Characterization of isoleucyl-tRNA synthetase from Staphylococcus aureus: I: Kinetic mechanism of the substrate activation reaction studied by transient and steady-state techniques

Journal of Biological Chemistry

Volumn 273, Issue 48, 1999, Pages 31680-31690

  Pope, Andrew J ^a   Lapointe, Jacques ^b   Mensah, Lucy ^a   Benson, Neil ^a   Brown, Murray J B ^a   Moore, Keith J ^a  

^a GLAXOSMITHKLINE   (United Kingdom)

^b UNIVERSITÉ LAVAL   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; ENZYME INHIBITOR; ISOLEUCINE; ISOLEUCINE TRANSFER RNA LIGASE;

AMINOACYLATION; ARTICLE; BINDING AFFINITY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME KINETICS; ENZYME SUBSTRATE COMPLEX; FLUORESCENCE ANALYSIS; NONHUMAN; PRIORITY JOURNAL; REACTION ANALYSIS; SIMULATION; STAPHYLOCOCCUS AUREUS;

ADENOSINE TRIPHOSPHATE; BINDING SITES; BINDING, COMPETITIVE; ISOLEUCINE; ISOLEUCINE-TRNA LIGASE; KINETICS; MODELS, CHEMICAL; SPECTROMETRY, FLUORESCENCE; STAPHYLOCOCCUS AUREUS;

BACTERIA (MICROORGANISMS); FELIS CATUS; STAPHYLOCOCCUS AUREUS;

EID: 0033610808     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.48.31680     Document Type: Article

References (24)

1. Meinnel, T., Mechulam, Y., and Blanquet, S. (1995) in tRNA, Structure, Biosynthesis and Function (Soll, D., and RajBhandary, U. L., eds) pp. 251-292, ASM Press, Washington, D. C.
2. Eriani, G., Delarue, M., Poch, O., Gangloff, J., and Moras, D. (1990) Nature 347, 203-206
3. Lamour, V., Quevillon, S., Diriong, S., N'Guyen, V. C., Lipinski, M., and Mirande, M. (1994) Proc. Natl. Acad. Sci. U. S. A. 91, 8670-8674
4. Rauhut, R., Gabius, H-J., and Cramer, F. (1986) Biosystems 19, 173-183
5. Nagel, G. M., and Doolittle, R. F. (1995) J. Mol. Evol. 40, 487-498
6. Carter, C. W., Jr. (1993) Annu. Rev. Biochem. 62, 715-748
7. Hughes, J., and Mellows, G. (1978) J. Antibiot. 31, 330-335
8. Hughes, J., and Mellows, G. (1980) Biochem. J. 191, 209-219
9. Dyke, K. G. H., Curnock, S. P., Golding, M., and Noble, W. C. (1991) FEMS Microbiol. Lett. 77, 195-198
10. Farmer, T. H., Gilbart, J., and Elson, S. (1992) J. Antimicrobial Chemotherapy 30, 587-596
11. Chalker, A., Ward, J., Fosberry, A., and Hodgson, J. (1994) Gene (Amst.) 141, 103-108
12. Pope, A. J., Moore, K. J., McVey, M., Mensah, L., Benson, N., Osbourne, N., Broom, N., Brown, M. J. B., and O'Hanlon, P. (1998) J. Biol. Chem. 273, 31691-31701
13. Pope, A. J., McVey, M., Fantom, K., and Moore, K. J. (1998) J. Biol. Chem. 273, 31702-31706
14. Fersht, A. R. (1984) Enzyme Structure and Mechanism, W. H. Freeman & Co., New York
15. Calendar, R., and Berg, P. (1966) Biochemistry 5, 1681-1690
16. Leatherbarrow, R. J. (1992) Grafit, Version 3.0, Erithacus Software Ltd., Staines, UK
17. Barshop, B. A., Wrenn, R. F., and Freiden, C. (1983) Anal. Biochem. 130, 134-145
18. Mendes, P. (1993) Comput. Appl. Biosci. 9, 563-571
19. Mendes, P. (1997) Trends Biochem. Sci. 22, 361-363
20. Gutfreund, H. (1995) Kinetics for the Life Sciences, Cambridge University Press, Cambridge, UK
21. Moore K. J., and Lohman, T. M. (1994) Biochemistry 33, 14565-14578
22. Moe, J. G., and Piszkiewicz, D. (1979) Biochemistry 18, 2804-2810
23. Segal, I. H. (1975) Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-state Enzyme Systems, John WileySons, New York
24. Cleland, W. W. (1970) in The Enzymes (Boyer, P. D., ed) pp. 1-61, Academic Press, New York