A novel selenium-containing glutathione transferase zeta1-1, the activity of which surpasses the level of some native glutathione peroxidases

International Journal of Biochemistry and Cell Biology

Volumn 40, Issue 10, 2008, Pages 2090-2097

  Zheng, Keyan ^a   Board, Philip G ^b   Fei, Xiaofang ^a   Sun, Ye ^a   Lv, Shaowu ^a   Yan, Ganglin ^a   Liu, Junqiu ^a   Shen, Jiacong ^a   Luo, Guimin ^a  

^a JILIN UNIVERSITY   (China)

^b Biology and Environment   (Australia)

Author keywords

Chemical mutation; Enzyme mimics; Glutathione peroxidase; Human glutathione transferase zeta1 1; Selenium containing human glutathione transferase zeta1 1

Indexed keywords

GLUTATHIONE PEROXIDASE; GLUTATHIONE TRANSFERASE; GLUTATHIONE TRANSFERASE ZETA 1 1; PEROXIDASE; SELENIUM;

ANIMAL TISSUE; ANTIOXIDANT ACTIVITY; ARTICLE; BINDING SITE; CATALYSIS; CHEMICAL REACTION; CHEMICAL STRUCTURE; ENZYME ACTIVITY; KINETICS; MATHEMATICAL ANALYSIS; MICHAELIS CONSTANT; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN EXPRESSION; PROTEIN PURIFICATION; RABBIT; RAT; X RAY PHOTOELECTRON SPECTROSCOPY;

CATALYSIS; GLUTATHIONE PEROXIDASE; GLUTATHIONE TRANSFERASE; HUMANS; KINETICS; SELENIUM; SERINE; SPECTRUM ANALYSIS; TOSYL COMPOUNDS;

ORYCTOLAGUS CUNICULUS; RATTUS;

EID: 48949117532     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2008.02.006     Document Type: Article

References (33)

