The Nature of the Transition State for Enzyme-Catalyzed Phosphoryl Transfer. Hydrolysis of O-Aryl Phosphorothioates by Alkaline Phosphatase

Biochemistry

Volumn 34, Issue 38, 1995, Pages 12255-12264

  Hollfelder, Florian ^a   Herschlag, Daniel ^a  

^a STANFORD UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; PHOSPHOROTHIOIC ACID;

ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME SPECIFICITY; ESCHERICHIA COLI; NONHUMAN; PHOSPHATE METABOLISM; PRIORITY JOURNAL;

ALKALINE PHOSPHATASE; ANILINE COMPOUNDS; BINDING SITES; CATALYSIS; COMPARATIVE STUDY; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; MODELS, CHEMICAL; ORGANOPHOSPHORUS COMPOUNDS; PHENOLS; PHOSPHORYLATION; SUPPORT, NON-U.S. GOV'T; THIOPHOSPHORIC ACID ESTERS; VISCOSITY;

ESCHERICHIA COLI; FELIS CATUS;

EID: 0029117035     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi00038a021     Document Type: Article

References (72)

1. Aimer, H., & Stromberg, R. (1991) Nucleosides Nucleotides 10, 653-656.
2. Applebury, M. L., Johnson, B. P., & Coleman, J. E. (1970) J. Biol. Chem. 245, 4968-4976.
3. Bale, J. R., Huang, C. Y., & Chock, P. B. (1980) J. Biol. Chem. 255, 8431-8436.
4. Barnard, P. W. C., Bunton, C. A., Llewellyn, D. R., Oldham, K. G., Silver, B. L., & Vernon, C. A. (1955) Chem. Ind. (London), 760-763.
5. Ba-Saif, S., & Williams, A. (1988) J. Org. Chem. 53, 2204.
6. Ba-Saif, S. A., Davis, A. M., & Williams, A. (1989) J. Org. Chem. 54, 5483-5486.
7. Baumler, J., & Rippstein, S. (1961) Helv. Chim. Acta 44, 1162-1164.
8. Benkovic, S. J., & Schray, K. J. (1973) Chemical Basis of Biological Phosphoryl Transfer. In The Enzymes, pp 201-238, Academic Press, New York.
9. Benkovic, S. J., & Schray, K. J. (1978) The Mechanism of Phosphoryl Transfer. In Transition States of Biochemical Processes, pp 493-528, Plenum Press, New York.
10. Bloch, W., & Schlesinger, M. J. (1973) J. Biol. Chem. 248, 5794-5805.
11. Bourne, N., & Williams, A. (1984a) J. Org. Chem. 49, 1200-1204.
12. Bourne, N., & Williams, A. (1984b) J. Am. Chem. Soc. 106, 7591-7596.
13. Breslow, R., & Katz, I. (1968) J. Am. Chem. Soc. 90, 7376-7377.
14. Brouwner, A. C., & Kirsch, J. F. (1982) Biochemistry 21, 1302-1307
15. Butcher, W. W., & Westheimer, F. H. (1955) J. Am. Chem. Soc. 77, 2420-2424.
16. Butler-Ransohoff, J. E., Kendall, D. A., & Kaiser, E. T. (1988) Proc. Natl. Acad. Sci. U.S.A. 85, 4276-4278. Butler-Ransohoff, J. E., Rokita, S. E., Kendall, D. A., Banzon, J. A., Carano, K. S., Kaiser, E. T., & Matlin, A. R. (1992) J. Org. Chem. 57, 142-145.
17. Chlebowski, J. F., & Coleman, J. E. (1974) J. Biol. Chem. 249, 7192-7202.
18. Cox, J. R., Jr., & Ramsey, O. B. (1964) Chem. Rev. 64, 317-351.
19. Davis, A. M., Regan, A. C., & Williams, A. (1988) Biochemistry 27, 9042-9047.
20. Domanico, P., Mizrahi, V., & Benkovic, S. J. (1986) Observations on the Chemistry of Phosphorothioate Transfer. In Mechanisms of Enzymatic Reactions: Stereochemistry, pp 127-138, Elsevier, Amsterdam.
21. Fanni, T., Taira, K., Gorenstein, D. G., Vaidyanathaswany, R., & Verkade, J. G. (1986) J. Am. Chem. Soc. 108, 6311-6314.
22. Garen, A., & Levinthal, C. (1960) Biochim. Biophys. Acta 38, 470-483.
23. Hall, A. D., & Williams, A. (1986) Biochemistry 25, 4784-4791.
24. Han, R., & Coleman, J. E. (1995) Biochemistry 34, 4238-4245.
25. Hardy, L. W., & Kirsch, J. F. (1984) Biochemistry 23, 1275-1282.
26. Hassett, A., Blattler, W., & Knowles, J. R. (1982) Biochemistry 21, 6335-6339.
27. Heath, D. F. (1956a) J. Chem. Soc., 3796-3804.
28. Heath, D. F. (1956b) J. Chem. Soc., 3804-3809.
