Involvement of a tyrosine residue in the ADP binding site of creatine kinase. A second-derivative UV-spectroscopy study

Biochemistry and Molecular Biology International

Volumn 41, Issue 4, 1997, Pages 777-784

  Leydier, Chantal ^a   Clottes, Eric ^a   Couthon, Fabienne ^a   Marcillat, Olivier ^a   Vial, Christian ^a  

^a Biomembranes et Enzymes Associes   (France)

Author keywords

Active site; MgADP binding site; MM creatine kinase; Second derivative spectroscopy; Tyrosine residue

Indexed keywords

ADENOSINE DIPHOSPHATE; CREATINE; CREATINE KINASE; MAGNESIUM ION; MITOCHONDRIAL ENZYME; SOLVENT; TYROSINE;

ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DISSOCIATION CONSTANT; ENZYME SUBSTRATE COMPLEX; MICHAELIS CONSTANT; MUSCLE MITOCHONDRION; NONHUMAN; RABBIT; ULTRAVIOLET SPECTROSCOPY;

EID: 0030995251     PISSN: 10399712     EISSN: None     Source Type: Journal    
DOI: 10.1080/15216549700201811     Document Type: Article

References (32)

1. Mahowald, T.A., Noltmann, E.A. and Kuby, S.A. (1962) J. Biol. Chem. 237, 1535-1548.
2. Buechter, D.D., Medzihradszky, K.F., Burlingame, A.L. and Kenyon, G.L. (1992) J. Biol. Chem. 267, 2173-2178.
3. James, P., Wyss, M., Lutsenko, S., Wallimann, T. and Carafoli, E. (1990) FEBS Lett. 273, 139-143.
4. Gross, M., Furter-Graves, E., Wallimann, T., Eppenberger, H. and Furter, R. (1994) Prot. Science 3, 1058-1068.
5. Clottes, E. and Vial, C. (1996) Arch. Biochim. Biophys. 329, 97-103.
6. Borders, C.L. and Riordan, J.F. (1975) Biochemistry 14, 4699-4704.
7. Fritz-Wolf, K., Schnyder, T., Wallimann, T. and Kabsch, W. (1996) Nature 381, 341-345.
8. Fattoum, A., Kassab, R. and Pradel, L.A. (1975) Biochim. Biophys. Acta 405, 324-339.
9. Raimbault, C., Buchet, R. and Vial, C. (1996) Eur. J. Biochem. 240, 134-142.
10. Ragone, R., Colonna, G., Balestrieri, C., Servillo, L. and Irace, G. (1984) Biochemistry 23, 1871-1875.
11. Fisher, M.T. and Sugar, S.G. (1985) Biochemistry 24, 6696-6701.
12. Atkins, W.M. and Sligar, S.G. (1990) Biochemistry 29, 1271-1275.
13. Laemmli, U.K. (1970) Nature 227, 680-685.
14. Lowry, O.H., Rosenbrough, M.J., Farr, A.F. and Randall, R.J. (1951) J. Biol. Chem. 193, 265-275.
15. Bensadoun, A. and Weinstein, D. (1976) Anal. Biochem. 70, 241-250.
16. Servillo, L., Colonna, G., Balestrieri, C., Ragone, R. and Irace, G. (1982) Anal. Biochem. 126, 251-257.
17. Putney, S., Herlihy, W., Royal, N., Pang, H., Vasken Aposhian, H., Pickering, L., Belagaje, R., Biemann, K., Page, D., Kuby, S. and Schimmel, P. (1984) J. Biol. Chem. 259, 14317-14320.
18. Watts, D.C. (1973) The Enzymes 8, 383-455.
19. Levine, R.L. and Federici, M. (1982) Biochemistry 21, 2600-2606.
20. Ramdas, L., Sherman, F. and Nall, B.T. (1986) Biochemistry 25, 6952-6958.
21. Weinsberg, R.B. (1988) Biochemistry 27, 1515-1521.
22. Ragone, R., Colonna, G., Bismuto, E. and Irace, G. (1987) Biochemistry 26, 2130-2134.
23. Lehrman, S.R., Tuls, J.L., Havel, H.A., Haskell, R.J., Putnam, S.D. and Tomich, C.S.C. (1991) Biochemistry 30, 5777-5784.
24. Clottes, E., Leydier, C., Couthon, F., Marcillat, O. and Vial, C. (1996) Biochim. Biophys. Acta, in press.
25. Fattoum, A., Kassab, R. and Pradel, L.A. (1971) Eur. J. Biochem. 22, 445-456.
26. Price, N.C. (1972) FEBS Letters 24, 21-23.
27. Couthon, F., Clottes, E., Ebel, C. and Vial, C. (1995) Eur. J. Biochem. 234, 160-170.
28. Reed, G.H. and Cohn, M. (1972) J. Biol. Chem. 247, 3073-3081.
29. Grossman, S.H., France, R.M. and Mattheis, J.R. (1992) Biochim. Biophys. Acta 1159, 29-36.
30. Raznikov, A.V., Sklyankina, V.A. and Avaeva, S.M. (1992) FEBS Letters 308, 62-64.
31. Story, R.M. and Steiz, T.A. (1992) Nature 355, 374-376.
32. Mühlebach, S.M., Gross, M., Wirz, T., Wallimann, T., Perriard, J.C. and Wyss, M. (1994) Mol. Cell. Biochem. 133, 245-262.