Crystallographic complexes of glucoamylase with maltooligosaccharide analogs: Relationship of stereochemical distortions at the nonreducing end to the catalytic mechanism

Biochemistry

Volumn 35, Issue 25, 1996, Pages 8319-8328

  Aleshin, Alexander E ^a   Stoffer, Bjarne ^c,d   Firsov, Leonid M ^b   Svensson, Birte ^c   Honzatko, Richard B ^a  

^a IOWA STATE UNIVERSITY   (United States)

^b PETERSBURG NUCLEAR PHYSICS INSTITUTE   (Russian Federation)

^c CARLSBERG LABORATORY   (Denmark)

^d UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

ACARBOSE; GLUCAN 1,4 ALPHA GLUCOSIDASE; MALTOSE; OLIGOSACCHARIDE;

ARTICLE; ASPERGILLUS AWAMORI; BINDING AFFINITY; CATALYSIS; COMPLEX FORMATION; CRYSTALLOGRAPHY; ENZYME ACTIVE SITE; ENZYME STRUCTURE; ENZYME SUBSTRATE; GLUCOSE METABOLISM; HYDROGEN BOND; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; STEREOCHEMISTRY;

ACARBOSE; ASPERGILLUS; BINDING SITES; CARBOHYDRATE SEQUENCE; CATALYSIS; COMPUTER SIMULATION; CRYSTALLOGRAPHY, X-RAY; ENZYME INHIBITORS; GLUCAN 1,4-ALPHA-GLUCOSIDASE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OLIGOSACCHARIDES; PROTEIN CONFORMATION; TRISACCHARIDES;

ASPERGILLUS AWAMORI;

EID: 0030056077     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi960321g     Document Type: Article

References (53)

