Activation of D-tyrosine by Bacillus stearothermophilus tyrosyl-tRNA synthetase: 1. Pre-steady-state kinetic analysis reveals the mechanistic basis for the recognition of D-tyrosine

Journal of Biological Chemistry

Volumn 283, Issue 19, 2008, Pages 12960-12970

  Sheoran, Anita ^a   Sharma, Gyanesh ^a   First, Eric A ^a  

^a LOUISIANA STATE UNIVERSITY HEALTH SCIENCES CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOLOGY; BINDING SITES; CARBOXYLATION; CHEMICAL ACTIVATION; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; LIGHT EMISSION; LUMINESCENCE; OXYGEN; RATE CONSTANTS;

ACTIVATION REACTIONS; ADENYLATE; AMINOACYLATION; BACILLUS STEAROTHERMOPHILUS; BLUE SHIFTS; FORWARD RATE CONSTANTS; INTRINSIC FLUORESCENCES; KINETIC ANALYSES; OXYGEN ATOMS; SIDE CHAINS; SYNTHETASE;

AMINO ACIDS;

AMINO ACID TRANSFER RNA LIGASE; BACTERIAL ENZYME; CARBON 14; RECOMBINANT ENZYME; TYROSINE; TYROSINE TRANSFER RNA LIGASE; DRUG DERIVATIVE; PYROPHOSPHATE;

ARTICLE; BINDING AFFINITY; CATALYSIS; ENZYME ACTIVATION; ENZYME KINETICS; ENZYME PURIFICATION; FLUORESCENCE SPECTROSCOPY; GEOBACILLUS STEAROTHERMOPHILUS; ISOTOPE LABELING; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; AMINOACYLATION; BIOLOGICAL MODEL; CHEMICAL STRUCTURE; ENZYMOLOGY; KINETICS; METABOLISM; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE;

GEOBACILLUS STEAROTHERMOPHILUS;

AMINOACYLATION; BACILLUS STEAROTHERMOPHILUS; DIPHOSPHATES; ENZYME ACTIVATION; KINETICS; MODELS, BIOLOGICAL; MODELS, MOLECULAR; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; TYROSINE; TYROSINE-TRNA LIGASE;

EID: 45149108596     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M801649200     Document Type: Article

References (45)

