Eight Histidine Residues Are Catalytically Essential in a Membrane-Associated Iron Enzyme, Stearoyl-CoA Desaturase, and Are Conserved in Alkane Hydroxylase and Xylene Monooxygenase

Biochemistry

Volumn 33, Issue 43, 1994, Pages 12787-12794

  Shanklin, John ^a   Whittle, Edward ^a   Fox, Brian G ^b  

^a BROOKHAVEN NATIONAL LABORATORY   (United States)

^b UNIVERSITY OF WISCONSIN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACYL COENZYME A DESATURASE; ALKANE; BACTERIAL ENZYME; HISTIDINE; HYDROCARBON; IRON; MEMBRANE ENZYME; OXYGENASE; UNSPECIFIC MONOOXYGENASE; XYLENE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CYANOBACTERIUM; ENZYME STRUCTURE; GENE EXPRESSION; GENETIC COMPLEMENTATION; IMMUNOBLOTTING; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; RAT; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; YEAST;

AMINO ACID SEQUENCE; ANIMAL; BASE SEQUENCE; CATALYSIS; CONSERVED SEQUENCE; CYTOCHROME P-450 ENZYME SYSTEM; GENETIC COMPLEMENTATION TEST; HISTIDINE; LIVER; MIXED FUNCTION OXYGENASES; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OXYGENASES; PHYLOGENY; PSEUDOMONAS; RATS; SACCHAROMYCES CEREVISIAE; STEAROYL-COA DESATURASE; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, NON-P.H.S.;

BACTERIA (MICROORGANISMS); CYANOBACTERIA; EMBRYOPHYTA; EUKARYOTA; FUNGI; HEXAPODA; MAMMALIA;

EID: 0028089687     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi00209a009     Document Type: Article

References (45)

