Probing the nucleotide-binding site of Escherichia coli succinyl-CoA synthetase

Biochemistry

Volumn 38, Issue 22, 1999, Pages 7273-7283

  Joyce, Michael A ^a   Fraser, Marie E ^a   Brownie, Edward R ^a   James, Michael N G ^a   Bridger, William A ^b   Wolodko, William T ^a  

^a UNIVERSITY OF ALBERTA   (Canada)

^b UNIVERSITY OF WESTERN ONTARIO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; HISTIDINE; MUTANT PROTEIN; NUCLEOTIDE; PURINE NUCLEOSIDE; PYROPHOSPHATE; SUCCINIC ACID; SUCCINYL COENZYME A SYNTHETASE;

AMINO TERMINAL SEQUENCE; ARTICLE; BETA CHAIN; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME BINDING; ESCHERICHIA COLI; NONHUMAN; PHOTOAFFINITY LABELING; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; AZIDES; BINDING SITES; CONSERVED SEQUENCE; ENZYME ACTIVATION; ESCHERICHIA COLI; GUANOSINE TRIPHOSPHATE; MASS SPECTROMETRY; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PEPTIDE FRAGMENTS; PHOSPHORYLATION; PHOTOAFFINITY LABELS; PURINE NUCLEOTIDES; SUBSTRATE SPECIFICITY; SUCCINATE-COA LIGASES;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0033151780     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi990527s     Document Type: Article

References (48)

1. Bridger, W. A. (1974) in The Enzymes (Boyer, P. D., Ed.) 3rd ed., Vol. X, pp 581-606, Academic Press, New York.
2. Nishimura, J. S. (1986) in Advances in Enzymology (Meister, A., Ed.) Vol. 58, pp 141-172, Wiley, New York.
3. Ottaway, J. H., McClellan, J. A., and Saunderson, C. L. (1981) Int. J. Biochem. 13, 401-410.
4. Labbe, R. F., Kurumada, T., and Onisawa, J. (1965) Biochim. Biophys. Acta 3, 403-415.
5. Murakami, K., Mitchell, T., and Nishimura, J. S. (1972) J. Biol. Chem. 247, 6247-6252.
6. McClellan, J. A., and Ottaway, J. H. (1980) Comp. Biochem. Physiol. 67B, 679-684.
7. Hamilton, M. L., and Ottaway, J. H. (1981) FEBS Lett. 123, 252-254.
8. Jenkins, T. M., and Weitzman, P. D. J. (1988) FEBS Lett. 230, 6-8.
9. Bailey, D. L., Wolodko, W. T., and Bridger, W. A. (1993) Protein Sci. 2, 1255-1262.
10. Johnson, J. D., Mehus, J. G., Tews, K., Milavetz, B. I., and Lambeth, D. O. (1998) J. Biol. Chem. 273, 27580-27586.
11. Johnson, J. D., Muhonen, W. W., and Lambeth, D. O. (1998) J. Biol. Chem. 273, 27573-27579.
12. Lynn, R., and Guynn, R. W. (1978) J. Biol. Chem. 253, 2546-2553.
13. Jenkins, T. M., and Weitzman, P. D. J. (1986) FEBS Lett. 205, 215-218.
14. Pearson, P. H., and Bridger, W. A. (1975) J. Biol. Chem. 250, 8524-8529.
15. Wolodko, W. T., Fraser, M. E., James, M. N. G., and Bridger, W. A. (1994) J. Biol. Chem. 269, 10883-10890.
16. Murzin, A. G. (1996) Curr. Opin. Struct. Biol. 6, 386-394.
17. Fraser, M. E., James, M. N. G., Bridger, W. A., and Wolodko, W. T. (1999) J. Mol. Biol. 285, 1633-1653.
18. Kraulis, P. J. (1991) J. Appl. Crystallogr. 24, 946-950.
19. Collier, G. E., and Nishimura, J. S. (1978) J. Biol. Chem. 253, 4938-4943.
20. Mann, C. J., Hardies, S. C., and Nishimura, J. S. (1989) J. Biol. Chem. 264, 1457-1460.
21. Hara, T., Kato, H., Katsube, Y., and Oda, J. (1996) Biochemistry 35, 11967-11974.
22. Fan, C., Moews, P. C., Walsh, C. T., and Knox, J. R. (1994) Science 266, 439-443.
23. Wolodko, W. T., Kay, C. M., and Bridger, W. A. (1986) Biochemistry 25, 5420-5425.
24. Laemmli, U. K. (1970) Nature 227, 680.
25. Stanislawski, J. (1991) ENZYME KINETICS, version 1.11, Vol. 63, Trinity Software, Campton, NH.
26. Bridger, W. A., Ramaley, R. F., and Boyer, P. D. (1969) Methods Enzymol. 13, 70-75.
27. Norby, J., Rubenstein, S., Tuerke, T., Schwallie Farmer, C., Forood, R., and Bennington, J. (1993) SIGMA PLOT, version 4.11, Jandel Scientific, San Rafael, CA.
28. Hill, A. V. (1910) J. Physiol. 40, 4-7.
29. Jayaram, B., and Haley, B. E. (1994) J. Biol. Chem. 269, 3233-3242.
30. Ho, S. N., Hunt, H. D., Horton, R. N., Pullen, J. K., and Pease, L. R. (1989) Gene 77, 51-59.
31. Buck, D., and Guest, J. R. (1989) Biochem. J. 260, 737-747.
32. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989) Molecular Cloning: a laboratory manual, 2nd ed., Cold Spring Harbor Laboratory Press, Plainview, NY.
33. Davis, D. G., Dibner, M. D., and Battey, J. F. (1986) Basic Methods in Molecular Biology, 1st ed., Elsevier Science Publishing Co., Inc., New York.
34. Froehlich, B., and Epstein, W. (1981) J. Bacteriol. 147, 1117-1120.
35. Krebs, A., and Bridger, W. A. (1974) Can. J. Biochem. 52, 594-598.
36. Potter, R. L., and Haley, B. E. (1983) Methods Enzymol. 91, 613-633.
37. Moffet, F. J., Wang, T., and Bridger, W. A. (1972) J. Biol. Chem. 247, 8139-8144.
38. Buck, D., Spencer, M. E., and Guest, J. R. (1985) Biochemistry 24, 6245-6252.
39. Liang, T., and Schuster, G. B. (1987) J. Am. Chem. Soc. 109, 7803-7810.
40. King, S. M., Kim, H., and Haley, B. E. (1991) Methods Enzymol. 196, 449-466.
41. Vogel, H. J., and Bridger, W. A. (1983) Biochem. Soc. Trans. 11, 315-323.
42. Moffet, F. J., and Bridger, W. A. (1970) J. Biol. Chem. 245, 2758-2762.
43. Sweeny, J. R., and Fisher, J. R. (1968) Biochemistry 7, 561-565.
44. Westley, J. (1969) in Enzymic Catalysis (Halvorson, H. O., Roman, H. L., and Bell, E., Eds.) 1st ed., Harper and Row, New York.
45. Moffet, F. J., and Bridger, W. A. (1973) Can. J. Biochem. 51, 44-55.
46. Tavale, S. S., and Sobel, H. M. (1970) J. Mol. Biol. 48, 109-123.
47. Ikehara, M., Uesugi, S., and Yoshida, K. (1972) Biochemistry 11, 830-836.
48. Ikehara, M., Uesugi, S., and Yoshida, K. (1972) Biochemistry 11, 836-842.