Identification of three key residues in substrate recognition site 5 of human cytochrome P450 3A4 by cassette and site-directed mutagenesis

Biochemistry

Volumn 36, Issue 29, 1997, Pages 8831-8839

  He, You Ai ^a   He, You Qun ^a   Szklarz, Grazyna D ^a   Halpert, James R ^a  

^a UNIVERSITY OF ARIZONA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ALPHA NAPHTHOFLAVONE; AMINO ACID; ARGININE; CYTOCHROME P450; HEME; ISOLEUCINE; LEUCINE; LYSINE; OXYGENASE; PROGESTERONE; STEROID; TESTOSTERONE; VALINE;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; ENZYME ACTIVITY; ENZYME SPECIFICITY; ESCHERICHIA COLI; GENE CASSETTE; IMMUNOBLOTTING; IMMUNOREACTIVITY; MODEL; MUTANT; NONHUMAN; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN TERTIARY STRUCTURE; SITE DIRECTED MUTAGENESIS; STEROID HYDROXYLATION;

AMINO ACID SEQUENCE; ARYL HYDROCARBON HYDROXYLASES; BASE SEQUENCE; BENZOFLAVONES; CYTOCHROME P-450 ENZYME SYSTEM; HUMANS; KINETICS; MIXED FUNCTION OXYGENASES; MODELS, CHEMICAL; MOLECULAR SEQUENCE DATA; MUTAGENESIS, INSERTIONAL; MUTAGENESIS, SITE-DIRECTED; PROGESTERONE; SEQUENCE ALIGNMENT; STEROID 16-ALPHA-HYDROXYLASE; TESTOSTERONE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; MAMMALIA; STAPHYLOCOCCUS PHAGE 3A;

EID: 0000227103     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi970182i     Document Type: Article

References (46)

