Probing the transition-state structure of dual-specificity protein phosphatases using a physiological substrate mimic

Biochemistry

Volumn 43, Issue 27, 2004, Pages 8807-8814

  Grzyska, Piotr K ^a   Kim, Youngjoo ^b   Jackson, Michael D ^b   Hengge, Alvan C ^a   Denu, John M ^c,d  

^a UTAH STATE UNIVERSITY   (United States)

^b OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

^c UNIVERSITY OF WISCONSIN MADISON   (United States)

^d UNIVERSITY OF WISCONSIN SCHOOL OF MEDICINE AND PUBLIC HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHARGE TRANSFER; CRYSTAL STRUCTURE; ENZYME KINETICS; HYDROLYSIS; PHYSIOLOGY; SUBSTRATES;

MUTANTS; PROTONATION; TRANSITION STATES;

BIOCHEMISTRY;

ALKALINE PHOSPHATASE; DEUTERIUM OXIDE; ORGANOPHOSPHATE; OXYGEN 18; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHOSERINE; PHOSPHOTHREONINE; PHOSPHOTYROSINE; PROTEIN TYROSINE PHOSPHATASE; PROTON;

ARTICLE; CATALYSIS; CHEMICAL STRUCTURE; CHICKEN; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; HYDROLYSIS; MICHAELIS MENTEN KINETICS; NONHUMAN; PHOSPHORUS NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; SPLEEN;

ANILINE COMPOUNDS; ANIMALS; CATALYSIS; CHICKENS; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR MIMICRY; MOLECULAR STRUCTURE; ORGANOPHOSPHORUS COMPOUNDS; PHASE TRANSITION; PHOSPHOPROTEIN PHOSPHATASE; SUBSTRATE SPECIFICITY;

GALLUS GALLUS;

EID: 3042854194     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049473z     Document Type: Article

References (35)

