Electrostatic interactions dominate the catalytic contribution of Arg39 in 4-oxalocrotonate tautomerase

Journal of the American Chemical Society

Volumn 126, Issue 40, 2004, Pages 12726-12727

  Metanis, Norman ^a,b   Brik, Ashraf ^a,b   Dawson, Philip E ^b   Keinan, Ehud ^a,b  

^a TECHNION ISRAEL INSTITUTE OF TECHNOLOGY   (Israel)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

4 OXALOCROTONATE TAUTOMERASE; ARGININE; CITRULLINE; ENZYME; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ELECTRICITY; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; ENZYME SYNTHESIS; HYDROGEN BOND; KINETICS; MOLECULAR STABILITY; MUTATION; PROTON TRANSPORT; SURFACE CHARGE;

EID: 5644246078     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja0463841     Document Type: Article

References (23)

1. Whitman, C. P. Arch. Biochem. Biophys. 2002, 402, 1-13.
2. Whitman, C. P.; Arid, B. A.; Gillespie, W. R.; Stolowich, N. J. J. Am. Chem. Soc. 1991, 113, 3154-3162 and references therein.
3. Chen, L. H.; Kenyon, G. L.; Curtin, F.; Harayama, S.; Bembenek, M. E.; Hajipour, G.; Whitman, C. P. J. Biol. Chem. 1992, 207, 17716-17721.
4. Harris, T. K.; Czerwinski, R. M.; Johnson, W. H., Jr.; Legier, P. M.; Abeygunawardana, C.; Massiah, M. A.; Stivers, J. T.; Whitman, C. P.; Mildvan, A. S. Biochemistry 1999, 38, 12343-12357.
5. Lian, H.; Whitman, C. P. J. Am. Chem. Soc. 1993, 115, 7978-7984.
6. Taylor, A. B.; Czerwinski, R. M.; Johnson, W. H., Jr.; Whitman, C. P.; Hackert, M. L. Biochemistry 1998, 37, 14692-14700.
7. Stivers, J. T.; Abeygunawardana, C.; Mildvan, A. S.; Hajipour, G.; Whitman, C. P.; Chen, L. H. Biochemistry 1996, 35, 803-813.
8. Czerwinski, R. M.; Johnson, W. H., Jr.; Whitman, C. P.; Harris, T. K.; Abeygunawardana, C.; Mildvan, A. S. Biochemistry 1997, 36, 14551-14560.
9. (a) Luo, S.; Martin, B. L.; Senshu, T.; Graves, D. J. Arch. Biochim. Biophys. 1995, 318, 362-369.
10. Kienhöfer, A.; Kast, P.; Hilvert, D. J. Am. Chem. Soc. 2003, 125, 3206-3207.
11. (c) Jantz, D.; Berg, J. M. J. Am. Chem. Soc. 2003, 125, 4960-4961.
12. Li, G.; Cui, Q. J. Am. Chem. Soc. 2003, 125, 15028-15038.
13. (a) Kent, S. B. H. Annu. Rev. Biochem. 1988, 57, 957-989.
14. (b) Dawson, P. E.; Kent, S. B. H. Annu. Rev. Biochem. 2000, 69, 923-960.
15. (c) Fitzgerald, M. C.; Chernushevich, I.; Standing, K. G.; Kent, S. B. H.; Whitman, C. P. J. Am. Chem. Soc. 1995, 117, 11075-11080.
16. Fitzgerald, M. C.; Chernushevich, I.; Standing, K. G.; Kent, S. B. H.; Whitman, C. P. Proc. Natl. Acad. Sci., U.S.A. 1996, 93, 6851-6856.
17. Standard assay conditions were used for all enzymes (20 mM sodium phosphate buffer, pH 7.38) following the appearance rate of 3 at 236 nm and calculating the kinetic parameters by nonlinear regression analysis as shown in ref 2.
18. -1 observed in ref 9b.
19. -1.
20. Mildvan, A. S.; Weber, D. J.; Kuliopulos, A. Arch. Biochem. Biophys. 1992, 294, 327-340.
21. Cisnêros, G. A.; Liu, H.; Zhang, Y.; Yang, W. J. Am. Chem. Soc. 2003, 125, 10384-10393.
22. (a) Brik, A.; D'Souza, L. J.; Keinan, E.; Grynszpan, F.; Dawson, P. E. ChemBioChem 2002, 3, 845-851.
23. (b) Brik, A.; Dawson, P. E.; Keinan, E. Bioorg. Med. Chem. 2002, 10, 3891-3897.