Transition state structure of arginine kinase: Implications for catalysis of bimolecular reactions

Proceedings of the National Academy of Sciences of the United States of America

Volumn 95, Issue 15, 1998, Pages 8449-8454

  Zhou, Genfa ^a   Somasundaram, Thayumanasamy ^a   Blanc, Eric ^a   Parthasarathy, Golapakrishnan ^a   Ellington, W Ross ^a   Chapman, Michael S ^a  

^a FLORIDA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ARGININE KINASE; CREATINE KINASE;

ACID BASE BALANCE; CATALYSIS; CONFERENCE PAPER; CRYSTALLOGRAPHY; ENERGY EXPENDITURE; ENZYME ACTIVE SITE; ENZYME KINETICS; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE; POLARIZATION; PRIORITY JOURNAL; STRUCTURE ANALYSIS;

EID: 0032555162     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.95.15.8449     Document Type: Article

References (54)

1. Fersht, A. (1985) Enzyme Structure and Function (Freeman, New York).
2. Page, M. I. & Jencks, W. P. (1971) Proc. Natl. Acad. Sci. USA 68, 1678-1683.
3. Storm, D. R. & Koshland, D. E., Jr. (1970) Proc. Natl. Acad Sci. USA 66, 445-452.
4. Dafforn, A. & Koshland, D. E., Jr. (1971) Proc. Natl. Acad. Sci. USA 68, 2463-2467.
5. Mesecar, A. D., Stoddard, B. L. & Koshland, D. E., Jr. (1997) Science 277, 202-206.
6. Kantrowitz, E. R. & Lipscomb, W. N. (1988) Science 241, 669-674.
7. Schneider, G., Lindqvist, Y. & Brändén, C.-I. (1992) Annu. Rev. Biophys. Biomol. Struct. 21, 119-143.
8. Gouaux, J. E. & Lipscomb, J. E. (1988) Proc. Natl. Acad. Sci. USA 85, 4205-4208.
9. Karpusas, M., Branchaud, B. & Remmington, S. J. (1990) Biochemistry 29, 2213-2219.
10. Bolduc, J. M., Dyer, D. H., Scott, W. G., Singer, P., Sweet, R. M., Koshland, D. E. & Stoddard, B. L. (1995) Science 268, 1312-1318.
11. Hansen, D. E. & Knowles, J. R. (1981) J. Biol. Chem. 256, 5967-5969.
12. Milner-White, E. J. & Watts, D. C. (1971) Biochem. J. 122, 727-740.
13. McLaughlin, A. C. & Cohn, M. (1972) J. Biol. Chem. 247, 4382-4388.
14. McGilvery, R. W. (1979) Biochemistry, A Functional Approach (Saunders, Philadelphia).
15. Stroud, R. M. (1996) Nat. Struct. Biol. 3, 567-569.
16. Fritz-Wolf, K., Schnyder, T., Wallimann, T. & Kabsch, W. (1996) Nature (London) 381, 341-345.
17. Cook, P. F., Kenyon, G. L. & Cleland, W. W. (1981) Biochemistry 20, 1204-1210.
18. Vasák, M., Nagayamne, K., Wüthrich, K., Mertens, M. L. & Kägi, J. H. R. (1979) Biochemistry 18, 5050-5055.
19. Reed, G. H. & Cohn, M. (1972) J. Biol. Chem. 247, 3073-3081.
20. Forstner, M., Kriechbaum, M., Laggner, M. P. & Wallimann, T. (1996) J. Mol. Struct. 383, 217-227.
21. Zhou, G., Parthasarathy, G., Somasundaram, T., Ables, A., Roy, L., Strong, S. J., Ellington, W. R. & Chapman, M. S. (1997) Protein Sci. 6, 444-449.
