Asp-170 is crucial for the redox properties of vanillyl-alcohol oxidase

Journal of Biological Chemistry

Volumn 275, Issue 20, 2000, Pages 14799-14808

  Van Den Heuvel, Robert H H ^a   Fraaije, Marco W ^b   Mattevi, Andrea ^b   Van Berkel, Willem J H ^a  

^a WAGENINGEN UNIVERSITY   (Netherlands)

^b UNIVERSITY OF PAVIA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL OXIDASE; ASPARTIC ACID; FLAVOPROTEIN;

ARTICLE; BIODEGRADATION; CATALYSIS; COMPLEX FORMATION; COVALENT BOND; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; LIGAND BINDING; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN DOMAIN;

ALCOHOL OXIDOREDUCTASES; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ASPARTIC ACID; ESCHERICHIA COLI; EUGENOL; FLAVINS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; PENICILLIUM; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY; SUBSTRATE SPECIFICITY; VARIATION (GENETICS);

EID: 0034685820     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.275.20.14799     Document Type: Article

References (46)

1. Fraaije, M. W., Pikkemaat, M., and van Berkel, W. J. H. (1997) Appl. Environ. Microbiol. 63, 435-439
2. Fraaije, M. W., van Berkel, W. J. H., Benen, J. A. E., Visser, J., and Mattevi, A. (1998) Trends Biochem. Sci. 23, 206-207
3. Fraaije, M. W., Veeger, C., and van Berkel, W. J. H. (1995) Eur. J. Biochem. 234, 271-277
4. Fraaije, M. W., and van Berkel, W. J. H. (1997) J. Biol. Chem. 272, 18111-18116
5. Hopper, D. J. (1976) Biochem. Biophys. Res. Commun. 69, 462-468
6. McIntire, W. S., Hopper, D. J., Craig, J. C., Everthart, E. T., Webster, R. V., Causer, M. J., and Singer, T. P. (1984) Biochem. J. 224, 617-621
7. Mattevi, A., Fraaije, M. W., Mozzarelli, A., Olivi, L., Coda, A., and van Berkel, W. J. H. (1997) Structure 5, 907-920
8. Fraaije, M. W., van den Heuvel, R. H. H., van Berkel, W. J. H., and Mattevi, A. (1999) J. Biol. Chem. 274, 35514-35520
9. Fox, K. M., and Karplus, P. A. (1994) Structure 2, 1089-1105
10. Woodcock, D. M., Crowther, P. J., Doherty, J., Jefferson, S., DeCruz, E., Noyer-Weidner, M., Smith, S. S., Michael, M. Z., and Graham, M. W. (1989) Nucleic Acids Res. 17, 3469-3478
11. Gibson, T. G. (1984) Studies on the Epstein-Barr Virus Genome. Ph.D. thesis. University of Cambridge, United Kingdom
12. Benen, J. A. E., Sánchez-Torres, P., Wagemaker, M., Fraaije, M. W., van Berkel, W. J. H., and Visser, J. (1998) J. Biol. Chem. 273, 7865-7872
13. De Jong, E., van Berkel, W. J. H., van der Zwan, R. P., and de Bont, J. A. M. (1992) Eur. J. Biochem. 208, 651-657
14. Laemmli, U. K. (1970) Nature 227, 680-685
15. Van den Heuvel, R. H. H., Fraaije, M. W., and van Berkel, W. J. H. (1998) J. Bacteriol. 180, 5646-5651
16. Massey, V. (1991) in Flavins and Flavoproteins 1990 (Curti, B., Ronchi, S., and Zannetti, G., eds) pp. 59-66, Walter De Gruyter & Co, New York
17. Clark, W. M. (1960) Oxidation-Reduction Potentials of Organic Systems, pp. 184-203, Williams & Wilkins, Baltimore
