Mechanism of Bacillus 1,3-1,4-β-D-glucan 4-glucanohydrolases: Kinetics and pH studies with 4-methylumbelliferyl β-D-glucan oligosaccharides

Biochemistry

Volumn 36, Issue 45, 1997, Pages 13838-13848

  Malet, Carles ^a   Planas, Antoni ^a  

^a INSTITUT QUÍMIC DE SARRIÀ   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

HYDROLASE; HYMECROMONE GLUCURONIDE;

ARTICLE; BACILLUS; BINDING SITE; ENZYME DEGRADATION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME STABILITY; ENZYME SUBUNIT; GENETIC CODE; HYDROLYSIS; MICHAELIS CONSTANT; NONHUMAN; PH; PRIORITY JOURNAL;

BACILLUS; BETA-GLUCANS; BINDING SITES; GLUCANS; GLUCOSIDES; GLYCOSIDE HYDROLASES; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; HYMECROMONE; KINETICS; OLIGOSACCHARIDES; STEREOISOMERISM; SUBSTRATE SPECIFICITY;

BACILLUS LICHENIFORMIS; FELIS CATUS;

EID: 0030694040     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9711341     Document Type: Article

References (56)

1. Parrish, F. W., Perlin, A. S., and Reese, E. T. (1960) Can. J. Chem. 38, 2094-2104.
2. Anderson, M. A., and Stone B. A. (1975) FEBS Lett. 52, 202-207.
3. Malet, C., Jiménez-Barbero, J., Bernabé, M., Brosa, C., and Planas, A. (1993) Biochem. J. 296, 753-758.
4. Stone, B. A., and Clarke, A. E. (1992) Chemistry and Biology of (1→3)-β-glucans, La Trobe University Press, Bundoora, Australia.
5. Varghese, J. N., Garret, T. P. J., Colman, P. M., Chen, L., Høj, P. B., and Fincher, G. B. (1994) Proc. Natl. Acad. Sci. U.S.A. 90, 2785-2789.
6. Borriss, R. (1994) Curr. Top. Mol. Genet. 2, 163-188.
7. Henrissat, B. (1991) Biochem. J. 280, 309-306.
8. Henrissat, B., and Bairoch, A. (1993) Biochem. J. 293, 781-788.
9. Høj, P. B., Condron, R., Traeger, J. C., McAuliffe, J. C., and Stone, B. A. (1992) J. Biol. Chem. 267, 25059-25066.
10. Planas, A., Juncosa, M., Lloberas, J., and Querol, E. (1992) FEBS Lett. 308, 141-145.
11. Juncosa M., Pons, J., Dot, T., Querol, E., and Planas, A. (1994) J. Biol. Chem. 289, 14530-14535.
12. Hahn, M., Olsen, O., Politz, O., Borris, R., and Heinemann, U. (1995) J. Biol. Chem. 7, 3081-3088.
13. Hahn, M., Pons, J., Planas, A., Querol, E., and Heinemann, U. (1995) FEBS Lett. 374, 221-224.
14. Heinemann, U., Aÿ, J., Gaiser, O., Müller, J. J., and Ponnuswamy, M. N. (1996) Biol. Chem. 377, 447-454.
15. Divne, C., Ståhlberg, J., Reinikainen, T., Ruohonen, L., Pettersson, G., Knowles, J. K. C., Teeri, T. T., and Jones, T. A. (1994) Science 265, 524-528.
16. Ståhlberg, J., Divne, C., Koivula, A., Piens, K., Claeyssens, M., Teeri, T. T., and Jones, T. A. (1996) J. Mol. Biol. 264, 337-349.
17. Wakarchuk, W. W., Campbell, R. L., Sung, W. L., Davoodi, J., and Yaguchi, M. (1994) Protein Sci. 3, 467-475.
18. Malet, C., Viladot, J. L., Ochoa, A., Gállego, B., Brosa, C., and Planas, A. (1995) Carbohydr. Res. 274, 285-301.
19. Malet, C., Vallés, J., Bou, J., and Planas, A. (1996) J. Biotechnol. 48, 209-219.
20. Garegg, P. J., Hultberg, H., and Wallin, S. (1982) Carbohydr. Res. 108, 97-101.