1. Aoyama, T., Yamano, S., Waxman, D. J., Lapenson, D. P., Mayer, U. A., Fisher, V., Tyndale, R., Inaba, T., Kalow, W., Gelboin, H. V., & Gonzalez, F. J. (1989) J. Biol. Chem. 264, 10388-10395.
2. Ciaccio, P. J., & Halpert, J. R. (1989) Arch. Biochem. Biophys. 271, 284-299.
3. Cohen, S. N., Chang, A. C. Y., & Hsu, L. (1972) Proc. Natl. Acad. Sci. U.S.A. 69, 2110-2114.
4. Conley, E. C., & Saunders, J. R. (1984) Mol. Gen. Genet. 194, 211-218.
5. Cupp-Vickery, J. R., & Poulos, T. L. (1995) Struct. Biol. 2, 144-153.
6. Gillam, E. M., Baba, T., Kim, B. R., Ohmori, S., & Guengerich, F. P. (1993) Arch. Biochem. Biophys. 305, 123-131.
7. Gotoh, O. (1992) J. Biol. Chem. 267, 83-90.
8. Guengerich, F. P. (1990) Chem. Res. Toxicol. 3, 363-371.
9. Guengerich, F. P. (1995) in Cytochrome P450: Structure, Mechanism, and Biochemistry (Ortiz de Montellano, P. R., Ed.) pp 473-535, Plenum Press, New York.
10. Harlow, G. R., & Halpert, J. R. (1997) J. Biol. Chem. 272, 5396-5402.
11. Hasemann, C. A., Ravichandran, K. G., Peterson, J. A., & Deisenhofer, J. (1994) J. Mol. Biol. 236, 1169-1185.
12. Hasemann, C. A., Kurumbail, R. G., Boddupalli, S. S., Peterson, J. A., & Deisenhofer, J. (1995) Structure 3, 41-62.
13. Hasler, J. A., Harlow, G. R., Szklarz, G. D., John, G. H., Kedzie, K. M., Burnett, V. L., He, Y. A., Kaminsky, L. S., & Halpert, J. R. (1994) Mol. Pharmacol. 46, 338-345.
14. He, Y., Luo, Z., Klekotka, P. A., Burnett, V. L., & Halpert, J. R. (1994) Biochemistry 33, 4419-4424.
15. He, Y. Q., He, Y. A., & Halpert, J. R. (1995) Chem. Res. Toxicol. 8, 574-579.
16. He, Y. Q., Szklarz, G. D., & Halpert, J. R. (1996) Arch. Biochem. Biophys. 335, 152-160.
17. Hill, D. E., Oliphant, A. R., & Struhl, K. (1987) Methods Enzymol. 155, 558-568.
18. Hsu, M. H., Griffin, K. J., Wang, Y., Kemper, B., & Johnson, E. F. (1993) J. Biol. Chem. 268, 6939-6944.
19. Huang, M. T., Johnson, E. F., Muller-Eberhard, U., Koop, D. R., Coon, M. J., & Conney, A. H. (1981) J. Biol. Chem. 256, 10897-10901.
20. John, G. H., Hasler, J. A., He, Y. A., & Halpert, J. R. (1994) Arch. Biochem. Biophys. 309, 52-57.
21. Johnson, E. F. (1992) Trends Pharmacol. Sci. 13, 122-126.
22. Johnson, E. F., Schwab, G. E., & Vickery, L. E. (1988) J. Biol. Chem. 263, 17672-17677.
23. Kaminsky, L. S., de Morais, S. M. F., Faletto, M. B., Dunbar, D. A., & Goldstein, J. A. (1992) Mol. Pharmacol. 43, 234-239.
24. Kedzie, K. M., Balfour, C. A., Escobar, G. Y., Grimm, S. W., He, Y. A., Pepperl, D. J., Regan, J. W., Stevens, J. C., & Halpert, J. R. (1991) J. Biol. Chem. 266, 22515-22521.
25. Laemmli, U. K. (1970) Nature 227, 680-685.
26. Lewis, D. F. V., Eddershaw, P. J., Goldfarb, P. S., & Tarbit, M. H. (1996) Xenobiotica 26, 1067-1086.
27. Lindberg, R. L. P., & Negishi, M. (1989) Nature 339, 632-634.
28. Matsunaga, E., Zeugin, T., Zanger, U. M., Aoyama, T., Meyer, U. A., & Gonzalez, F. J. (1990) J. Biol. Chem. 265, 17197-17201.
29. Paulsen, M. D., & Ornstein, R. L. (1991) Proteins: Struct., Funct., Genet. 11, 184-204.
30. Paulsen, M. D., & Ornstein, R. L. (1992) J. Comput.-Aided Mol. Des. 6, 449-460.
31. Poulos, T. L. (1991) Methods Enzymol. 206, 11-30.
32. Poulos, T. L., Finzel, B. C., & Howard, A. J. (1987) J. Mol. Biol. 195, 687-700.
33. Ramarao, M. K., Straub, P., & Kemper, B. (1995) J. Biol. Chem. 270, 1873-1880.
34. Schwab, G. E., Raucy, J. L., & Johnson, E. F. (1988) Mol. Pharmacol. 33, 493-499.
35. Shimada, T., & Guengerich, F. P. (1989) Proc. Natl. Acad. Sci. U.S.A. 86, 462-465.
36. Shimada, T., Martin, M. V., Preuss-Schwartz, D., Marnett, L. D., & Guengerich, F. P. (1989) Cancer Res. 49, 6304-6312.
37. Shou, M., Grogan, J., Mancewicz, J. A., Krausz, K. W., Gonzalez, F. J., Gelboin, H. V., & Korzekwa, K. R. (1994) Biochemistry 33, 6450-6455.
38. Straub, P., Lloyd, M., Johnson, E. F., & Kemper, B. (1994) Biochemistry 33, 8029-8034.
39. Szklarz, G. D., & Halpert, J. R. (1997) J. Comp.-Aided Mol. Des. 11, 265-272.
40. Szklarz, G. D., He, Y. A., & Halpert, J. R. (1995) Biochemistry 34, 14312-14322.
41. Von Wachenfeldt, C., & Johnson, E. F. (1995) in Cytochrome P450: Structure, Mechanism, and Biochemistry (Ortiz de Montellano, P. R., Ed.) pp 183-223, Plenum Press, New York.
42. Wandel, C., Bocker, R., Bohrer, H., Browne, A., Rugheimer, E., & Martin, E. (1994) Br. J. Anaesth. 73, 658-661.
43. Waxman, D. J., Attisano, C., Guengerich, F. P., & Lapenson, D. P. (1988) Arch. Biochem. Biophys. 263, 424-436.
44. Waxman, D. J., Lapenson, D. P., Aoyama, T., Gelboin, H. V., Gonzalez, F. J., & Korzekwa, K. (1991) Arch. Biochem. Biophys. 290, 160-166.
45. Ueng, Y., Shimada, T., Yamazaki, H., & Guengerich, F. P. (1995) Chem. Res. Toxicol. 8, 218-225.
46. Ueng, Y.-F., Kuwabara, T., Chun, Y.-J., & Guengerich, F. P. (1997) Biochemistry 36, 370-381.