Anatomy of a proficient enzyme: The structure of orotidine 5′-monophosphate decarboxylase in the presence and absence of a potential transition state analog

Proceedings of the National Academy of Sciences of the United States of America

Volumn 97, Issue 5, 2000, Pages 2011-2016

  Miller, Brian G ^a   Hassell, Anne M ^b   Wolfenden, Richard ^a   Milburn, Michael V ^b   Short, Steven A ^b  

^a UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^b GLAXOSMITHKLINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYLIC ACID DERIVATIVE; OROTIDINE 5' PHOSPHATE DECARBOXYLASE; PYRIMIDINE; RECOMBINANT ENZYME; RIBOSE PHOSPHATE; URIDINE PHOSPHATE;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; DECARBOXYLATION; ENZYME ACTIVE SITE; ENZYME STRUCTURE; HYDROGEN BOND; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; SACCHAROMYCES CEREVISIAE;

AMINO ACID SEQUENCE; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OROTIDINE-5'-PHOSPHATE DECARBOXYLASE; PROTEIN CONFORMATION; RECOMBINANT FUSION PROTEINS; SACCHAROMYCES CEREVISIAE;

SACCHAROMYCES CEREVISIAE;

EID: 0034104285     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.030409797     Document Type: Article

References (25)

1. Radzicka, A. & Wolfenden, R. (1995) Science 267, 90-93.
2. Bell, J. B. & Jones, M. E. (1991) J. Biol. Chem. 266, 12662-12667.
3. Miller, B. G., Traut, T. W. & Wolfenden, R. (1998) Bioorg. Chem. 26, 283-288.
4. Levine, H. L., Brody, R. & Westheimer, F. H. (1980) Biochemistry 19, 4990-4999.
5. Miller, B. G., Smiley, J. A., Short, S. A. & Wolfenden, R. (1999) J. Biol. Chem. 274, 23841-23843.
6. Otwinowski, Z. & Minor, W. (1997) Methods Enzymol. 276, 307-326.
7. Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, R., Grosse-Kunstleve, W., Jiang, J.-S., Kuszewski, J., Nilges, M., Pannu, N. S., et al. (1998) Acta Crystallogr. D 54, 905-921.
8. Cowtan, K. (1994) Protein Crystallogr. 31, 34-38.
9. Collaborative Computing Project 4 (1994) Acta Crystallogr. D 50, 760-776.
10. Banner, D. W., Bloomer, A. C., Petsko, G. A., Phillips, D. C., Pogson, C. I., Wilson, I. A., Corran, P. H., Furth, A. J., Milman, J. D., Offord, R. E., et al. (1975) Nature (London) 255, 609-614.
11. Alani, E. & Kleckner, N. (1987) Genetics 117, 5-12.
12. Cullin, C. & Minvielle-Sebastia, L. (1994) Yeast 10, 105-112.
13. Schneider, B. L., Seufert, W., Steiner, B., Yang, Q. H. & Futcher, A. B. (1995) Yeast 11, 1265-1274.
14. Yablonski, M. J., Pasek, D. A., Han, B.-D., Jones, M. E. & Traut, T. W. (1996) J. Biol. Chem. 271, 10704-10708.
15. Farber, G. F. & Petsko, G. A. (1990) Trends Biochem. Sci. 15, 228-234.
16. Smiley, J. A., Paneth, P., O'Leary, M. H., Bell, J. B. & Jones, M. E. (1991) Biochemistry 30, 6216-6223.
17. Beak, P. & Siegel, B. (1976) J. Am. Chem. Soc. 98, 3601-3606.
18. Hruska, F. (1971) J. Am. Chem. Soc. 93, 1795-1797.
19. Smiley, J. A. & Jones, M. E. (1992) Biochemistry 31, 12162-12168.
20. Lee, J. K. & Houk, K. N. (1997) Science 276, 942-945.
21. Warshel, A. (1998) J. Biol. Chem. 273, 27035-27038.
22. Jencks, W. P. (1975) Adv. Enzymol. Relat. Areas Mol. Biol. 43, 219-410.
23. Wolfenden, R. (1999) Bioorg. Med. Chem. 7, 647-652.
24. Wolfenden, R. (1974) Mol. Cell. Biochem. 3, 207-211.
25. Carson, M. (1997) Methods. Enzymol. 277, 493-505.