22. Strong, S. J. & Ellington, W. R. (1996) Comp. Biochem. Physiol. B 113, 809-816.
23. Navaza, J. & Saludjian, P. (1997) Methods Enzymol. 277, 581-594.
24. Brünger, A. T. (1997) Methods Enzymol. 276, 558-580.
25. Cowtan, K. D. & Main, P. (1993) Acta Crystallogr. D 49, 148-157.
26. Kleywegt, G. J. & Jones, T. A. (1997) Methods Enzymol. 277, 208-230.
27. Brünger, A. T. (1997) Methods Enzymol. 277, 366-396.
28. Chapman, M. S. (1995) Acta Crystallogr. A 51, 69-80.
29. Chapman, M. S. & Blanc, E. (1997) Acta Crystallogr. D 53, 203-206.
30. Brünger, A. T. (1992) X-PLOR Version 3.1: A System for X-ray Crystallography and NMR (Yale Univ. Press, New Haven, CT).
31. Bhat, T. N. (1988) J. Appl. Crystallogr. 21, 279-281 .
32. Buchwald, S. L., Friedman, J. M. & Knowles, J. R. (1984) J. Am. Chem. Soc. 106, 4911-4916.
33. Skoog, M. T. & Jencks, W. P. (1984) J. Am. Chem. Soc. 106, 7597-7606.
34. Murali, N., Joaori, G. K. & Rao, B. D. N. (1994) Biochemistry 33, 14227-14236.
35. Leyh, T. S., Goodhart, P. J., Nguyen, A. C., Kenyon, G. L. & Reed, G. H. (1985) Biochemistry 24, 308-316.
36. Cohn, M., Shih, N. & Nick, J. (1982) J. Biol. Chem. 257, 7646-7649.
37. Almassy, R. J., Janson, C. A., Hamlin, R., Xuong, N.-H. & Eisenberg, D. S. (1986) Nature (London) 323, 304-309.
38. Kabsch, W. & Fritz-Wolf, K. (1997) Curr. Opin. Struct. Biol. 7, 811-818.
39. Bennett, W. S. Jr., & Steitz, T. A. (1978) Proc. Natl. Acad. Sci. USA 75, 4848-4852.
40. Dumas, C. & Camonis, J. (1993) J. Biol. Chem. 268, 21599-21606.
41. Strong, S. J. & Ellington, W. R. (1995) Biochim. Biophys. Acta 1246, 197-200.
42. Suzuki, T., Kawasaki, Y., Furukohri, T. & Ellington, W. R. (1997) Biochim. Biophys. Acta 1343, 152-159.
43. Fersht, A. R., Blow, D. M. & Fastrez, J. (1973) Biochemistry 12, 2035-2041.
44. Robertus, J. D., Kraut, J., Alden, R. A. & Birktoft, J. J. (1972) Biochemistry 11, 4293-4303.
45. Rosevear, P. R., Desmeules, P., Kenyon, G. L. & Mildvan, A. S. (1981) Biochemistry 20, 6155-6164.
46. Chen, L. H., Borders, C. L., Jr., Vásquez, J. R. & Kenyon, G. L. (1996) Biochemistry 35, 7895-7902.
47. Dunn, B. M., Di Bello, C. & Anfinsen, C. B. (1973) J. Biol. Chem. 248, 4769-4774.
48. Cotton, F. A., Hazen, E. E. & Legg, M. J. (1979) Proc. Natl. Acad. Sci. USA 76, 2551-2555.
49. Kyte, J. (1995) Mechanism in Protein Chemistry (Garland, New York).
50. Virden, R. & Watts, D. C. (1966) Biochem. J. 99, 162-172.
51. Watts, D. C. & Rabin, B. R. (1962) Biochem. J. 85, 507-516.
52. Wu, H., Yao, Q.-Z. & Tsou, C.-L. (1989) Biochim. Biophys. Acta 997, 78-82.
53. Lin, L., Perrymann, M. B., Friedman, D., Roberts, R. & Ma, T. S. (1994) Biochim. Biophys. Acta 1206, 97-104.
54. Furter, R., Furter-Graves, E. M. & Wallimann, T. (1993) Biochemistry 32, 7022-7029.