The role of Arg114 at subsites E and F in reactions catalyzed by hen egg-white lysozyme

Bioscience, Biotechnology and Biochemistry

Volumn 72, Issue 3, 2008, Pages 823-832

  Kawamura, Shunsuke ^a   Chijiiwa, Yuki ^a   Minematsu, Toshie ^b   Fukamizo, Tamo ^b   Vårum, Kjell M ^c   Torikata, Takao ^a  

^a TOKAI UNIVERSITY   (Japan)

^b KINKI UNIVERSITY   (Japan)

^c NORWEGIAN UNIVERSITY OF SCIENCE AND TECHNOLOGY   (Norway)

Author keywords

1H NMR; Lysozyme; Lysozyme catalyzed reaction; Site directed mutagenesis; Transglycosylation

Indexed keywords

LYSOZYME; LYSOZYME-CATALYZED REACTION; SITE-DIRECTED MUTAGENESIS; TRANSGLYCOSYLATION;

AMINES; CATALYSIS; FREE ENERGY; MUTAGENESIS; REACTION KINETICS;

ENZYME ACTIVITY;

ARGININE; HEN EGG LYSOZYME; LYSOZYME; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ANIMAL; ARTICLE; CATALYSIS; CHEMISTRY; CHICKEN; ENZYME ACTIVE SITE; FEMALE; KINETICS; METABOLISM; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN BINDING; PROTEIN CONFORMATION;

AMINO ACID SUBSTITUTION; ANIMALS; ARGININE; CATALYSIS; CATALYTIC DOMAIN; CHICKENS; FEMALE; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MURAMIDASE; PROTEIN BINDING; PROTEIN CONFORMATION;

EID: 41549094623     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.70694     Document Type: Article

References (44)

