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doi:10.1016/0014-5793(91)81175-8 
Copyright © 1991 Published by Elsevier Science B.V. All rights reserved.
Cysteine residues are not essential for the catalytic activity of human class Mu glutathione transferase M1a-1a*1
Mikael Widersten, Eva Holmström and Bengt Mannervik
Department of Biochemistry, Uppsala University, Biomedical Center, Box 576, S-751 23 Uppsala, Sweden
Received 17 September 1991.
Abstract
To investigate the possible involvement of a Cys thiol in the catalysis of the human glutathione transferase M1a-1a, we constructed mutants of this enzyme wherein the four Cys residues present in the native enzyme where replaced by Ala residues. Three mutants, one where all four Cys residues had been replaced and two mutants where three out of four Cys residues were changed into Ala, were characterized regarding their catalytic activities with three different substrates as well as by their binding of three different inhibitors. All three Cys-deficient mutant forms of glutathione transferase M1a-1a were catalytically active with the tested substrates and their binding of inhibitors, measured by l50, were not significantly different from the values previously obtained for the wild-type enzyme. We therefore conclude that none of the Cys residues in this class Mu glutathione transferase are directly involved in the catalysis performed by this enzyme.
Author Keywords: Glutathione transferase; Site-directed mutagenesis; Cysteine residue
References
1. B. Mannervik Adv. Enzymol. Rel. Areas Mol. Biol. 57 (1985), pp. 357–417. View Record in Scopus | Cited By in Scopus (406)
2. J. Schäffer, O. Gallay and R. Ladenstein J. Biol. Chem. 263 (1988), pp. 17405–17411. View Record in Scopus | Cited By in Scopus (11)
3. G. Ricci, G. DelBoccio, A. Pennelli, A. Aceto, E.P. Whitehead and G. Federici J. Biol. Chem. 264 (1989), pp. 5462–5467. View Record in Scopus | Cited By in Scopus (10)
4. G. DelBoccio, A. Pennelli, E.P. Whitehead, M. LoBello, R. Petruzzelli, G. Federici and G. Ricci J. Biol. Chem. 266 (1991), pp. 13777–13782. View Record in Scopus | Cited By in Scopus (16)
5. P.A. Hirrell, M.F. Collins, I.A. Nimmo and R.C. Strange Biochim. Biophys. Acta 913 (1987), pp. 92–96. Abstract | 
PDF (342 K)
| View Record in Scopus | Cited By in Scopus (0)
6. K. Tamai, K. Satoh, S. Tsuchida, I. Hatayama, T. Maki and K. Sato Biochem. Biophys. Res. Commun. 167 (1990), pp. 331–338. Abstract | Article | PDF (557 K)
| View Record in Scopus | Cited By in Scopus (37)
7. P. Reinemer, H.W. Dirr, R. Ladenstein, J. Schäffer, O. Gallay and R. Huber EMBO J. 10 (1991), pp. 1997–2005. View Record in Scopus | Cited By in Scopus (171)
8. T. Carne, E. Tipping and B. Ketterer Biochem. J. 177 (1979), pp. 433–439. View Record in Scopus | Cited By in Scopus (10)
9. M.M. Bhargava, I. Listowsky and I.M. Arias J. Biol. Chem. 253 (1978), pp. 4112–4115. View Record in Scopus | Cited By in Scopus (18)
10. D.M. Rhoads, R.P. Zarlengo and C.-P.D. Tu Biochem. Biophys. Res. Commun. 145 (1987), pp. 474–481. Abstract | Article | PDF (507 K)
| View Record in Scopus | Cited By in Scopus (26)
11. D.B. Smith, K.M. Davern, P.G. Board, W.U. Tiu, E.G. Garcia and G.F. Mitchell Proc. Natl. Acad. Sci. USA 83 (1986), pp. 8703–8707. View Record in Scopus | Cited By in Scopus (73)
12. M. Warholm, C. Guthenberg and B. Mannervik Biochemistry 22 (1983), pp. 3610–3617. View Record in Scopus | Cited By in Scopus (48)
13. R. Vince, S. Daluge and W.B. Wadd J. Med. Chem. 14 (1971), pp. 402–404. View Record in Scopus | Cited By in Scopus (47)
14. J.L. DeJong, C.-M. Chang, J. Whang-Peng, T. Knutsen and C.-P.D. Tu Nucleic Acids Res. 16 (1988), pp. 8541–8554. View Record in Scopus | Cited By in Scopus (32)
15. M. Widersten, W.R. Pearson, A. Engström and B. Mannervik Biochem. J. 276 (1991), pp. 519–524. View Record in Scopus | Cited By in Scopus (39)
16. J.W. Taylor, J. Ott and F. Eckstein Nucleic Acids Res. 13 (1985), pp. 8765–8785. View Record in Scopus | Cited By in Scopus (147)
17. F. Sanger, S. Nicklen and A.R. Coulson Proc. Natl. Acad. Sci. USA 74 (1977), pp. 5463–5467. View Record in Scopus | Cited By in Scopus (20586)
18. B. Mannervik and C. Guthenberg Methods Enzymol. 77 (1981), pp. 231–235. Abstract | Article | PDF (265 K)
| View Record in Scopus | Cited By in Scopus (140)
19. U.K. Laemmli Nature 22??? (1970), pp. 680–685. View Record in Scopus | Cited By in Scopus (81403)
20. G.L. Peterson Anal. Biochem. 83 (1977), pp. 346–356. Abstract | Article | PDF (728 K)
| View Record in Scopus | Cited By in Scopus (2514)
21. Farrants A.-K. Ostlund, D.J. Meyer, B. Coles, C. Southan, A. Aitken, P.J. Johnson and B. Ketterer Biochem. J. 245 (1987), pp. 423–428.
22. W.H. Habig and W.B. Jakoby Methods Enzymol. 77 (1981), pp. 398–405. Abstract | Article | PDF (457 K)
| View Record in Scopus | Cited By in Scopus (641)
23. M.K. Tahir and B. Mannervik J. Biol. Chem. 261 (1986), pp. 1048–1051. View Record in Scopus | Cited By in Scopus (22)
24. J.-C. Hsieh, S.-C. Huang, W.-L. Chen, Y.-C. Lai and M.F. Tam Biochem. J. 278 (1991), pp. 293–297. View Record in Scopus | Cited By in Scopus (10)
25. A.E.P. Adang, W.J. Morec, J. Brussee, G.J. Mulder and der Gen A. van Biochem. J. 278 (1991), pp. 63–68. View Record in Scopus | Cited By in Scopus (9)
*1 Glutathione transferase M1a-1a has also been named glutathione transferase μ and glutathione transferase B1B1.
Correspondence address: B. Mannervik, Department of Biochemistry, Uppsala University, Biomedical Center, Box 576, S-751 23 Uppsala, Sweden. Fax: (46) (18) 55 8431.
