Polymorphisms

Indexed keywords

GLUTATHIONE; GLUTATHIONE TRANSFERASE;

ANTIOXIDANT ACTIVITY; CANCER SUSCEPTIBILITY; DETOXIFICATION; ENZYME ACTIVITY; ENZYME INDUCTION; HUMAN; LIVER DISEASE; NONHUMAN; PRIORITY JOURNAL; REVIEW;

EID: 0032437130     PISSN: 02728087     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-2007-1007169     Document Type: Review

References (20)

1. Hayes JD, Pulford DJ. The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit Rev Biochem Mol Biol 1995:30:445-600
2. Seidegard J, Ekstrom G. The role of human glutathione transferases and epoxide hydrolases in the metabolism of xenobiotics. Environ Health Perspect 1997;105(suppl 4):791-799
3. Halliwell B. Reactive oxygen species in living systems: source, biochemistry, and role in human disease. Am J Med 1991;91: 14S-22S
4. Tsuchida S, Sato K. Glutathione transferases and cancer. Crit Rev Biochem Mol Biol 1992;27:337-384
5. Armstrong RN. Structure, catalytic mechanism, and evolution of the glutathione transferases. Chem Res Toxicol 1997;10:2-18
6. Daniel V. Glutathione S-transferases: gene structure and regulation of expression. Crit Rev Biochem Mol Biol 1993;28: 173-207
7. Mannervik B, Awasthi YC, Board PG, et al. Nomenclature for human glutathione transferases. Biochem J 1992;282:305-308
8. Bass NM, Kirsch RE, Tuff SA, et al. Ligandin heterogeneity: evidence that the two non-identical subunits are the monomers of two distinct proteins. Biochim Biophys Acta 1977;492:163-175
9. Board PG. Identification of cDNAs encoding two human alpha class glutathione transferases (GSTA3 and GSTA4) and the heterologous expression of GSTA4- 4. Biochem J 1998;330:827-831
10. Singhal SS, Zimniak P, Sharma R, et al. A novel glutathione S-transferase isozyme similar to GST 8-8 of rat and mGSTA4-4 (GST 5.7) of mouse is selectively expressed in human tissues. Biochim Biophys Acta 1994;1204:279-286
11. Andersson C, Mosialou E, Weinander R, et al. Enzymology of microsomal glutathione S-transferase. Adv Pharmacol 1994;27: 19-35
12. Mosialou E, Andersson C, Lundqvist G, et al. Human liver microsomal glutathione transferase. Substrate specificity and important protein sites. FEBS Lett 1993:315:77-80
13. Bernat BA, Laughlin LT, Armstrong RN. Fosfomycin resistance protein (FosA) is a manganese metalloglutathione transferase related to glyoxalase I and the extradiol dioxygenases. Biochemistry 1997;36:3050-3055
14. Blocki FA, Ellis LB, Wackett LP. MIF protein are theta-class glutathione S-transferase homologs. Protein Sci 1993;2:2095-2102
15. Pearson WR. MIF proteins are not glutathione transferase homologs. Protein Sci 1994;3:525-527
16. Bach MK, Brashler JR, Peck RE, et al. Leukotriene C synthetase, a special glutathione S-transferase: properties of the enzyme and inhibitor studies with special reference to the mode of action of U-60,257, a selective inhibitor of leukotriene synthesis. J Allergy Clin Immunol 1984;74:353-357
17. Nicholson DW, Ali A, Vaillancourt JP, et al. Purification to homogeneity and the N-terminal sequence of human leukotriene C4 synthase: a homodimeric glutathione S-transferase composed of 18-kDa subunits. Proc Natl Acad Sci U S A 1993; 90:2015-2019
18. Reinemer P, Dirr HW, Ladenstein R, et al. The three-dimensional structure of class π glutathione S-transferase in complex with glutathione sulfonate at 2.3 A resolution. EMBO J 1991; 10:1997-2005
19. Reinemer P, Dirr H, Ladenstein R, et al. Three-dimensional structure of class π glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 A resolution. J Mol Biol 1992;227:214-226
20. Sinning I, Kleywegt GJ, Cowan SW, et al. Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the mu and pi class enzymes. J Mol Biol 1993;232:192-212