Chemical mechanism of the fructose-6-phosphate,2-kinase reaction from the pH dependence of kinetic parameters of site-directed mutants of active site basic residues

Biochemistry

Volumn 36, Issue 29, 1997, Pages 8775-8784

  Mizuguchi, Hiroyuki ^a   Cook, Paul F ^b   Hasemann, Charles A ^c   Uyeda, Kosaku ^a  

^a VA NORTH TEXAS HEALTH CARE SYSTEM   (United States)

^b UNIVERSITY OF OKLAHOMA   (United States)

^c UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

6 PHOSPHOFRUCTO 2 KINASE; ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE DERIVATIVE; ADENOSINE TRIPHOSPHATE MAGNESIUM; ALANINE; ARGININE; FRUCTOSE 2,6 BISPHOSPHATASE; FRUCTOSE 2,6 BISPHOSPHATE; FRUCTOSE 6 PHOSPHATE; LEUCINE; LYSINE; PHOSPHATE;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING KINETICS; DISSOCIATION CONSTANT; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SUBSTRATE; PH; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; STEADY STATE;

ADENOSINE TRIPHOSPHATE; ANIMALS; ANTHRANILIC ACIDS; BINDING SITES; CATALYSIS; HYDROGEN-ION CONCENTRATION; KINETICS; MALE; MODELS, CHEMICAL; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PHOSPHOFRUCTOKINASE-2; PHOSPHOTRANSFERASES (ALCOHOL GROUP ACCEPTOR); RATS; TESTIS;

EID: 0030837733     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi970639o     Document Type: Article

References (42)

1. Uyeda, K. (1991) in Enzyme Catalysis (Kurby, S. A., Ed.) Vol. II, pp 445-456, CRC Press, Boston.
2. Darville, M. I., Crepin, K. M., Vandekerckhove, J., van Damme, J., Octave, J. N., Rider, M. H., Marchand, M. J., Hue, L., and Rousseau, G. G. (1987) FEBS Lett. 224, 317-321.
3. Livery, M. O., El-Maghrabi, M. R., Pilkis, J., D'Angelo, G., Colosia, A. D., Ciavola, A. J., Fraser, B. A., and Pilkis, S. J. (1988) J. Biol. Chem. 263, 829-849.
4. Algaier, J., and Uyeda, K. (1988) Biochem. Biophys. Res. Commun. 153, 328-333.
5. Crepin, K. M., Darville, M. I., Michel, A., Hue, L., and Rousseau, G. G. (1989) Biochem. J. 264, 151-160.
6. Sakata, J., and Uyeda, K. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 4951-4955.
7. Sakata, J., Abe, Y., and Uyeda, K. (1991) J. Biol. Chem. 266, 15764-15770.
8. Watanabe, F., Sakai, A., Furuya, E., and Uyeda, K. (1994) Biochem. Biophys. Res. Commun. 198, 335-340.
9. Kitajima, S., Sakakibara, R., and Uyeda, K. (1984) J. Biol. Chem. 259, 6896-6903.
10. Kountz, P. D., Freeman, S., Cook, A. G., El-Maghrabi, M. R., Knowles, J. R., and Pilkis, S. J. (1988) J. Biol. Chem. 263, 16069-16072.
11. Istvan, E. S., Hasemann, C. A., Kurumbail, R. G., Uyeda, K., and Deisenhofer, J. (1995) Protein Sci. 4, 2439-2441.
12. Hasemann, C. A., Istavan, E. S., Uyeda, K., and Deisenhofer, J. (1996) Structure 4, 1017-1029.
13. Uyeda, K., Wang, X.-L., Mizuguchi, H., Li, Y., Cu, N., and Hasemann, C. A. (1997) J. Biol. Chem. 272, 7867-7872.
14. Müller, C. W., and Schultz, G. E. (1992) J. Mol. Biol. 224, 159-177.
15. Müller-Dickmann, H.-J., and Schultz, G. E. (1995) J. Mol. Biol. 246, 522-530.
16. Walker, J. E., Saraste, M., Runswick, M. J., and Gay, N. J. (1982) EMBO J. 1, 945-951.
17. Li, L., Liu, K., Kurland, I. J., Correia, J. J., and Pilkis, S. J. (1992) J. Biol. Chem. 267, 4386-4393.
18. Tsujikawa, T., Watanabe, F., and Uyeda, K. (1995) Biochemistry 34, 6389-6393.
19. Rider, M. H., Crepin, K. M., De Cloedt, M., Bertrand, L., Vertommen, D., and Hue, L. (1995) Biochem. J. 309, 341-346.
20. Kurland, I., Chapman, B., Lee, Y.-H., and Pilkis, S. (1995) Biochem. Biophys. Res. Commun. 213, 663-672.
21. Sakakibara, R., Kitajima, S., Hartman, F. C., and Uyeda, K. (1984) J. Biol. Chem. 259, 14023-14028.
22. Kitamura, K., Uyeda, K., Hartman, F. C., Kangawa, K., and Matsuo, H. (1989) J. Biol. Chem. 264, 6344-6348.
23. Hiratsuka, T. (1983) Biochim. Biophys. Acta 742, 496-508.
24. Hazlett, T. L., Moore, K. J. M., Lowe, P. N., Jameson, D. M., and Eccleston, J. F. (1993) Biochemistry 32, 13575-13583.
25. Uyeda, K., Miyatake, A., Luby, L. J., and Richards, E. G. (1978) J. Biol. Chem. 253, 8319-8327.
26. Tabor, S., and Richardson, C. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 1074-1078.
27. Kunkel, T. A. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 488-492.
28. Sanger, F., Nicklen, S., and Coulson, A. R. (1977) Proc. Natl. Acad. Sci. U.S.A. 74, 5463-5467.
29. Penefsky, H. S. (1977) J. Biol. Chem. 252, 2891-2899.
30. Tominaga, N., Minami, Y., Sakakibara, R., and Uyeda, K. (1993) J. Biol. Chem. 268, 15951-15957.
31. Furuya, E., and Uyeda, K. (1981) J. Biol. Chem. 256, 7109-7112.
32. Uyeda, K., Furuya, E., and Luby, L. J. (1981) J. Biol. Chem. 256, 8394-8399.
33. Ellis, K. J., and Morrison, J. F. (1982) Methods Enzymol. 87, 405-426.
34. Cleland, W. W. (1979) Methods Enzymol. 63, 103-139.
35. Bradford, M. M. (1976) Anal. Biochem. 72, 248-254.
36. Laemmli, U. K. (1970) Nature 227, 680-685.
37. Muegge, I., Schweins, T., Langen, R., and Warshel, A. (1996) Structure 4, 475-489.
38. Vertommen, D., Bertrand, L., Sontag, B., DiPietro, A., Louckx, M. P., Vidal, H., Hue, L., and Rider, M. H. (1996) J. Biol. Chem. 271, 17875-17880.
39. Cleland, W. W. (1977) Adv. Enzymol. Relat. Areas Mol. Biol. 45, 273-383.
40. Dawson, R. M. C., Elliot, D. C., Elliott, W. H., and Jones, K. M. (1969) Data for Biochemical Research, 2nd ed., Oxford University Press, London.
41. Coleman, D. E., Berghuis, A. M., Lee, E., Linder, M. E., Gilman, A. G., and Sprang, S. R. (1994) Science 265, 1405-1412.
42. Maegley, K. A., Admiraal, S. J., and Herschlag, D. (1996) Proc. Natl. Acad. Sci. U.S.A. 93, 8160-8166.