1. Armstrong R.N. Structure, catalytic mechanism, and evolution of the glutathione transferases. Chemical Research in Toxicology 10 (1997) 2-18
2. Babizhayev M.A. Failure to withstand oxidative stress induced by phospholipid hydroperoxides as a possible cause of the lens opacities in systemic diseases and ageing. Biochimica et Biophysica Acta 1315 (1996) 87-99
3. Blackburn A.C., Tzeng H.F., Anders M.W., and Board P.G. Discovery of a functional polymorphism in human glutathione transferase zeta by expressed sequence tag database analysis. Pharmacogenetics 10 (2000) 49-57
4. Board P.G., and Anders M.W. Human glutathione transferase zeta. Methods in Enzymology 401 (2005) 61-77
5. Board P.G., Baker R.T., Chelvanayagam G., and Jermiin L.S. Zeta, a novel class of glutathione transferases in a range of species from plants to humans. The Biochemical Journal 328 (1997) 929-935
6. Board P.G., Chelvanayagam G., Jermiin L.S., Tetlow N., Tzeng H.F., Anders M.W., et al. Identification of novel glutathione transferases and polymorphic variants by expressed sequence tag database analysis. Drug Metabolism and Disposition: The Biological Fate of Chemicals 29 (2001) 544-547
7. Board P.G., Taylor M.C., Coggan M., Parker M.W., Lantum H.B., and Anders M.W. Clarification of the role of key active site residues of glutathione transferase zeta/maleylacetoacetate isomerase by a new spectrophotometric technique. The Biochemical Journal 374 (2003) 731-737
8. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72 (1976) 248-254
9. Burke M.P., and Opeskin K. Fulminant heart failure due to selenium deficiency cardiomyopathy (Keshan disease). Medicine, Science, and the Law 42 (2002) 10-13
10. Cavallini D., Graziani M.T., and Dupre S. Determination of disulphide groups in proteins. Nature 212 (1966) 294-295
11. Chiu D., Tappel A.L., and Millard M.M. Improved procedure for X-ray photoelectron spectroscopy of selenium-glutathione peroxidase and application to the rat liver enzyme. Archives of Biochemistry and Biophysics 184 (1977) 209-214
12. Chu F.F., Doroshow J.H., and Esworthy R.S. Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI. The Journal of Biological Chemistry 268 (1993) 2571-2576
13. Davis R.L., Lavine C.L., Arredondo M.A., McMahon P., and Tenner Jr. T.E. Differential indicators of diabetes-induced oxidative stress in New Zealand White rabbits: Role of dietary vitamin E supplementation. International Journal of Experimental Diabetes Research 3 (2002) 185-192
14. Ding L., Liu Z., Zhu Z.Q., Luo G.M., Zhao D.Q., and Ni J.Z. Biochemical characterization of selenium-containing catalytic antibody as a cytosolic glutathione peroxidase mimic. The Biochemical Journal 332 (1998) 251-255
15. Dirr H.W., Reinemer P., and Huber R. X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function. European Journal of Biochemistry 220 (1994) 645-661
16. Epp O., Ladenstein R., and Wendel A. The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution. European Journal of Biochemistry 133 (1983) 51-69
17. Flohé L. Coenzymes and Cofactors: Glutathione-Chemical, Biochemical, and Medical Aspects (1989), John Wiley & Sons, New York pp. 644-731
18. Flohé L., Loschen G., Cunzler W.A., and Eichele E. Glutathione peroxidase, V. The kinetic mechanism. Hoppe-Seyler's Zeitschrift für physiologische Chemie 353 (1972) 987-999
19. Forgione M.A., Cap A., Liao R., Moldovan N.I., Eberhardt R.T., Lim C.C., et al. Heterozygous cellular glutathione peroxidase deficiency in the mouse: Abnormalities in vascular and cardiac function and structure. Circulation 27 (2002) 1154-1158
20. Forstron J.W., Zakowski J.J., and Tappel A.L. Identification of the catalytic site of rat liver glutathione peroxidase as selenocysteine. Biochemistry 17 (1978) 2639-2644
21. Klayman D.L., and Griffin T.S. Reaction of selenium with sodium borohydride in protic solvents. A facile method for the introduction of selenium into organic molecules. Journal of the American Chemical Society 95 (1973) 197-199
22. Ma W.C., Luo G.M., and Yang T.S. Purification of glutathione peroxidase from rabbit liver by using affinity chromatography. Chinese Journal of Biochemistry and Molecular Biology 9 (1993) 234-236
23. Maiorino M., Roche C., Kiess M., Koenig K., Gawlik D., Matthes M., et al. A selenium-containing phospholipid-hydroperoxide glutathione peroxidase in Schistosoma mansoni. European Journal of Biochemistry 238 (1996) 838-844
24. Polekhina G., Board P.G., Blackburn A.C., and Parker M.W. Crystal structure of maleylacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity. Biochemistry 40 (2001) 1567-1576
25. Ren X.J., Jemth P., Board P.G., Luo G.M., Mannervik B., Liu J.Q., et al. A semisynthetic glutathione peroxidase with high catalytic efficiency: Selenoglutathione transferase. Chemistry & Biology 9 (2002) 789-794
26. Sun Y., Li T.Y., Chen H., Zhang K., Zheng K.Y., Mu Y., et al. Selenium-containing 15-mer peptides with high glutathione peroxidase-like activity. The Journal of Biological Chemistry 279 (2004) 37235-37240
27. Tong Z., Board P.G., and Anders M.W. Glutathione transferase zeta-catalyzed biotransformation of dichloroacetic acid and other alpha-haloacids. Chemical Research in Toxicology 11 (1998) 1332-1338
28. Tong Z., Board P.G., and Anders M.W. Glutathione transferase zeta catalyses the oxygenation of the carcinogen dichloroacetic acid to glyoxylic acid. The Biochemical Journal 331 (1998) 371-374
29. Vanhaelen N., Francis F., and Haubruge E. Purification and characterization of glutathione S-transferases from two syrphid flies (Syrphus ribesii and Myathropa florea). Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology 137 (2004) 95-100
30. Wilson S.R., Zucker P.A., Huang R.R.C., and Spector A. Development of synthetic compounds with glutathione peroxidase activity. Journal of the American Chemical Society 111 (1989) 5936-5939
31. Yamamoto Y., and Takahashi K. Glutathione peroxidase isolated plasma reduces phospholipid hydroperoxides. Archives of Biochemistry and Biophysics 305 (1993) 541-545
32. Yu H.J., Liu J.Q., Bo{combining double acute accent}ck A., Li J., Luo G.M., and Shen J.C. Engineering glutathione transferase to a novel glutathione peroxidase mimic with high catalytic efficiency. The Journal of Biological Chemistry 280 (2005) 11930-11935
33. Zielinski S., and Pörtner H.O. Oxidative stress and antioxidative defense in cephalopods: A function of metabolic rate or age?. Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology 125 (2000) 147-160