Role of the C-terminal helix 9 in the stability and ligandin function of class α glutathione transferase Al-1

Biochemistry

Volumn 38, Issue 47, 1999, Pages 15631-15640

  Dirr, Heini W ^a   Wallace, Louise A ^a  

^a UNIVERSITY OF THE WITWATERSRAND   (South Africa)

Author keywords

[No Author keywords available]

Indexed keywords

GLUTATHIONE TRANSFERASE; LIGANDIN; POLYPEPTIDE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME STABILITY; HUMAN; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FOLDING;

ACRYLAMIDE; ANILINO NAPHTHALENESULFONATES; BINDING SITES; ENZYME STABILITY; FLUORESCENT DYES; GLUTATHIONE TRANSFERASE; HUMANS; ISOENZYMES; KINETICS; LIGANDS; MUTAGENESIS, SITE-DIRECTED; PEPTIDE FRAGMENTS; PHENYLALANINE; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE DELETION; SPECTROMETRY, FLUORESCENCE; SULFOBROMOPHTHALEIN; TRYPTOPHAN;

EID: 0033598690     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi991179x     Document Type: Article

References (48)

1. Armstrong, R. N. (1997) Chem. Res. Toxicol. 10, 2-18.
2. Listowski, I. (1993) in Hepatic transport and bile secretion: physiology and pathophysiology (Tavoloni, N., and Berk, P., Eds.) pp 397-405, Raven Press, New York.
3. Mannervik, B., Alin, P., Guthenberg, C., Jenssen, H., Tahir, M. K., Warholm, M., and Jornvall, H. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 7202-7206.
4. Ji, X., von Rosenvinge, E. C. M., Johnson, W. W., Tomarev, S. I., Piatigorski, J., Armstrong, R. N., and Gilliland, G. L. (1995) Biochemistry 34, 5317-5328.
5. Meyer, D. J., Coles, B., Pemble, S. E., Gilmore, K. S., Fraser, G. M., and Ketterer, B. (1991) Biochem. J. 274, 409-414.
6. Pemble, S. E., Wardle, A. F., and Taylor, J. B. (1996) Biochem. J. 319, 749-754.
7. Dirr, H. W., Reinemer, P., and Huber, R. (1994) Eur. J. Biochem. 220, 645-661.
8. Wilce, M. C. J., and Parker, M. W. (1994) Biochim. Biophys. Acta 1205, 1-18.
9. Wallace, L. A., Sluis-Cremer, N., and Dirr, H. W. (1998) Biochemistry 37, 5320-5328.
10. Wallace, L. A., Blatch, G. L., and Dirr, H. W. (1998) Biochem. J. 336, 413-418.
11. Dirr, H. W., and Reinemer, P. (1991) Biochem. Biophys. Res. Commun. 180, 294-300.
12. Erhardt, J., and Dirr, H. W. (1995) Eur. J. Biochem. 230, 614-620.
13. Sluis-Cremer, N., and Dirr, H. (1995) FEBS Lett. 371, 94-98.
14. Sluis-Cremer, N., Naidoo, N., and Dirr, H. (1996) Eur. J. Biochem. 242, 301-307.
15. Stevens, J. M., Hornby, J. A. T., Armstrong, R. N., and Dirr, H. W. (1998) Biochemistry 37, 15534-15541.
16. Kaplan, W., Hüsler, P., Klump, H., Erhardt, J., Sluis-Cremer, N., and Dirr, H. W. (1997) Protein Sci. 6, 399-406.
17. Sinning, I., Kleywegt, G. J., Cowan, S. W., Reinemer, P., Dirr, H. W., Huber, R., Gilliland, G. L., Armstrong, R. N., Ji, X., Board, P. G., Olin, B., Mannervik, B., and Jones, T. A. (1993) J. Mol. Biol. 232, 192-212.
