Plant chitinases use two different hydrolytic mechanisms

FEBS Letters

Volumn 382, Issue 1-2, 1996, Pages 186-188

  Iseli, Beatrice ^a   Armand, Sylvie ^b   Boller, Thomas ^a   Neuhaus, Jean Marc ^c   Henrissat, Bernard ^b  

^a UNIVERSITY OF BASEL   (Switzerland)

^b CNRS   (France)

^c UNIVERSITY OF NEUCHÂTEL   (Switzerland)

Author keywords

Anomeric configuration; Catalytic mechanism; Chitinase; Lysozyme

Indexed keywords

CHITINASE; LYSOZYME;

ANIMAL TISSUE; ARTICLE; BACTERIUM; CHICKEN; EGG; ENZYME ACTIVITY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROLYSIS; NONHUMAN; PLANT; PRIORITY JOURNAL; PROTEIN FAMILY; SPECIES DIFFERENCE;

EID: 0029876802     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/0014-5793(96)00174-3     Document Type: Article

References (27)

1. Boller, T., Gehri, A., Mauch, F. and Vögeli, U. (1983) Planta 157, 22-31.
2. Heitz, T., Segond, S., Kauffmann, S., Geoffroy, P., Prasad, V., Brunner, F., Fritig, B. and Legrand, M. (1994) Mol. Gen. Genet. 245, 246-254.
3. Collinge, D.B., Kragh, K.M., Mikkelsen, J.D., Nielsen, K.K., Rasmussen, U. and Vad, K. (1993) Plant J. 3, 31-40.
4. Schlumbaum, A., Mauch, F., Vögeli, U. and Boller, T. (1986) Nature 324, 365-367.
5. Koga, D., Hirata, T., Sueshige, N., Tanaka, S. and Ide, A. (1992) Biosci. Biotechnol. Biochem. 56, 280-285.
6. Staehelin, C. et al. (1994) Proc. Natl. Acad. Sci. USA 91, 2196-2200.
7. De Jong, A.J. et al. (1993) Plant Cell 5, 615-620.
8. Meins, F., Jr., Fritig, B., Linthorst, H.J.M., Mikkelsen, J.D., Neuhaus, J.-M. and Ryals, J. (1994) Plant Mol. Biol. Rep. 12, S22-S28.
9. Henrissat, B. and Bairoch, A. (1993) Biochem. J. 293, 781-788.
10. Armand, S., Tomita, H., Heyraud, A., Gey, C., Watanabe, T. and Henrissat, B. (1994) FEBS Lett. 343, 177-180.
11. Terwisscha van Scheltinga, A.C., Armand, S., Kalk, K.H., Isogai, A., Henrissat, B. and Dijkstra, B.W. (1995) Biochemistry 34, 15619-15623.
12. Dahlquist, F.W., Borders, C.L., Jacobson, G. and Raftery, M.A. (1969) Biochemistry 8, 694-700.
13. Kuroki, R., Weaver, L.R. and Matthews, B.W. (1995) Nature Struct. Biol. 2, 1007-1011.
14. Holm, L. and Sander, C. (1994) FEBS Lett. 340, 129-132.
15. Iseli, B., Boller, T. and Neuhaus, J.-M. (1993) Plant Physiol. 103, 221-226.
16. Boller, T. and Métraux, J.P. (1988) Physiol Mol Plant Pathol. 33, 11-16.
17. Laemmli, U.K. (1970) Nature 227, 680-685.
18. Blum, H., Beier, H. and Gross, H.J. (1987) Electrophoresis 8, 93-99.
19. Perrakis, A., Tews, I., Dauter, Z., Oppenheim, A.B., Chet, I., Wilson, K.S. and Vorgias, C.E. (1994) Structure 2, 1169-1180.
20. Fukamizo, T., Koga, D. and Goto, S. (1995) Biosci. Biotechnol. Biochem. 59, 311-313.
21. Hart, P.J., Pfluger, H.D., Monzingo, A.F., Hollis, T. and Robertus, J.D. (1995) J. Mol. Biol. 248, 402-413.
22. Henrissat, B., Callebaut, I., Fabrega, S., Lehn, P., Mornon, J.P. and Davies, G. (1995) Proc. Natl. Acad. Sci. USA 92, 7090-7094.
23. Davies, G. and Henrissat, B. (1995) Structure 5, 853-859.
24. Usui, T., Hayashi, Y., Nanjo, F. and Ishido, Y. (1987) Biochim. Biophys. Acta 923, 302-309.
25. Sinnott, M.L. (1990) Chem. Rev. 90, 1171-1202.
26. Wright, H.T., Sandrasegaram, G. and Wright, C.S. (1991) J. Mol. Evol. 33, 283-294.
27. Fukamizo, T., Honda, Y., Goto, S., Boucher, I. and Brzezinski, R. (1995) Biochem. J. 311, 377-383.