29. Hengge, A. C., Edens, W. A., & Elsing, H. (1994) J. Am. Chem. Soc. 116, 5045-5049.
30. Herschlag, D. (1994) J. Am. Chem. Soc. 116, 11631-11635.
31. Herschlag, D., & Jencks, W. P. (1987) J. Am. Chem. Soc. 109, 4665-4674.
32. Herschlag, D., & Jencks, W. P. (1989a) J Am. Chem. Soc. 111, 7579-7586.
33. Herschlag, D., & Jencks, W. P. (1989b) J. Am. Chem. Soc. 111, 7587-7596.
34. Herschlag, D., & Jencks, W. P. (1990) Biochemistry 29, 5172-5179.
35. Herschlag, D., Piccirilli, J. A., & Cech, T. R. (1991) Biochemistry 30, 4844-4854.
36. Horn, H., & Ahlrichs, R. (1990) J. Am. Chem. Soc. 112, 2121-2124.
37. Huang, Z., Wagner, C. R., & Benkovic, S. J. (1994) Biochemistry 33, 11576-11585.
38. Jencks, W. P. (1975) Adv. Enzymol. 43, 219-410.
39. Jencks, W. P. (1987) Catalysis in Chemistry and Enzymology, Dover, New York.
40. Jencks, W. P., & Regenstein, J. (1976) Ionization Constants of Acids and Bases. In Handbook of Biochemistry and Molecular Biology, pp 305-351, CRC Press, Cleveland.
41. Ketelaar, J. A. A., Gersmann, H. R., & Koopsmans, K. (1952) Recl. Trav. Chim. 71, 1253-1258.
42. Khan, S. A., & Kirby, A. J. (1970) J. Chem. Soc. B. 1172-1182.
43. Kim, E. E., & Wyckoff, H. W. (1991) J. Mol. Biol. 218, 449-464.
44. Kirby, A. J., & Jencks, W. P. (1965) J. Am. Chem. Soc. 87, 3209-3216.
45. Kirby, A. J., & Varvoglis, A. G. (1967) J. Am. Chem. Soc. 89, 415-423.
46. Kirsch, J. F. (1972) Linear Free Energy Relationships in Enzymology. In Advances in Linear Free Energy Relationships, pp 369-400, Plenum, New York.
47. Knowles, J. R. (1980) Annu. Rev. Biochem. 49, 877-919.
48. Kumamoto, J., & Westheimer, F. H. (1955) J. Am. Chem. Soc. 77, 2515-2518.
49. Labow, B. I., Herschlag, D., & Jencks, W. P. (1993) Biochemistry 32, 8737-8741.
50. Lienhard, G. E. (1973) Science 180, 149-154.
51. Lowry, T. H., & Richardson, K. S. (1981) Mechanism and Theory in Organic Chemistry, Harper & Row, New York.
52. Martin, B., Pallen, C. J., Wang, J. H., & Graves, D. J. (1985) J. Biol. Chem. 260, 14932-14937.
53. Mildvan, A. S., & Fry, D. C. (1987) Adv. Enzymol. 59, 241-313.
54. Mushak, P., & Coleman, J. E. (1972) Biochemistry 11, 202-205.
55. Nath, R. L., & Rydon, H. N. (1954) Biochem. J. 57, 1-10.
56. Rajca, A., Rice, J., Streitweiser, A., & Schaefer, H. (1987) J. Am. Chem. Soc. 109, 4189-4192.
57. Reid, T. W., & Wilson, I. B. (1971a) Biochemistry 10, 380-387.
58. Reid, T. W., & Wilson, I. B. (1971b) E. coli Alkaline Phosphatase. In The Enzymes, Vol. 4, pp 373-415, Academic Press, New York.
59. Seiler, H. (1961) Helv. Chim. Acta 44, 1753-1755.
60. Simopoulos, T. T., & Jencks, W. P. (1994) Biochemistry 33, 10375-10380.
61. Skoog, M. T., & Jencks, W. P. (1984) J. Am. Chem. Soc. 106, 7597-7606.
62. Snyder, S. L., & Wilson, I. B. (1972) Biochemistry 11, 3220-3223.
63. Sowadski, J. M., Handschumacher, M. D., Krishna Murthy, H. M., Foster, B. A., & Wyckoff, H. W. (1985) J. Mol. Biol. 186, 417-433.
64. Steitz, T. A., & Steitz, J. A. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 6498-6502.
65. Thatcher, G. R. J., & Kluger, R. (1989) Adv. Phys. Org. Chem. 25, 99-265.
66. Tolkmith, H. (1958) J. Org. Chem. 23, 1685-1690.
67. Toney, M. D., & Kirsch, J. F. (1989) Science 243, 1485-1488.
68. Tull, D., & Withers, S. G. (1994) Biochemistry 33, 6363-6370.
69. Williams, A. (1992) Adv. Phys. Org. Chem. 27, 1-55.
70. Williams, A., & Naylor, R. A. (1971) J. Chem. Soc. B. 1973-1979.
71. Wolfenden, R. (1972) Acc. Chem. Res. 5, 10-18.
72. Zhang, Z.-Y., & Van Etten, R. (1991) Biochemistry 30, 8954-8959.