18. Gibson, Q. H., Swoboda, B. E. P., and Massey, V. (1964) J. Biol. Chem. 239, 3927-3934
19. Abrahams. J. P., and Leslie, A. G. W. (1996) Acta Crystallogr. Sec. D Biol. Crystallogr. 52, 30-42
20. Collaborative Computational Project Number 4 (1994) Acta Crystallogr. Sec. D Biol. Crystallogr. 50, 760-767
21. Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Acta Crystallogr. Sec. D Biol. Crystallogr. 53. 240-255
22. Lamzin, V. S., and Wilson, K. S. (1993) Acta Crystallogr. Sec. D Biol. Crystallogr. 49, 129-147
23. Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjelgaard, M. (1991) Acta Crystallogr. Sec. A 47, 110-119
24. Morris, A. L., MacArthur, M. W., Hutchinson, E. G., and Thornton, J. M. (1992) Proteins 12, 345-364
25. Fraaije, M. W., Mattevi, A., and van Berkel, W. J. H. (1997) FEBS Lett. 402, 33-35
26. Ghisla, S., Massey, V., and Choong, Y. S. (1979) J. Biol. Chem. 254, 10662-10669
27. Fraaije, M. W., van den Heuvel, R. H. H., Roelofs, J. C. A. A., and van Berkel, W. J. H. (1998) Eur. J. Biochem. 253, 712-719
28. Visser, A. J. W. G., van Berkel, W. J. H., and de Kok, A. (1995) Biochim. Biophys. Acta 1229, 381-385
29. Massey, V., Müller, F., Feldberg, R., Schuman, M., Sullivan, P. A., Howell, L. G., Mayhew, S. G., Matthews, R. G., and Foust, G. P. (1969) J. Biol. Chem. 244, 3999-4006
30. Strickland, S., Palmer, G., and Massey, V. (1975) J. Biol. Chem. 250, 4048-4052
31. Porter, D. J. T., Voet, J. G., and Bright, H. J. (1977) J. Biol. Chem. 252, 4464-4473
32. Pollegioni, L., Blodig, W., and Ghisla, S. (1994) J. Biol. Chem. 272, 4924-4934
33. Minnaert, K. (1965) Biochim. Biophys. Acta 110, 42-56
34. Palfey, B. A., Entsch, B., Ballou, D. P., and Massey, V. (1994) Biochemistry 33, 1545-1554
35. Mancini-Samuelson, G. J., Kieweg, V., Sabaj, K. M., Ghisla, S., and Stankovich, M. T. (1998) Biochemistry 37, 14605-14612
36. Chang, F.-C., and Swenson, R. P. (1999) Biochemistry 38, 7168-7176
37. Müller, F. (1991) in Chemistry and Biochemistry of Flavoenzymes (Müller, F., ed) Vol. III, pp. 557-595, CRC Press Inc., Boca Raton, FL
38. Mewies, M., McIntire, W. S., and Scrutton, N. S. (1998) Protein Sci. 7, 7-20
39. Miller, J. R., and Edmondson, D. E. (1999) J. Biol. Chem. 274, 23515-23525
40. Frost, J. W., and Rastetter, W. H. (1980) J. Am. Chem. Soc. 102, 7157-7159
41. Trickey, P., Wagner, M. A., Schuman Jorns, M., and Mathews, F. S. (1999) Structure 7, 331-345
42. Bolton, J. L., Turnipseed, S. B., and Thompson, J. A. (1997) Chem. Biol. Interact. 107, 185-200
43. Bodell, W. J., Ye, Q., Pathak, D. N., and Pongracz, K. (1998) Carcinogenesis 19, 437-443
44. Cunane, L. M., Chen, Z.-W., Shamala, N., Mathews, F. S., Cronin, C., and McIntire, W. S. (2000) J. Mol. Biol. 295, 357-374
45. Mathews, F. S., Chen, Z.-W., Bellamy, H. D., and McIntire, W. S. (1991) Biochemistry 30, 238-247
46. Kraulis, P. J. (1991) J. Appl. Crystallogr. 24, 946-950