Structural and functional properties of mutant Arg203Pro from yeast phosphoglycerate kinase, as a model of phosphoglycerate kinase-Uppsala

Protein Engineering

Volumn 9, Issue 2, 1996, Pages 181-187

  Tougard, Pierre ^a   Le, Thanh Hung ^a   Minard, Philippe ^a   Desmadril, Michel ^a   Yon, Jeannine M ^a   Bizebard, Thierry ^a   Lebras, Gérard ^a   Dumas, Christian ^a,b  

^a CNRS   (France)

^b CENTRE DE BIOCHIMIE STRUCTURALE   (France)

Author keywords

Enzyme activity; Pathological mutation; Phosphoglycerate kinase; Stability; Structure

Indexed keywords

FUNGAL PROTEIN; MUTANT PROTEIN; PHOSPHOGLYCERATE KINASE;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME STABILITY; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION; YEAST;

EID: 0029920369     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/9.2.181     Document Type: Article

References (30)

1. Aune, K. and Tanford, C (1969) Biochemistry, 8, 4586-4590.
2. Ballery, N., Minard, P., Desmadril, M. and Yon, J.M (1993) Biochemistry, 32, 708-714.
3. Banks, R.D., Blake, C.C.F , Evans, P.R., Haser, R., Rice, D.W., Hardy, G.W., Merett, M. and Phillips, A.W. (1979) Nature, 279, 773-777.
4. Betton, J.M., Desmadril, M., Mitraki, A. and Yon, J.M (1984) Biochemistry, 23, 6654-6651.
5. Brünger, A T. (1988) XPLOR Manual. Version 1.5. Yale University, New Haven, CT.
6. Brünger, A.T., Kuriyan, J. and Karplus, M. (1987) Science, 235, 458-460.
7. Bücher, T. (1955) Methods Enzymol., 1, 415-422.
8. Crowther, R.A. (1972) In The Molecular Replacement Method, M.G. Rossmann (ed.). Gordon and Breach, New York, pp. 173-178.
9. Davies, G.J., Gamblin, S.J., Littlechild, J.A. and Watson, H.C. (1993) Proteins Struct Funct. Genet., 15, 283-289.
10. Fourme, R., Dhez, P., Benoît, J.P., Kahn, R., Dubuisson, J.M., Besson, P. and Frouin, J. (1992) Rev. Sci. Instrum., 63B, 982-987.
11. Fujti, H. and Yoshida, A. (1980) Proc. Natl Acad. Sci. USA, 77, 5461-5465.
12. Harlos, K., Vas, M. and Blake, C.C.F. (1992) Proteins Struct. Funct. Genet., 12, 133-144.
13. Jones, T.A. (1982) In Sayre, D. (ed.), Computational Crystallography. Oxford University Press, Oxford, pp. 303-317.
14. Leslie, A.G.W., Brick, P. and Wonacott, A.T. (1986) Daresbury Lab. Inf. Q. Protein Crystallogr, 18, 33-39.
15. Mas, M.T., Bailey, J.M. and Resplandor, Z.E. (1988) Biochemistry, 27, 1168-1172.
16. Matthews, B.W. (1968) J. Mol. Biol., 33, 491-497.
17. Minard, P., Desmadril, M., Ballery, N., Perahia, D., Mouawad, L. Hall, L., and Yon, J.M. (1989) Eur. J. Biochem., 185, 419-423.
18. Minard, P., Bowen, D.J., Hall, L., Littlechild, J.A. and Watson, H.C. (1990) Protein Engng, 3, 515-521.
19. Navaza, J. (1987) Acta Crystallogr., Sect. A, 43, 645-653
20. Pace, C.N. (1986) Methods Enzymol., 131, 266-280.
21. Rossmann, M.G. and Blow, D.M. (1962) Acta Crystallogr, 15, 24-31.
22. Sayle, R.A. and Milner-White, E.J. (1995) Trends Biol. Sci., 20, 374-376.
23. Scopes, R.K. (1978) Eur. J. Biochem., 85, 503-516.
24. Serrano, L., Sancho, J., Hirshberg, M. and Fersht, A.N. (1992) J. Mol. Biol., 227, 544-559.
25. Sherman, M.A., Szpikowska, B.K., Dean, S.A., Mathiowetz, A.M., McQueen, N.L. and Mas, M.T. (1990) J. Biol. Chem., 265, 10659-10665.
26. Ten Eyck, L.F. (1977) Acta Crystallogr., Sect. A, 33, 486-492.
27. Tickle, I. (1985) In 'Molecular Replacement'. Proceedings of the Daresbury Laboratory, Warrington, pp. 22-26.
28. Watson, H.C., Wendell, P.L., and Scopes, R.K. (1971) J. Mol. Biol., 57, 623-625.
29. Watson, H.C. et al. (1982) EMBO J., 1, 1635-1640.
30. Yoshida, A. and Watanabe, S. (1972) J. Biol. Chem., 247, 440-445.