1. Arnold, F. H., & Haymore, B. L. (1991) Science 252, 1796.
2. Arondel, V., Lemieux, B., Hwang, I., Gibson, S., Goodman, H. M., & Somerville, C. R. (1992) Science 258, 1353.
3. Cahoon, E. B., Shanklin, J., & Ohlrogge, J. B. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 11184.
4. Felsenstein, J. (1989) Cladistics 5, 164
5. Fox, B. G., Shanklin, J., Somerville, C., & Münck, E. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 2486
6. Fox, B. G., Shanklin, J., Ai, J., Loehr, T. M., & Sanders-Loehr, J. (1994) Biochemistry (preceding paper in this issue)
7. Fulco, A. J. (1974) Annu. Rev. Biochem. 43, 215
8. Holloway, P. W. (1983) in The Enzymes (Boyer, P. D., Ed.) 3rd ed., Vol. 16, pp 63-83, Academic Press, New York
9. Holmes, M. A., Le Trong, I., Turley, S., Sieker, L. C., & Stenkamp, R. E. (1991) J. Mol. Biol. 218, 583
10. Iba, K., Gibson, S., Nishiuchi, T., Fues, T., Nishimura, M., Arnodel, V., Hughly, S., & Somerville, C. (1993) J. Biol. Chem. 268, 24099.
11. Jaworski, J. G., & Stumpf, P. K. (1974) Arch. Biochem. Biophys. 162, 158.
12. Kok, M., Oldenhuis, R., van der Linden, M. P. G., Ratjees, P., Kingma, J., van Lelyveld, P. H., & Witholt, B. (1989) J. Biol. Chem. 264, 5435
13. Kyte, J., & Doolittle, R. F. (1982) J. Mol. Biol. 157, 105.
14. Laemmli, U. K. (1970) Nature 227, 680.
15. Luo, C. (1993) Ph.D. Thesis, Oklahoma State University
16. Maniatis, T., Fritsch, E. F., & Sambrook, J. (1982) Molecular Cloning, A Laboratory Manual, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
17. Morris, L. J. (1970) Biochem. J. 118, 681
18. Nagai, J., & Bloch, K. (1968) J. Biol. Chem. 243, 4626
19. Needleman, S., & Wunsch, C. (1970) J. Mol. Biol. 48, 443
20. Nordlund, P., & Eklund, H. (1993) J. Mol. Biol. 232, 123
21. Ntambi, J., Buhrow, S. A., Kaestner, K. H., Christy, R. J., Sibley, E., Kelly, T. J., Jr., & Lane, M. D. (1988) J. Biol. Chem. 263, 17291.
22. Okuley, J., Lightner, J., Feldman, K. A., Yadav, N. S., Lark, E., & Browse, J. (1994) Plant Cell 6, 147
23. Pearson, W. R., & Lipman, D. J. (1988) Proc. Natl. Acad. Sci. U.S.A. 85, 2444
24. Peterson, J. A., & Coon, M. J. (1968) J. Biol. Chem. 243, 329
25. Reddy, A. S., Nuccio, M. L., Gross, L. M., & Thomas, T. L. (1993) Plant Mol. Biol. 22, 293
26. Regan, L. (1993) Annu. Rev. Biophys. Biomol. Struct. 22, 257
27. Rosenzweig, A. C., Frederick, C. A., Lippard, S. J., & Nordlund, P. (1993) Nature 366, 537
28. Sanders-Loehr, J. (1988) Prog. Clin. Biol. Res. 274, 193.
29. Sanders-Loehr, J. (1989) in Iron Carriers and Iron Proteins (Loehr, T. M., Ed.) pp 375-466, VCH Publishers, New York
30. Sanger, F., Nicklen, S., & Coulson, A. R. (1977) Proc. Natl. Acad. Sci. U.S.A. 74, 5463
31. Schroepfer, G. J., Jr., & Bloch, K. (1965) J. Biol. Chem. 240, 54.
32. Shanklin, J., & Somerville, C. (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 2510
33. Shapleigh, J. P., Hosler, J. P., Tecklenburg, M. M. J., Kim, Y., Babcock, G. T., Gennis, R. B., & Ferguson-Miller, S. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 4786
34. Strittmatter, P., Spatz, L., Corcoran, D., Rogers, M. J., Setlow, B., & Redline, R. (1974) Proc. Natl. Acad. Sci. U.S.A. 71, 4565
35. Stukey, J. E., McDonough, V. M., & Martin, C. E. (1989) J. Biol. Chem. 265, 16537.
36. Stukey, J. E., McDonough, V. M., & Martin, C. E. (1990) J. Biol. Chem. 266, 20144
37. Suzuki, M., Hayakawa, T., Shaw, J. P., Rekik, M., & Harayama, S. (1991) J. Bacteriol. 173, 1690
38. Thiede, M. A., Ozols, J., & Strittmatter, P. (1986) J. Biol. Chem. 261, 13230.
39. Thompson, G. A., Scherer, D. E., Foxall-Van Aken, S., Kenny, J. W., Young, H. L., Shintani, D. K., Kridl, J. C., & Knauf, V. C. (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 2578
40. Towbin, H. T., Staehelin, T., & Gordon, J. (1979) Proc. Natl. Acad. Sci. U.S.A. 76, 4350
41. van Beilen, J. B., Penninga, D., & Witholt, B. (1992) J. Biol. Chem. 267, 9194
42. Volbeda, A., & Hol, W. G. J. (1989) J. Mol. Biol. 206, 531
43. Wada, H., Gombos, Z., & Murata, H. (1990) Nature 347, 200
44. Wada, H., Schmidt, H., Heinz, E., & Murata, N. (1993) J. Bacteriol. 175, 544
45. Yadav, N. S., Wierzbicki, A., Aegerter, M., Caster, C. S., Pérez-Grau, L., Kinney, A. J., Hitz, W. D., Booth, R., Jr., Schweiger, B., Stecca, K. L., Allen, S. M., Blackwell, M., Reiter, R. S., Carlson, T. J., Russell, S. H., Feldmann, K. A., Pierce, J., & Browse, J. (1993) Plant Physiol. 103, 467