1. Imoto, T., Johnson, L. N., North, A. C. T., Phillips, D. C., and Rupley, J. A., Lysozyme. In "Enzymes" Vol. 7, 3rd ed., ed. Boyer, P. D., Academic Press, New York, pp. 665-868 (1972).
2. Blake, C. C. F., Koenig, D. F., Mair, G. A., North, A. C. T., Phillips, D. C., and Sarma, V. R., Structure of hen egg-white lysozyme: a three-dimensional fourier synthesis at 2 angstrom resolution. Nature, 206, 757-761 (1965).
3. Blake, C. C. F., Johnson, L. N., Mair, G. A., North, A. C. T., Phillips, D. C., and Sarma, V. R., Crystallographic studies on the activity of hen egg white lysozyme. Proc. Roy. Soc. Ser. B, 167, 378-388 (1967).
4. Kuroki, R., Yamada, H., Moriyama, T., and Imoto, T., Chemical mutations of the catalytic carboxyl groups in lysozyme to the corresponding amides. J. Biol. Chem., 261, 13572-13574 (1986).
5. Malcolm, B. A., Rosenberg, S., Corey, M. J., Allen, J. S., Baetselier, A. D., 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).
6. Hashimoto, Y., Yamada, K., Motoshima, H., Omura, T., Yamada, H., Yasukochi, T., Miki, T., Ueda, T., and Imoto, T., A mutation study of catalytic residue Asp52 in hen egg white lysozyme. J. Biochem., 119, 145-150 (1996).
7. Vocadlo, D. J., Davies, G. J., Laine, R., and Withers, S. G., Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate. Nature, 412, 835-838 (2001).
8. Kravchenko, N. A., Lysozyme as a transferase. Proc. Roy. Soc. Ser. B, 167, 429-430 (1967).
9. Rupley, J. A., The binding and cleavage by lysozyme of N-acetylglucosamine oligosaccharides. Proc. Roy. Soc. Ser. B, 167, 416-428 (1967).
10. Sharon, N., The chemical structure of lysozyme substrates and their cleavage by the enzyme. Proc. Roy. Soc. Ser. B, 167, 402-415 (1967).
11. Johnson, L. N., Cheetam, J., McLaughlin, P. J., Acharya, K. R., Barford, D., and Phillips, D. C., Protein-oligosaccharide interactions: lysozyme, phosphorylase, amylases. In "Current Topics in Microbiology and Immunology" Vol. 139, Springer-Verlag, Berlin, pp. 81-134 (1988).
12. Hadfield, A. T., Harvey, D. J., Archer, D. B., MacKenzie, D. A., Jeenes, D. J., Radford, S. E., Lowe, G., Dobson, C. M., and Johnson, L. N., Crystal structure of the mutant D52S hen egg white lysozyme with an oligosaccharide product. J. Mol. Biol., 243, 856-872 (1994).
13. Kuroki, R., Ito, Y., Kato, Y., and Imoto, T., A covalent enzyme-substrate adduct in a mutant hen egg white lysozyme (D52E). J. Biol. Chem., 272, 19976-19981 (1997).
14. Pincus, M. R., and Scheraga, H. A., Conformational energy calculations of enzyme-substrate and enzymeinhibitor complexes of lysozyme. 2. Calculations of the structures of complexes with a flexible enzyme. Macromolecules, 12, 633-644 (1979).
15. Pincus, M. R., and Scheraga, H. A., Prediction of the three-dimensional structures of complexes of lysozyme with cell wall substrates. Biochemistry, 20, 3960-3965 (1981).
16. 6 in the active site of lysozyme. Biochemistry, 23, 993-997 (1984).
17. Inoue, M., Yamada, H., Yasukochi, T., Miki, T., Horiuchi, T., and Imoto, T., Left-sided substrate binding of lysozyme: evidence for the involvement of asparagine-46 in the initial binding of substrate to chicken lysozyme. Biochemistry, 31, 10322-10330 (1992).
18. Muraki, M., Morikawa, M., Jigami, Y., and Tanaka, H., A structural requirement in the subsite F of lysozyme. Eur. J. Biochem., 179, 573-579 (1989).
19. Harata, K., Muraki, M., and Jigami, Y., Role of Arg115 in the catalytic action of human lysozyme. J. Mol. Biol., 233, 524-535 (1993).
20. Toshima, G., Kawamura, S., Araki, T., and Torikata, T., Histidine-114 at subsites E and F can explain the characteristic enzymatic activity of guinea hen egg-white lysozyme. Biosci. Biotechnol. Biochem., 67, 540-546 (2003).
21. Yamada, H., and Imoto, T., A convenient synthesis of glycol chitin, a substrate of lysozyme. Carbohydr. Res., 92, 160-162 (1981).
22. Rupley, J. A., The hydrolysis of chitin by concentrated hydrochloric acid, and the preparation of low-molecular weight substrates for lysozyme. Biochim. Biophys. Acta, 83, 245-255 (1964).
23. 1HNMR-spectroscopy. Eur. J. Biochem., 251, 335-342 (1998).
24. Sarkar, G., and Sommer, S. S., The "megaprimer" method of site-directed mutagenesis. Biotechniques, 8, 404-407 (1990).
25. Kawamura, S., Toshima, G., Imoto, T., Araki, T., and Torikata, T., Amino acid residues in subsites E and F responsible for the characteristic enzymatic activity of duck egg-white lysozyme. J. Biochem., 131, 663-670 (2002).
26. Pace, C. N., Measuring and increasing in protein stability. Trends Biotechnol., 8, 93-98 (1990).
27. Masaki, A., Fukamizo, T., Otakara, A., Torikata, T., Hayashi, K., and Imoto, T., Lysozyme-catalyzed reaction of chitooligosaccharides. J. Biochem., 90, 527-533 (1981).
28. Masaki, A., Fukanizo, T., Otakara, A., Torikata, T., Hayashi, K., and Imoto, T., Estimation of rate constants in lysozyme-catalyzed reaction of chitooligosaccharides. J. Biochem., 90, 1167-1175 (1981).
29. Fukamizo, T., Minematsu, T., Yanase, Y., Hayashi, K., and Goto, S., Substrate size dependence of lysozyme-catalyzed reaction. Arch. Biochem. Biophys., 250, 312-321 (1986).
30. Fukamizo, T., Goto, S., Torikata, T., and Araki, T., Enhancement of transglycosylation activity of lysozyme by chemical modification. Agric. Biol. Chem., 53, 2641-2651 (1989).
31. Kuhara, S., Ezaki, E., Fukamizo, T., and Hayashi, K., Estimation of the free energy change of substrate binding in lysozyme-catalyzed reactions. J. Biochem., 92, 121-127 (1982).
32. Fukamizo, T., Torikata, T., Nagayama, T., Minematsu, T., and Hayashi, K., Enzymatic activity of avian eggwhite lysozymes. J. Biochem., 94, 115-122 (1983).
33. Kawamura, S., Fukamizo, T., Araki, T., and Torikata, T., Expression of a synthetic gene coding for ostrich eggwhite lysozyme in Pichia pastoris and its enzymatic activity. J. Biochem., 133, 123-131 (2003).
34. 1H-NMR assignments and secondary structure of hen egg white lysozyme in solution. Biochemistry, 27, 122-136 (1988).
35. 1H-NMR spectroscopy. Biosci. Biotechnol. Biochem., 65, 1766-1773 (2001).
36. Fukamizo, T., Kuhara, S., and Hayashi, K., Enzymatic activity of Trp 62-modified lysozyme. J. Biochem., 92, 717-724 (1982).
37. Fukamizo, T., Hayashi, K., and Goto, S., The role of binding subsite A in reactions catalyzed by hen egg-white lysozyme. Eur. J. Biochem., 158, 463-467 (1986).
38. Fukamizo, T., Goto, S., Torikata, T., and Araki, T., State of binding subsites in Asp 101-modified lysozymes. J. Biochem., 158, 463-467 (1990).
39. Fukamizo, T., Hatta, T., and Goto, S., Hen-egg-white lysozyme modified with histamine. Eur. J. Biochem., 231, 56-64 (1995).
40. Araki, T., Yamamoto, T., and Torikata, T., Reptile lysozyme: the complete amino acid sequence of soft-shelled turtle lysozyme and its activity. Biosci. Biotechnol. Biochem., 62, 316-324 (1998).
41. Araki, T., Matsumoto, T., and Torikata, T., The amino acid sequence of monal pheasant lysozyme and its activity. Biosci. Biotechnol. Biochem., 62, 1988-1994 (1998).
42. Araki, T., Toshima, G., Kusao, T., Chijiiwa, Y., Kawamura, S., and Torikata, T., The amino acid sequence of satyr tragopan lysozyme and its activity. Biosci. Biotechnol. Biochem., 67, 2621-2626 (2003).
43. Araki, T., Seki, S., Hirakawa, H., Chijiiwa, Y., Kawamura, S., Kuhara, S., and Torikata, T., Bare-faced curassow lysozyme carrying amino acid substitutions at subsites E and F shows a change in activity against chitooligosaccharide caused by a local conformational change. J. Biochem., 136, 485-493 (2004).
44. Chijiiwa, Y., Kawamura, S., Torikata, T., and Araki, T., Amino acid sequence and activity of green turtle (Chelonia mydas) lysozyme. Protein J., 25, 336-344 (2006).