18. Cameron, A. D., Sinning, I., L'Hermite, G., Olin, B., Board, P. G., Mannervik, B., and Jones, T. A. (1995) Structure 3, 717-727.
19. Board, P. G., and Mannervik, B. (1991) Biochem. J. 275, 171-174.
20. Atkins, W. M., Dietze, E. C., and Ibarra, C. (1997) Protein Sci. 6, 873-881.
21. Lian, L.-Y., (1998) Cell. Mol. Life Sci. 54, 359-362.
22. McTique, M., Williams, D. R., and Tainer, J. A. (1995) J. Mol. Biol. 246, 21-27.
23. Ji, X., von Rosenvinge, E. C., Johnson, W. W., Armstrong, R. N., and Gilliland, G. L. (1996) Proc. Natl. Acad. Sci. U.S.A. 93, 8208-8213.
24. Sluis-Cremer, N., Naidoo, N. N., Kaplan, W. H., Manoharan, T. H., Fahl, W. E., and Dirr, H. W. (1996) Eur. J. Biochem. 241, 484-488.
25. Sluis-Cremer, N., Wallace, L., Burke, J., Stevens, J., and Dirr, H. (1998) Eur. J. Biochem. 257, 434-442.
26. Barycki, J. J. and Colman, R. F. (1997) Arch. Biochem. Biophys. 345, 16-31.
27. Stenberg, G., Bjornestedt, R., and Mannervik, B. (1992) Protein Expression Purif. 3, 80-84.
28. Weiner, M. P., Costa, G. L., Schoettlin, W., Cline, J., Mathur, E., and Bauer, J. C. (1994) Gene 151, 119-123.
29. Laemmli, U. K. (1970) Nature (London) 227, 680-685.
30. Perkins, S. J. (1986) Eur. J. Biochem. 157, 169-180.
31. Bico, P., Erhardt, J., Kaplan, W., and Dirr, H. (1995) Biochim. Biophys. Acta 1247, 225-230.
32. Tonomura, B., Nakatani, H., Ohnishi, M., Yamaguchi-Ito, J., and Hiromi, K. (1978) Anal. Biochem. 84, 370-383.
33. Lacroix, E., Viguera, A. R., and Serrano, L. (1998) J. Mol. Biol. 284, 173-191.
34. Johnson, W. C., Jr. (1990) Proteins: Struct. Funct. Gene. 7, 205-214.
35. Myers, J. K., Pace, C. N., and Scholz, J. M. (1995) Protein Sci. 4, 2138-2148.
36. Semisotnov, G. V., Rodionova, N. A., Kutyshenko, V. P., Ebert, B., Blank, J., and Ptitsyn, O. B. (1987) FEBS Lett. 224, 9-13.
37. Kumar, T. K. S., Jayaraman, G., Lin, W.-Y., and Yu, C. (1996) Biochim. Biophys. Acta 1294, 103-105.
38. Tanford, C. (1970) Adv. Protein Chem. 24, 1-95.
39. Widersten, M., Bjornestedt, R., and Mannervik, B. (1996) Biochemistry 35, 7731-7742.
40. Wang, R. W., Nweton, D. J., Johnson, A. R., Pickett, C. B., and Lu, A. Y. H. (1993) J. Biol. Chem. 268, 23981-23985.
41. Chakrabartty, A., and Baldwin, R. L. (1995) Adv. Protein Chem. 46, 141-176.
42. Erhardt, J., and Dirr, H. W. (1996) FEBS Lett. 391, 313-316.
43. McCarthy, R. M., Farmer, P., and Sheenan, D. (1996) Biochim. Biophys. Acta 1293, 185-190.
44. Ji, X., Tordova, M., O'Donnell, R., Parsons, J. F., Hayden, J. B., Gilliland, G. L., and Zimniak, P. (1997) Biochemistry 36, 9690-9702.
45. Prade, L., Huber, R., Manoharan, T. H., Fahl, W. E., and Reuter, W. (1997) Structure 5, 1287-1295.
46. Kraulis, P. J. (1991) J. Appl. Crystallogr. 24, 946-950.
47. Matulis, D., Baumann, C. G., Bloomfield, V. A., and Lovrien, R. E. (1999) Biopolymers 49, 451-458.
48. Nieslanik, B. S., Dabrowski, M. J., Lyon, R. P., and Atkins, W. M. (1999) Biochemistry 38, 6971-6980.