Mutations at four active site residues of biotin carboxylase abolish substrate-induced synergism by biotin

Biochemistry

Volumn 38, Issue 11, 1999, Pages 3393-3400

  Blanchard, Carol Z ^a   Lee, Yvonne M ^a   Frantom, Patrick A ^a   Waldrop, Grover L ^a  

^a LOUISIANA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BIOTIN; CARBOXYLASE; MUTANT PROTEIN;

ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME INDUCTION; ENZYME STRUCTURE; ENZYME SUBSTRATE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; ARGININE; ASPARAGINE; BINDING SITES; BIOTIN; CARBON-NITROGEN LIGASES; DRUG SYNERGISM; ESCHERICHIA COLI; GLUTAMIC ACID; HISTIDINE; KINETICS; MAGNESIUM; MUTAGENESIS, SITE-DIRECTED; PEPTIDES; PLASMIDS; SUBSTRATE SPECIFICITY;

EID: 0033574251     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi982660a     Document Type: Article

References (21)

1. Wakil, S. J., Stopps, J. K., and Joshi, V. C. (1983) Annu. Rev. Biochem. 52, 537-579.
2. Li, S.-J., and Cronan, J. E., Jr. (1992) J. Biol. Chem. 267, 855-863.
3. Blanchard, C. Z., and Waldrop, G. L. (1998) J. Biol. Chem. 273, 19140-19145.
4. Waldrop, G. L., Rayment, I., and Holden, H. M. (1994) Biochemistry 33, 10249-10256.
5. Galperin, M. Y., and Koonin, E. V. (1997) Protein Sci. 6, 2639-2643.
6. Thoden, J. B., Holden, H. M., Wesenberg, G., Raushel, F. M., and Rayment, I. (1997) Biochemistry 36, 6305-6316.
7. Stapleton, M. A., Javid-Majd, F., Harmon, M. F., Hanks, B. A., Grahmann, J. L., Mullins, L. S., and Raushel, F. M. (1996) Biochemistry 35, 14352-14361.
8. Shi, Y., and Walsh, C. T. (1995) Biochemistry 34, 2768-2776.
9. Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., and Pease, L. (1989) Gene 77, 51-59.
10. Asada, K. (1982) Biological Carboxylations in Organic and Bio-organic Chemistry of Carbon Dioxide (Inoue, S., and Yamazaki, N., Eds.) John Wiley & Sons, New York.
11. Guchhait, R. B., Polakis, S. E., Dimroth, P., Stoll, E., Moss, J., and Lane, M. D. (1974) J. Biol. Chem. 249, 6633-6645.13.
12. Kazuta, Y., Tokunaga, E., Aramaki, E., and Kondo, H. (1998) FEBS Lett. 427, 377-380.
13. Climent, I., and Rubio, V. (1986) Arch. Biochem. Biophys. 251, 465-470.
14. Ogita, T., and Knowles, J. R. (1988) Biochemsitry 27, 8028-8033.
15. Polakis, S. E., Guchhait, R. B., Zwergel, E. E., Lane, M. D., and Cooper, T. G. (1974) J. Biol. Chem. 249, 6657-6667.
16. Bridger, W. A., Millen, W. A., and Boyer, P. D. (1968) Biochemistry 7, 3608-3616.
17. Eggerer, H. (1965) Biochem. Z. 343, 111-138.
18. Wolodko, W. T., Brownie, E. R., O'Connor, M. D., and Bridger, W. A. (1983) J. Biol. Chem. 258, 14116-14119.
19. Jencks, W. P. (1975) Adv. Enzymol. Relat. Areas Mol. Biol. 43, 219-410.
20. Fersht, A. R., Knill-Jones, J. W., Bedouelle, H., and Winter, G. (1988) Biochemistry 27, 1581-1587.
21. Cannon, W. R., Singleton, S. F., and Benkovic, S. J. (1996) Nat. Struct. Biol. 3, 821-833.