21. Planas, A., Juncosa, M., Cayetano, A., and Querol, E. (1992) Appl. Microbiol. Biotechnol. 37, 583-589.
22. Laemmli, U. K (1970) Nature 227, 680-685.
23. Lloberas, J., Querol, E., and Bernués, J. (1988) Appl. Microbiol. Biotechnol. 29, 32-38.
24. Somogyi, M. (1952) J. Biol. Chem. 195, 19-23.
25. Nelson, N. (1944) J. Biol. Chem. 153, 375-380.
26. van Tilbeurgh, H., Claeyssens, M., and de Bruyne, C. K. (1982) FEBS Lett. 149, 152-156.
27. Rosenthal, A. L., and Saifer, A. (1973) Anal. Biochem. 55, 85-92.
28. Ellis, K. J., and Morrison, J. F. (1982) Methods Enzymol. 87, 405-426.
29. van Tilbeurgh, H., Loontiens, F. C., de Bruyne, C. K., and Claeyssens, M.(1988) Methods Enzymol. 160, 45-49.
30. Claeyssens, M., van Tilbeurgh, H., Kamerling, J. P., Berg, J., Vrsanska, M., and Biely, P. (1990) Biochem. J. 270, 251-256.
31. Allen, J. D., and Thoma, J. A. (1976) Biochem. J. 159, 105-120.
32. Allen, J. D. (1980) Methods Enzymol. 64, 248-277.
33. Hoare, D. G., and Koshland, D. E., Jr. (1967) J. Biol. Chem. 242, 2447-2453.
34. Sokolovsky, M., Riordan, J. F., and Vallee, B. L. (1966) Biochemistry 5, 3582-3589.
35. Levy, H. M., Leber, P. D., and Ryan, E. M. (1963) J. Biol. Chem. 238, 3654-3659.
36. Hermans, M. M. P., Kroos, M. A., van Beeumen, J., Oostra, B. A., and Reuser, A. J.J. (1991) J. Biol. Chem. 266, 13507-13512.
37. Yang, Y., and Hamaguchi, K. (1980) J. Biochem. (Tokyo) 87, 1003-1014.
38. Keitel, T., Simon, O., Borris, R., and Heinemann, U. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 5287-5291.
39. Bernabé, M., Jiménez-Barbero, J., and Planas, A. (1994) J. Carbohydr. Chem. 13, 799-817.
40. Koshland, D. E. (1953) Biol. Rev. 28, 416-436.
41. Sinnott, M. L. (1990) Chem. Rev. 90, 1171-1202.
42. Svensson, B. and Søgaard, M. (1993) J. Biotechnol. 29, 1-37.
43. McCarter, J. D., and Withers, S. G. (1994) Curr. Opin. Struct. Biol. 4, 885-892.
44. Brocklehurst, K. (1994) Protein Eng. 7, 291-299.
45. McIntosh, L. P., Hand, G., Johnson, P. E., Joshi, M. D., Körner, M., Plesniak, L. A., Ziser, L., Wakarchuk, W. W., and Withers, S. G. (1996) Biochemistry 35, 9958-9966.
46. Inoue, M., Yamada, H., Yasukochi, T., Kuriki, R., Miki, T., Horiuchi, T., and Imoto, T. (1992) Biochemistry 31, 5545-5553.
47. Bartik, K., Redfield, C. and Dobson, C. M. (1994) Biophys. J. 66, 1180-1184.
48. Thoma, J. A., Brothers, C., and Spradlin, J. (1970) Biochemistry 9, 1768-1775.
49. Thoma, J. A., and Allen, J. D. (1976) Carbohydr. Res. 48, 105-124.
50. Hiromi, K. (1970) Biophys. Res. Commun. 40, 1-14.
51. Hiromi, K., Nitta, Y., Numata, C., and Ono, S. (1973) Biochim. Biophys. Acta 302, 362-375.
52. Iwasa, S., Aoshima, H., Hiromi, K., and Hatano, H. (1974) J. Biochem. 75, 969-978.
53. Suganuma, T., Matsuno, R., Ohnishi, M., and Hiromi, K. (1978) J. Biochem. 84, 293-316.
54. Kato, M., Hiromi, K., and Morita, Y. (1974) J. Biochem. (Tokyo) 75, 565-576.
55. Biely, P., Kratky, Z., and Vrsanska, M. (1981) Eur. J. Biochem. 119, 559-564.
56. Biely, P., Vrsanska, M., and Gorbacheva, I. V. (1983) Biochim. Biophys. Acta 743, 155-161.