By Abelson J.N., Simon M.I., Sies H. (eds.)
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Floh6, W. A. Gtinzler, and H. H. Schock, F E B S Lett. 32, 132 (1973). 6 j. T. Rotruck, A. L. Pope, H. E. Ganther, A. B. Swanson, D. G. Hafeman, and W. G. Hoekstra, Science 179, 558 (1973). 7 O. A. Levander, in "Selenium in Biology and Medicine" (A. ), p. 205. SpringerVerlag, Berlin, 1989. 8 L. Floh6, in "Glutathione: Chemical, Biochemical, and Medical Aspects" (D. Dolphin, R. Poulson, and O. ), p. 643. Wiley, New York, 1989. 9 T. C. Stadtman, Annu. Rev. Biochem. 49, 93 (1980). lo R. F. Burk and K.
Heider, and C. Baron, Trends Biochem. Sci. 16, 463 (1991). 43 F. Zinoni, J. Heider, and A. B/)ck, Proc. Natl. Acad. Sci. A. 87, 4660 (1990). 44 G. E. Garcia and T. C. Stadtman, J. Bacteriol. 173, 2093 (1991). 45M. J. Berry, L. Banu, J. W. Harnex, and P. R. Larsen, E M B O J. 12, 3315 (1993). 44 GLUTATHIONE [5] proteins maintained up to mammals should deserve more than curiosity, as their mere existence stresses their biological importance. S t r u c t u r e a n d F u n c t i o n of G l u t a t h i o n e P e r o x i d a s e s C o m m o n Features Bovine c G P X has been extensively investigated functionally.
F : I~l ,- i/ Fro. 4. Comparison of the Ccz carbon backbone of a bovine cGPX subunit51 with other members of the cGPX superfamily. (a) Residues of bovine cGPX (red) which are conserved in homologous positions in all members of the superfamily. Note that these residues accumulate around the active-site selenium (orange ball) in the pleated sheets and turns. (b) Overlay of the bovine cGPX structure and a model of human pGPX. Here the pleated sheets are marked in green, and the cz helices in red. Deviations of the pGPX model from the cGPX structure are shown in yellow.
Biothiols: Glutathione & Thioredoxin: Thiols in Signal Transduction & Gene Regulation by Abelson J.N., Simon M.I., Sies H. (eds.)
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