Structural and functional effect of Trp-62 → Gly and Asp-101 → Gly substitutions on substrate-binding modes of mutant hen egg-white lysozymes

Biochemical Journal

Volumn 333, Issue 1, 1998, Pages 71-76

  Maenaka, Katsumi ^a,b,f   Matsushima, Masaaki ^c,d   Kawai, Gota ^b   Kidera, Akinori ^c,g   Watanabe, Kimitsuna ^b   Kuroki, Ryota ^e   Kumagai, Izumi ^a  

^a TOHOKU UNIVERSITY   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

^c BIOMOL ENG RESEARCH INSTITUTE   (Japan)

^d Rational Drug Design Laboratories   (Japan)

^e KIRIN BREWERY CO LTD   (Japan)

^f UNIVERSITY OF OXFORD   (United Kingdom)

^g KYOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME INHIBITOR; LYSOZYME; MUTANT PROTEIN; N ACETYLGLUCOSAMINE;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; ENZYME BINDING; ENZYME INHIBITION; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; HEN; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY;

EID: 0032127073     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/bj3330071     Document Type: Article

References (29)

1. Pauling, L. (1946) Chem. Eng. News 24, 1375-1377
2. Wolfenden, R. (1969) Nature (London), 223, 704-705
3. Song, H., Inaka, K., Maenaka, K. and Matsushima, M. (1994) J. Mol. Biol. 244, 522-540
4. Jolles, P. and Jolles, J. (1984) Mol. Cell. Biochem. 53, 165-189
5. Imoto, T., Johnson, L. N., North, A. C. T., Phillips, D. C. and Rupley, J. A. (1972) in The Enzymes, vol. 7 (Boyer, P. D., ed.), pp. 665-868, Academic Press, New York
6. Johnson, L. N., Cheetham, J. C., McLaughlin, P. J., Archarya, K. R., Barford, D. and Phillips, D. C. (1988) Curr. Topics Microbiol. Immunol. 139, 81-134
7. Strynadka, K. C. J. and James, M. N. G. (1991) J. Mol. Biol. 220, 401-424
8. Cheetham, J. C., Artymiuk, P. J. and Phillips, D. C. (1992) J. Mol. Biol. 224, 613-618
9. Kidera, A. and Go, N. (1992) J. Mol. Biol. 225, 457-475
10. Quiocho, F. A. (1988) Curr. Topics Microbiol. Immunol. 126, 135-148
11. Vyas, N. K. (1991) Curr. Opin. Struct. Biol. 1, 732-740
12. Maenaka, K., Matsushima, M., Song, H., Sunada, F., Watanabe, K. and Kumagai, I. (1995) J. Mol. Biol. 247, 281-293
13. Kumagai, I., Maenaka, K., Sunada, F., Takeda, S. and Miura, K. (1993) Eur. J. Biochem. 212, 151-156
14. Maenaka, K., Kawai, G., Watanabe, K., Sunada, F. and Kumagai, I. (1994) J. Biol. Chem. 269, 7070-7075
15. Kumagai, I., Sunada, F., Takeda, S. and Miura, K. (1992) J. Biol. Chem. 267, 4608-4612
16. Miyahara, J., Takahashi, K., Amemiya, Y., Kamiya, N. and Satow, Y. (1986) Nucl. Instrum. Methods A 246, 572-578
17. Amemiya, Y., Matsushita, T., Nakagawa, A., Satow, Y., Miyahara, J. and Chikawa, J. (1988) Nucl. Instrum. Methods A 226, 645-653
18. Tanaka, I., Yao, M., Suzuki, M., Hikichi, K., Matsumoto, T., Kozasa, M. and Katayama, C. (1990) J. Appl. Crystallogr. 23, 334-339
19. Steigeman, W. (1974) Ph.D. Thesis, Technische Universitat, Munchen
20. Jones, T. A. (1978) J. Appl. Crystallogr. 11, 268
21. Hendrickson, W. A. (1985) Methods Enzymol. 115, 252-270
22. Pähler, A. and Hendrickson, W. A. (1990) J. Appl. Crystallogr. 23, 218-221
23. Kuroki, R., Weaver, L. H. and Matthews, B. W. (1993) Science 262, 2030-2033
24. Kuroki, R., Weaver, L. H. and Matthews, B. W. (1995) Nat. Struct. Biol. 2, 1007-1011
25. Harata, K. and Muraki, M. (1995) Acta Crystallogr. D51, 718-724
26. Lumb, K. J., Cheetham, J. C. and Dobson, C. M. (1994) J. Mol. Biol. 235, 1071-1087
27. Blake, C. C. F., Cassels, R., Dobson, C. M., Poulsen, F. M., Williams, R. J. P. and Wilson, K. S. (1981) J. Mol. Biol. 147, 73-95
28. Muraki, M., Harata, K., Sugita, N. and Sato, K. (1996) Biochemistry 35, 13562-13567
29. Kraulis, P. (1991) J. Appl. Crystallogr. 24, 946-950