Local and Global Control Mechanisms in Allosteric Threonine Deaminase

Methods in Enzymology

Volumn 380, Issue , 2004, Pages 85-106

  Gallagher, D Travis ^b   Chinchilla, Diana ^a   Lau, Heidi ^a   Eisenstein, Edward ^a  

^a UNIVERSITY OF MARYLAND BIOTECHNOLOGY INSTITUTE   (United States)

^b NATIONAL INSTITUTE OF STANDARDS AND TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

THREONINE DEHYDRATASE;

ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE; FEEDBACK SYSTEM; MICROORGANISM; MODEL; MOLECULAR WEIGHT; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; THERMODYNAMICS;

EID: 1542379833     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(04)80004-1     Document Type: Article

References (40)

1. H. K. Schachman, J. Biol. Chem. 263, 18583 (1988).
2. J.-P. Changeux, BioEssays 15, 625 (1993).
3. W. N. Lipscomb, Chemtracts-Biochemi. Mol. Biol. 2, 1 (1991).
4. P. R. Evans, Curr. Opin. Struct. Biol. 1, 773 (1991).
5. A. Mattevi, M. Rizzi, and M. Bolognesi, Curr. Opin. Struct. Biol. 6, 824 (1996).
6. H. E. Umbarger, Science 123, 848 (1956).
7. J. C. Gerhart and A. B. Pardee, J. Biol. Chem. 237, 891 (1962).
8. H. E. Umbarger, Adv. Enzymol. 37, 349 (1973).
9. H. E. Umbarger, Annu. Rev. Biochem. 47, 533 (1978).
10. H. E. Umbarger, "The Biosynthesis of Isoleucine and Valine and Its Regulation." Addison-Wesley, Reading, MA, 1983.
11. E. Eisenstein, J. Biol. Chem. 266, 5801 (1991).
12. R. O. Burns, Methods Enzymol. 17B (1971).
13. P. Datta, Methods Enzymol. 17B, 566 (1971).
14. G. W. Hatfield and H. E. Umbarger, Methods Enzymol. 17B, 561 (1971).
15. Y. Shizuta and M. Tokushige, Methods Enzymol. 17B, 575 (1971).
16. D. T. Gallagher, G. L. Gilliland, G. Xiao, J. Zondlo, E. E. Fisher, D. Chinchilla, and E. Eisenstein, Structure 6, 465 (1998).
17. J. Monod, J. Wyman, and J.-P. Changeux, J. Mol. Biol. 12, 88 (1965).
18. C. J. Decedue, J. G. Hofler, and R. O. Burns, J. Biol. Chem. 250, 1563 (1975).
19. J. G. Hofler and R. O. Burns, J. Biol. Chem. 253, 1245 (1978).
20. E. Eisenstein, H. D. Yu, and F. P. Schwarz, J. Biol. Chem. 269, 29423 (1994).
21. E. Eisenstein, J. Biol. Chem. 269, 29416 (1994).
22. J.-P. Changeux, J. Mol. Biol. 4, 220 (1962).
23. J.-P. Changeux, Cold Spring Harbor Symp. Quant. Biol. 28, 497 (1963).
24. E. Eisenstein, H. D. Yu, K. E. Fisher, D. A. Iacuzio, K. R. Ducote, and F. P. Schwarz, Biochemistry 34, 9403 (1995).
25. M. M. Rubin and J.-P. Changeux, J. Mol. Biol. 21, 265 (1966).
26. M. L. Johnson and S. G. Fraser, Methods Enzymol. 117, 301 (1985).
27. E. Eisenstein, Arch. Biochem. Biophys. 316, 311 (1995).
28. B. E. Taillon, R. Little, and R. P. Lawther, Gene 63, 245 (1988).
29. K. E. Fisher and E. Eisenstein, J. Bacteriol. 175, 6605 (1993).
30. R. W. Noble, J. Mol. Biol. 39, 479 (1969).
31. G. K. Ackers and H. R. Halvorson, Proc. Natl. Acad. Sci. USA 71, 4312 (1974).
32. G. K. Ackers, M. L. Johnson, F. C. Mills, and S. H. C. Ip, Biochem. Biophys. Res. Commun. 69, 135 (1976).
33. G. K. Ackers, M. L. Doyle, D. Myers, and M. A. Daugherty, Science 255, 54 (1992).
34. F. R. Smith and G. K. Ackers, Proc. Natl. Acad. Sci. USA 82, 5347 (1985).
35. Y. R. Yang and H. K. Schachman, Anal. Biochem. 163, 188 (1987).
36. S. R. Wente and H. K. Schachman, Proc. Natl. Acad. Sci. USA 84, (1987).
37. E. Eisenstein and H. K. Schachman, in "Protein Function: A Practical Approach" (T. Creighton, ed.), p. 135. IRL Press, Oxford, 1989.
38. E. Eisenstein, M. S. Han, T. S. Woo, J. M. Ritchey, I. Gibbons, Y. R. Yang, and H. K. Schachman, J. Biol. Chem. 267, 22148 (1992).
39. G. K. Ackers, Adv. Protein Chem. 51, 185 (1998).
40. D. Chinchilla, F. P. Schwarz, and E. Eisenstein, J. Biol. Chem. 273, 23219 (1998).