1. Kirby, A. J., and Varvoglis, A. G. (1967) J. Am. Chem. Soc. 89, 415-423.
2. Cleland, W. W., and Hengge, A. C. (1995) Mechanisms of phosphoryl and acyl transfer, FASEB J. 15, 1585-1594.
3. Keyse, S. M. (2000) Protein phosphatases and the regulation of mitogen-activated protein kinase signalling, Curr. Opin. Cell Biol. 12, 186-192.
4. Neel, B. G., and Tonks, N. K. (1997) Protein tyrosine phosphatases in signal transduction, Curr. Opin. Cell Biol. 9, 193-204.
5. Tonks, N. K., and Neel, B. G. (2001) Combinatorial control of the specificity of protein tyrosine phosphatases, Curr. Opin. Cell Biol. 13, 182-195.
6. Denu, J. M., and Dixon, J. E. (1998) Protein tyrosine phosphatases: Mechanisms of catalysis and regulation, Curr. Opin. Chem. Biol. 2, 633-641.
7. Pannifer, A. D., Flint, A. J., Tonks, N. K., and Barford, D. (1998) Visualization of the cysteinyl-phosphate intermediate of a protein-tyrosine phosphatase by X-ray crystallography, J. Biol. Chem. 273, 10454-10462.
8. Denu, J. M., Lohse, D. L., Vijayalakshmi, J., Saper, M. A., and Dixon, J. E. (1996) Visualization of intermediate and transition-state structures in protein-tyrosine phosphatase catalysis, Proc. Natl. Acad. Sci. U.S.A. 93, 2493-2498.
9. Denu, J. M., and Dixon, J. E. (1995) A catalytic mechanism for the dual-specific phosphatases, Proc. Natl. Acad. Sci. U.S.A. 92, 5910-5914.
10. Lohse, D. L., Denu, J. M., Santoro, N., and Dixon, J. E. (1997) Roles of aspartic acid-181 and serine-222 in intermediate formation and hydrolysis of the mammalian protein-tyrosine-phosphatase PTP1, Biochemistry 36, 4568-4575.
11. Zhang, Z. Y., Wang, Y., and Dixon, J. E. (1994) Dissecting the catalytic mechanism of protein-tyrosine phosphatases, Proc. Natl. Acad. Sci. U.S.A. 91, 1624-1627.
12. Denu, J. M., Zhou, G., Guo, Y., and Dixon, J. E. (1995) The catalytic role of aspartic acid-92 in a human dual-specific protein-tyrosine-phosphatase, Biochemistry 34, 3396-3403.
13. Hengge, A. C., Denu, J. M., and Dixon, J. E. (1996) Transition-state structures for the native dual-specific phosphatase VHR and D92N and S131A mutants. Contributions to the driving force for catalysis, Biochemistry 35, 7084-7092.
14. Zhang, Z.-Y., Wu, L., and Chen, L. (1995) Transition state and rate-limiting step of the reaction catalyzed by the human dual-specificity phosphatase, VHR, Biochemistry 34, 16088-16096.
15. Grzyska, P. K., Czyryca, P. G., Purcell, J., and Hengge, A. C. (2003) Hydrolysis reactions of alkyl versus aryl phosphate monoester monoanions, J. Am. Chem. Soc. 125, 13106-13111.
16. 2-, J. Phys. Chem. 106, 6521-6526.
17. Ames, N. A., and Dubin, D. T. (1960) The role of polyamine in the neutralization of bacteriophage deoxyribonucleic acid, J. Biol. Chem. 235, 769-775.
18. Hengge, A. C. (2002) Isotope effects in the study of phosphoryl and sulfuryl transfer reactions, Acc. Chem. Res. 35, 105-112.
19. Bigeleisen, J., and Wolfsberg, M. (1958) Theoretical and experimental aspects of isotope effects in chemical kinetics, Adv. Chem. Phys. 1, 15-76.
20. Schowen, K. B., and Schowen, R. L. (1982) Solvent isotope effects of enzyme systems, Methods Enzymol. 87, 551-606.
21. Zhang, Z.-Y., Malachowski, W. P., Van Etten, R. L., and Dixon, J. E. (1994) Nature of the rate-determining steps of the reaction catalyzed by the Yersinia protein-tyrosine phosphatase, J. Biol. Chem. 269, 8140-8145.
22. Kolmodin, K., Nordlund, P., and Aqvist, J. (1999) Mechanism of substrate dephosphorylation in low Mr protein tyrosine phosphatase, Proteins: Struct., Funct., Genet. 36, 370-379.
23. Hart, J. C., Hillier, I. H., Burton, N. A., and Sheppard, D. W. (1998) An alternative role for the conserved Asp residue in phosphoryl transfer reactions, J. Am. Chem. Soc. 120, 13535-13536.
24. Asthagiri, D., Dillet, V., Liu, T., Noodleman, L., Van Etten, R. L., and Bashford, D. (2002) Density functional study of the mechanism of a tyrosine phosphatase: I. Intermediate formation, J. Am. Chem. Soc. 124, 10225-10235.
25. 18O isotope effects on the deprotonation of phosphate and phosphate esters and the anomeric effect on deprotonation of glucose-6-phosphate, J. Am. Chem. Soc. 108, 2759-2761.
26. Lad, C., Williams, N. H., and Wolfenden, R. (2003) The rate of hydrolysis of phosphomonoester dianions and the exceptional catalytic proficiencies of protein and inositol phosphatases, Proc. Natl. Acad. Sci. U.S.A. 100, 5607-5610.
27. 18O, J. Am. Chem. Soc. 95, 7375-7381.
28. 2O exchange reaction, J. Phys. Chem. 67, 1565-1566.
29. 18O equilibrium isotope effects and fractionation factors, Can. J. Chem. 77, 967-977.
30. Hengge, A. C., and Hess, R. A. (1994) Concerted or stepwise mechanisms for acyl transfer reactions of p-nitrophenyl acetate? Transition state structures from isotope effects, J. Am. Chem. Soc. 116, 11256-11263.
31. Melander, L., and Saunders, W. H. (1987) Reaction Rates of Isotopic Molecules, pp 130-139, Robert E. Krieger, Malabar, FL.
32. Quinn, D. M., and Sutton, L. D. (1991) in Enzyme Mechanism from Isotope Effects (Cook, P. F., Ed.) pp 73-126, CRC Press, Boca Raton, FL.
33. Fife, T. H. (1972) General acid catsalysis of acetal, ketal, and ortho ester hydrolysis, Acc. Chem. Res. 5, 264-272.
34. Jencks, W. P. (1987) Catalysis in Chemistry and Enzymology, Dover Publications, Inc, New York.
35. Kresge, A. J., and Preto, R. J. (1965) The mechanism of hydrolysis of ortho esters, J. Am. Chem. Soc. 87, 4593.