Site-directed mutagenesis of Asp280 suggests substrate-assisted catalysis of chitinase Al from Bacillus circulans WL-12

Journal of Bioscience and Bioengineering

Volumn 89, Issue 1, 2000, Pages 100-102

  Hashimoto, Masayuki ^a   Honda, Yuji ^b   Nikaidou, Naoki ^a   Fukamizo, Tamo ^c   Watanabe, Takeshi ^a  

^a NIIGATA UNIVERSITY   (Japan)

^b Osaka Prefecture University   (Japan)

^c KINKI UNIVERSITY   (Japan)

Author keywords

Bacillus circulans WL 12; Chitinase; Substrate assisted catalysis

Indexed keywords

BACTERIA; CATALYSIS; MUTAGENESIS;

SITE-DIRECTED MUTAGENESIS;

ENZYME KINETICS;

ASPARTIC ACID; CHITINASE;

ARTICLE; BACILLUS CIRCULANS; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; KINETICS; NONHUMAN; SITE DIRECTED MUTAGENESIS;

BACILLUS CIRCULANS;

EID: 0033974048     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1016/s1389-1723(00)90031-8     Document Type: Article

References (13)

1. 1. Henrissat, B. and Bairoch, A.: Updating the sequence-based classification of glycosyl hydrolases. Biochem. J., 316, 695-696 (1996).
2. 2. Perrakis, A., Tews, I., Dauter, Z., Oppenheim, A. B., Chet, I., Wilson, K. S., and Vorgias, C. E.: Crystal structure of a bacterial chitinase at 2.3 Ȧ resolution. Structure, 2, 1169-1180 (1994).
3. 3. Terwisscha van Scheltinga, A. C., Kalk, K. H., Beintema, J. J., and Dijkstra, B. W.: Crystal structures of hevamine, a plant defence protein with chitinase and lysozyme activity, and its complex with an inhibitor. Structure, 2, 1181-1189 (1994).
4. 4. Watanabe, T., Kobori, K., Miyashita, K., Fujii, T., Sakai, H., Uchida, M., and Tanaka, H.: Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity. J. Biol. Chem., 268, 18567-18572 (1993).
5. 5. Terwisscha van Scheltinga, A. C., Armand, S., Kalk, K. H., Isogai, A., Henrissat, B., and Dijkstra, B. W.: Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis. Biochemistry, 34, 15619-15623 (1995).
6. 6. Tews, I., Scheltinga, A. C., Perrakis, A., Wilson, K. S., and Dijkstra, B. W.: Substrate-assisted catalysis unifies two families of chitinolytic enzymes. J. Am. Chem. Soc., 119, 7954-7959 (1997).
7. 7. Suzuki, K., Taiyoji, M., Sugawara, N., Nikaidou, N., Henrissat, B., and Watanabe, T.: The third chitinase gene (chiC) of Serratia marcescens 2170 and the relationship of its product to other bacterial chitinases. Biochem. J., 343, 587-596 (1999).
8. 8. Aronson, N. N., Blanchard, C. J., and Madura, J. D.: Homology modeling of glycosyl hydrolase family 18 enzymes and proteins. J. Chem. Inf. Comput. Sci., 37, 999-1005 (1997).
9. 9. Imoto, T. and Yagishita, K.: A simple activity measurement of lysozyme. Agric. Biol. Chem., 35, 1154-1156 (1971).
10. 10. Pace, C. N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T.: How to measure and predict the molar absorption coefficient of a protein. Prot. Sci., 4, 2411-2423 (1995).
11. 11. Malcolm, B. A., Rosenberg, S., Corey, M. J., Allen, J. S., de Baetselier, A., and Kirsch, J. F.: Site-directed mutagenesis of the catalytic residues Asp-52 and Glu-35 of chicken egg white lysozyme. Proc. Natl. Acad. Sci. USA, 86, 133-137 (1989).
12. 12. Terwisscha van Scheltinga, A. C., Hennig, M., and Dijkstra, B. W.: The 1.8 Ȧ resolution structure of hevamine, a plant chitinase/lysozyme, and analysis of the conserved sequence and structure motifs of glycosyl hydrolase family 18. J. Mol. Biol., 262, 243-257 (1996).
13. 13. Watanabe, T., Uchida, M., Kobori, K., and Tanaka, H.: Site-directed mutagenesis of the Asp-197 and Asp-202 residues in chitinase A1 of Bacillus circulans WL-12. Biosci. Biotech. Biochem., 58, 2283-2285 (1994).