Histidine modification and mutagenesis point to the involvement of a large conformational change in the mechanism of action of phage lambda lysozyme

FEBS Letters

Volumn 460, Issue 3, 1999, Pages 442-446

  Evrard, Christine ^a   Fastrez, Jacques ^a   Soumillion, Patrice ^a  

^a UNIVERSITÉ CATHOLIQUE DE LOUVAIN   (Belgium)

Author keywords

Diethyl pyrocarbonate; Functional motion; Lysozyme

Indexed keywords

ASPARAGINE; HISTIDINE; LYSOZYME;

ARTICLE; BACTERIOPHAGE LAMBDA; CHEMICAL MODIFICATION; CONFORMATIONAL TRANSITION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME INACTIVATION; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN STABILITY;

BACTERIOPHAGE LAMBDA; DIETHYL PYROCARBONATE; ENZYME ACTIVATION; ENZYME STABILITY; HISTIDINE; MODELS, MOLECULAR; MURAMIDASE; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; VIRAL PROTEINS;

EID: 0032731391     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(99)01395-2     Document Type: Article

References (30)

1. Yon J.M., Perahia D., Ghelis C. Biochimie. 80:1998;33-42.
2. Imada M., Tsugita A. Nature. 233:1971;230-231.
3. Sanger F., Coulson A.R., Hong G.F., Hill D.F., Petersen G.B. J. Mol. Biol. 162:1982;729-773.
4. Black, L.W. and Hogness (1969) J. Biol. Chem. 244, 1968-1975, 1976-1981 and 1982-1987.
5. Bienkowska-Szewczyk K., Taylor A. Biochim. Biophys. Acta. 615:1980;489-496.
6. Evrard C., Fastrez J., Declercq J.-P. J. Mol. Biol. 276:1998;151-164.
7. Jespers L., Sonveaux E., Fastrez J. J. Mol. Biol. 228:1992;529-538.
8. Mchaourab H.S., Oh K.J., Fang C.J., Hubbell W.L. Biochemistry. 36:1997;307-316.
9. Faber H.R., Matthews B.W. Nature. 348:1990;263-266.
10. Zhang X.J., Wozniak J.A., Matthews B.W. J. Mol. Biol. 250:1995;527-552.
11. Duewel H., Daub E., Robinson V., Honek J.F. Biochemistry. 36:1997;3404-3416.
12. Imoto, T., Johnson, L.N., North, A.C.T., Phillips, D.C. and Rupley, J.A. (1972) in: The Enzymes, 3rd edn. (Boyer, P., Ed.), Vol. 7, pp. 665-868, Academic Press, New York.
13. Tsugita, A. (1971) in: The Enzymes, 3rd edn. (Boyer, P., Ed.), Vol. 5, pp. 343-411, Academic Press, New York.
14. Jollès P., Jollès J. Mol. Cell. Biochem. 63:1984;165-189.
15. Fastrez J. EXS. 75:1996;35-64.
16. Taylor A., Gorazdowska M. Biochim. Biophys. Acta. 342:1974;133-136.
17. Taylor A., Das B.C., Van Heijenoort J. Eur. J. Biochem. 53:1975;47-54.
18. Bienkowska-Szewczyk K., Lipinska B., Taylor A. Mol. Gen. Genet. 184:1981;111-114.
19. Engel H., Kazemier B., Keck W. J. Bacteriol. 173:1991;6773-6782.
20. Thunnissen A.M., Dijkstra A.J., Kalk K.H., Rozeboom H.J., Engel H., Keck W., Dijkstra B.W. Nature. 367:1994;750-753.
21. Thunnissen A.M., Isaacs N.W., Dijkstra B.W. Proteins. 22:1995;245-258.
22. Remaut E., Stanssens P., Fiers W. Gene. 15:1981;81-93.
23. Jespers L., Sonveaux E., Fastrez J., Phanapoulos A., Davison J. Protein Eng. 4:1991;485-492.
24. Nakamaye K.L., Eckstein F. Nucleic Acids Res. 14:1986;9679-9698.
25. Soumillion P., Fastrez J. Biochem. J. 286:1992;187-193.
26. Soumillion P., Fastrez J. Protein Eng. 8:1995;451-456.
27. Lundblad, R.L. and Noyes, C.M. (1984) in: Chemical Reagents for Protein Modification, Vol. 1, pp. 105-125, CRC Press, Boca Raton, FL.
28. Muhlrad A., Hegyi G., Toth G. Acta Biochim. Biophys. 2:1967;19-29.
29. Burstein Y., Walsh K.A., Neurath H. Biochemistry. 13:1974;205-210.
30. Soumillion P., Fastrez J. Protein Eng. 11:1998;213-217.