1. Aleshin, A., Golubev, A., Firsov, L. M., & Honzatko, R. B. (1992) J. Biol. Chem. 267, 19291-19298.
2. Aleshin, A. E., Hoffman, C., Firsov, L. M., & Honzatko, R. B. (1994a) J. Mol. Biol. 238, 575-591.
3. Aleshin, A. E., Firsov, L. M., & Honzatko, R. B. (1994b) J. Biol. Chem. 269, 15631-15639.
4. Arnott, S., & Scott, W. E. (1972) J. Chem. Soc., Perkin Trans. 2, 324-335.
5. Beckhaus, H.-D., Hellmann, G., Ruchardt, C., Kitschke, B., & Lindner, H. J. (1978) Chem. Ber. 111, 3780-3789.
6. Berland, C. R., Sigurskjold, B. W., Stoffer, B., Frandsen, T. P., & Svensson, B. (1995) Biochemistry 34, 10153-10161.
7. Blake, C. C. F., Mair, G. A., North, A. C. T., Phillips, D. C., & Sarma, V. R. (1967) Proc. R. Soc. London B 167, 378-388.
8. Bock, K., Meldal, M., & Refn, S. (1991) Carbohydr. Res. 221, 1-16.
9. Boel, E., Hjort, I., Svensson, B., Norris, F., Norris, K. E., & Fiil, N. P. (1984) EMBO J. 3, 1097-1102.
10. Brunger, A. T. (1992) in XPLOR: Version 3.1, A system for X-ray crystallography and NMR, Yale University Press, New Haven, CT, and London.
11. Cambillau, C., & Horjales, E. (1987) J. Mol. Graphics 5, 174-177.
12. Dowd, M. K., Zeng, J., French, A. D., & Reilly, P. J. (1992) Carbohydr. Res. 264, 1-19.
13. Engh, R. A., & Huber, R. (1991) Acta Crystallogr. A47, 392-400.
14. Firsov, L. M. (1978) Biokhimiya 43, 2222-2232.
15. Ford, L. O., Johnson, L. N., Machin, P. A., Phillips, D. C., & Tjian, R. (1974) J. Mol. Biol. 88, 349-371.
16. Frandsen, T. P., Dupont, C., Lehmbeck, J., Stoffer, B., Sierks, M. R., Honzatko, R. B., & Svensson, B. (1994) Biochemistry 33, 13808-13816.
17. Golubev, A. M., Neustroev, K. N., Aleshin, A. E., & Firsov, L. M. (1992) J. Mol. Biol. 226, 271-272.
18. Hackert, M. L., & Jacobson, R. A. (1971) Acta. Crystallogr. B27, 203-209.
19. Hadfield, A. T., Harvey, D. J., Archer, D. B., Mackenzie, D. A., Jeenes, D. J., Radford, S. E., Lowe, G., Dobson, C. M., & Johnson, L. N. (1994) J. Mol. Biol. 243, 856-872.
20. Harris, E. M. S., Aleshin, A. E., Firsov, L. M., & Honzatko, R. B. (1993) Biochemistry 32, 1618-1626.
21. Hiromi, K. (1970) Biochem. Biophys. Res. Commun. 40, 1-6.
22. Howard, A. J., Nielsen, C., & Xuong, N. H. (1985) Methods Enzymol. 114, 452-472.
23. Imoto, I., Johnson, L. N., North, A. C. T., Phillips, D. C., & Rupley, J. A. (1972) in The Enzymes (3rd ed.) (Boyer, P., Ed.) Vol. 7, pp 665-868, Academic Press, New York.
24. Joshi, N. V., & Rao, V. S. R. (1979) Biopolymers 18, 2993-3004.
25. Koyama, T., Inokuchi, N., Kikuchi, Yu., Shimada, H., Iwama, M., Takahashi, T., & Irie, M. (1984) Chem. Pharm. Bull. 32, 757-776.
26. Kraulis, J. (1991) J. Appl. Crystallogr. 24, 946-950.
27. Kuroki, R., Weaver, L. H., & Matthews, B. W. (1993) Science 262, 2030-2033.
28. Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) J. Appl. Crystallogr. 26, 283-291.
29. Luzzati, V. (1952) Acta Crystallogr. 5, 802-810.
30. Matsui, H., Blanchard, J. S., Brewer, C. F., & Hehre, E. J. (1989) J. Biol. Chem. 264, 8714-8716.
31. McCarter, J. D., & Withers, S. G. (1994) Curr. Opin. Struct. Biol. 4, 885-892.
32. Meagher, M. M., Nikolov, Z. L., & Reilly, P. J. (1989) Biotechnol. Bioeng. 34, 681-688.
33. Melberg, S., Rasmussen, K., Scordamaglia, R., & Tosi, C. (1979) Carbohydr. Res. 76, 23-37.
34. Neustroev, K. N., & Firsov, L. M. (1990) Biokhimiya 55, 776-785.
35. Pazur, J. H., & Ando, T. (1960) J. Biol. Chem. 235, 297-302.
36. Phillips, D. C. (1967) Proc. Natl. Acad. Sci. U.S.A. 57, 484-495.
37. Post, C. B., & Karplus, M. (1986) J. Am. Chem. Soc. 108, 1317-1319.
38. Sergeev, V. R., & Firsov, L. M. (1985b) Biokhimiya 50, 416-423.
39. Sierks, M. R., Ford, C., Reilly, P. J., & Svensson, B. (1990) Protein Eng. 3, 193-198.
40. Sigurskjold, B. W., Berland, C. R., & Svensson, B. (1994) Biochemistry 33, 10191-10199.
41. Sinnott, M. L. (1990) Chem. Rev. 90, 1171-1202.
42. Squillacote, M., Sheridan, R. C., Chapman, O. L., & Anet, F. A. L. (1975) J. Am. Chem. Soc. 97, 3244-3246.
43. Stoffer, B., Aleshin, A. E., Firsov, L. M., Svensson, B., & Honzatko, R. B. (1995) FEBS Lett. 358, 57-61.
44. Strynadka, N. C. J., & James, M. N. G. (1991) J. Mol. Biol. 220, 401-424.
45. Svensson, B., & Sierks, M. R. (1992) Carbohydr. Res. 227, 29-44.
46. Svensson, B., Larsen, K., Svendsen, I., & Boel, E. (1983) Carlsberg Res. Commun. 48, 529-544.
47. Tanaka, A., Ohnishi, M., & Hiromi, K. (1982) Biochemistry 21, 107-113.
48. Takaka, Y., Tao, W., Blanchard, J. S., & Hehre, E. (1994) J. Biol. Chem. 269, 32306-32312.
49. Thoma, J. A. (1968) J. Theor. Biol. 19, 297-310.
50. Vernon, C. A. (1967) Proc. R. Soc. London, B 167, 389-401.
51. Warshel, A., & Levitt, M. (1976) J. Mol. Biol. 103, 227-249.
52. Weill, C. E., Burch, R. J., & Van Dyk, J. W. (1954) Cereal Chem. 31, 150-158.
53. Weis, W. I., Brunger, A. T., Skehel, J. J., & Wiley, D. C. (1990) J. Mol. Biol. 212, 737-761.