1. Fersht, A. R., Knill-Jones, J. W., Bedouelle, H., and Winter, G. (1988) Biochemistry 27, 1581-1587
2. Avis, J. M., Day, A. G., Garcia, G. A., and Fersht, A. R. (1993) Biochemistry 32, 5312-5320
3. Fersht, A. R., Mulvey, R. S., and Koch, G. L. (1975) Biochemistry 14, 13-18
4. Calendar, R., and Berg, P. (1966) Biochemistry 5, 1690-1695
5. Calendar, R., and Berg, P. (1967) J. Mol. Biol. 26, 39-54
6. Soutourina, J., Blanquet, S., and Plateau, P. (2000) J. Biol. Chem. 275, 11626-11630
7. Soutourina, O., Soutourina, J., Blanquet, S., and Plateau, P. (2004) J. Biol. Chem. 279, 42560-42565
8. Kleeman, T. A., Wei, D., Simpson, K. L., and First, E. A. (1997) J. Biol. Chem. 272, 14420-14425
9. Wakasugi, K., Quinn, C. L., Tao, N., and Schimmel, P. (1998) EMBO J. 17, 297-305
10. Wang, L., Brock, A., Herberich, B., and Schultz, P. G. (2001) Science 292, 498-500
11. First, E. A., and Fersht, A. R. (1993) Biochemistry 32, 13658-13663
12. First, E. A., and Fersht, A. R. (1993) Biochemistry 32, 13651-13657
13. First, E. A., and Fersht, A. R. (1993) Biochemistry 32, 13644-13650
14. First, E. A., and Fersht, A. R. (1995) Biochemistry 34, 5030-5043
15. Jones, D. H., McMillan, A. J., Fersht, A. R., and Winter, G. (1985) Biochemistry 24, 5852-5857
16. Fersht, A. R., Wilkinson, A. J., Carter, P., and Winter, G. (1985) Biochemistry 24, 5858-5861
17. Gibson, T. (1984) Studies on the Epstein-Barr Virus Genome. Ph.D. thesis, University of Cambridge, Cambridge, UK
18. Wilkinson, A. J., Fersht, A. R., Blow, D. M., and Winter, G. (1983) Biochemistry 22, 3581-3586
19. Appel, R. D., Bairoch, A., and Hochstrasser, D. F. (1994) Trends Biochem. Sci. 19, 258-260
20. Xin, Y., Li, W., and First, E. A. (2000) Biochemistry 39, 340-347
21. Uter, N. T., Gruic-Sovulj, I., and Perona, J. J. (2005) J. Biol. Chem. 280, 23966-23977
22. Fersht, A. R. (1975) Biochemistry 14, 5-12
23. Scatchard, G. (1948) Ann. N. Y. Acad. Sci. 51, 660-672
24. Langmuir, I. (1916) J. Am. Chem. Soc. 38, 2221-2295
25. Clarke, A. R. (1996) in Enzymology Labfax (Engel, P., ed) 1st Ed., pp. 201-205, Academic Press, New York
26. Wells, T. N., and Fersht, A. R. (1986) Biochemistry 25, 1881-1886
27. Ho, C. K., and Fersht, A. R. (1986) Biochemistry 25, 1891-1897
28. Fersht, A. R., Leatherbarrow, R. J., and Wells, T. N. (1987) Biochemistry 26, 6030-6038
29. Santi, D. V., and Pena, V. A. (1971) FEBS Lett. 13, 157-160
30. Brick, P., and Blow, D. M. (1987) J. Mol. Biol. 194, 287-297
31. Retailleau, P., Huang, X., Yin, Y., Hu, M., Weinreb, V., Vachette, P., Vonrhein, C., Bricogne, G., Roversi, P., Ilyin, V., and Carter, C. W., Jr. (2003) J. Mol. Biol. 325, 39-63
32. Collaborative Computational Project, No 4. (1994) Acta Crystallogr. 50, 760-763
33. Emsley, P., and Cowtan, K. (2004) Acta Crystallogr. 60, 2126-2132
34. Kabsch, W. (1976) Acta Crystallogr. Sect. A 32, 922-923
35. Morris, G. M., Goodsell, D. S., Halliday, R. S., Huey, R., Hart, W. E., Belew, R. K., and Olson, A. J. (1998) J. Comput. Chem. 19, 1639-1662
36. Davis, I. W., Leaver-Fay, A., Chen, V. B., Block, J. N., Kapral, G. J., Wang, X., Murray, L. W., Arendall, W. B., III, Snoeyink, J., Richardson, J. S., and Richardson, D. C. (2007) Nucleic Acids Res. 35, W375-W383
37. Doublie, S., Bricogne, G., Gilmore, C., and Carter, C. W., Jr. (1995) Structure (Lond.) 3, 17-31
38. Soutourina, J., Plateau, P., and Blanquet, S. (2000) J. Biol. Chem. 275, 32535-32542
39. Jakubowski, H., and Goldman, E. (1992) Microbiol. Rev. 56, 412-429
40. Asahara, H., and Uhlenbeck, O. C. (2005) Biochemistry 44, 11254-11261
41. Thompson, D., Lazennec, C., Plateau, P., and Simonson, T. (2007) J. Biol. Chem. 282, 30856-30868
42. Lin, S. X., Baltzinger, M., and Remy, P. (1983) Biochemistry 22, 681-689
43. Tsui, W. C., and Fersht, A. R. (1981) Nucleic Acids Res. 9, 4627-4637
44. Delano, W. L. (2002) The PyMol Molecular Graphics System, Delano Scientific, Palo Alto, CA
45. Sheoran, A., and First, E. A. (2008) J. Biol. Chem. 283, 12971-12980