메뉴 건너뛰기




Volumn 43, Issue 25, 2004, Pages 8256-8264

Mechanistic studies of protein tyrosine phosphatases YopH and Cdc25A with m-nitrobenzyl phosphate

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CHEMICAL BONDS; ENZYME KINETICS; ENZYMES; HYDROLYSIS; ISOTOPES; PHYSIOLOGY; PROTONS;

EID: 3042610043     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0496182     Document Type: Article
Times cited : (18)

References (38)
  • 1
    • 0038286174 scopus 로고    scopus 로고
    • The rate of hydrolysis of phosphomonoester dianions and the exceptional catalytic proficiencies of protein and inositol phosphatases
    • 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.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 5607-5610
    • Lad, C.1    Williams, N.H.2    Wolfenden, R.3
  • 2
    • 2542559631 scopus 로고    scopus 로고
    • Mechanistic studies on protein tyrosine phosphatases
    • Zhang, Z.-Y. (2003) Mechanistic studies on protein tyrosine phosphatases, Prog. Nucleic Acid Res. Mol. Biol. 73, 171-220.
    • (2003) Prog. Nucleic Acid Res. Mol. Biol. , vol.73 , pp. 171-220
    • Zhang, Z.-Y.1
  • 3
    • 0028871944 scopus 로고
    • Nature of the transition state of the protein-tyrosine phosphatase-catalyzed reaction
    • Hengge, A. C., Sowa, G., Wu, L., and Zhang, Z.-Y. (1995) Nature of the transition state of the protein-tyrosine phosphatase-catalyzed reaction, Biochemistry 34, 13982-13987.
    • (1995) Biochemistry , vol.34 , pp. 13982-13987
    • Hengge, A.C.1    Sowa, G.2    Wu, L.3    Zhang, Z.-Y.4
  • 4
    • 0029994512 scopus 로고    scopus 로고
    • Transition-state structures for the native dual-specific phosphatase VHR and D92N and S131A mutants. Contributions to the driving force for catalysis
    • 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.
    • (1996) Biochemistry , vol.35 , pp. 7084-7092
    • Hengge, A.C.1    Denu, J.M.2    Dixon, J.E.3
  • 5
    • 0030804063 scopus 로고    scopus 로고
    • Examination of the transition state of the low-molecular mass tyrosine phosphatase 1. Comparisons with other protein phosphatases
    • Hengge, A. C., Zhao, Y., Wu, L., and Zhang, Z.-Y. (1997) Examination of the transition state of the low-molecular mass tyrosine phosphatase 1. Comparisons with other protein phosphatases, Biochemistry 36, 7928-7936.
    • (1997) Biochemistry , vol.36 , pp. 7928-7936
    • Hengge, A.C.1    Zhao, Y.2    Wu, L.3    Zhang, Z.-Y.4
  • 6
    • 0035836486 scopus 로고    scopus 로고
    • Transition state analysis and requirement of Asp-262 general acid/base catalyst for full activation of dual-specificity phosphatase MKP3 by extracellular regulated kinase
    • Rigas, J. D., Hoff, R. H., Rice, A. E., Hengge, A. C., and Denu, J. M. (2001) Transition state analysis and requirement of Asp-262 general acid/base catalyst for full activation of dual-specificity phosphatase MKP3 by extracellular regulated kinase, Biochemistry 40, 4398-4406.
    • (2001) Biochemistry , vol.40 , pp. 4398-4406
    • Rigas, J.D.1    Hoff, R.H.2    Rice, A.E.3    Hengge, A.C.4    Denu, J.M.5
  • 8
    • 33947333789 scopus 로고
    • The reactivity of phosphate esters. Monoester hydrolysis
    • Kirby, A. J., and Varvoglis, A. G. (1967) The reactivity of phosphate esters. monoester hydrolysis, J. Am. Chem. Soc. 89, 415-423.
    • (1967) J. Am. Chem. Soc. , vol.89 , pp. 415-423
    • Kirby, A.J.1    Varvoglis, A.G.2
  • 9
    • 0142152414 scopus 로고    scopus 로고
    • Transition state differences in hydrolysis reactions of alkyl versus aryl phosphate monoester monoanions
    • Grzyska, P. K., Czyryca, P. G., Purcell, J., and Hengge, A. C. (2003) Transition state differences in hydrolysis reactions of alkyl versus aryl phosphate monoester monoanions, J. Am. Chem. Soc. 125, 13106-13111.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13106-13111
    • Grzyska, P.K.1    Czyryca, P.G.2    Purcell, J.3    Hengge, A.C.4
  • 10
    • 0029005759 scopus 로고
    • Are protein-tyrosine phosphatases specific for phosphotyrosine?
    • Zhang, Z.-Y. (1995) Are protein-tyrosine phosphatases specific for phosphotyrosine? J. Biol. Chem. 270, 16052-16055.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16052-16055
    • Zhang, Z.-Y.1
  • 11
    • 0028858055 scopus 로고
    • Transition state and rate-limiting step of the reaction catalyzed by the human dual specificity phosphatase, VHR
    • 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.
    • (1995) Biochemistry , vol.34 , pp. 16088-16096
    • Zhang, Z.-Y.1    Wu, L.2    Chen, L.3
  • 12
    • 0142180154 scopus 로고    scopus 로고
    • Aurintricarboxylic acid blocks in vitro and in vivo activity of YopH, an essential virulent factor of Yersinia pestis, the agent of plague
    • Liang, F., Huang, Z., Lee, S.-Y., Liang, J., Ivanov, M. I., Alonso, A., Bliska, J. B., Lawrence, D. S., Mustelin, T., and Zhang, Z.-Y. (2003) Aurintricarboxylic acid blocks in vitro and in vivo activity of YopH, an essential virulent factor of Yersinia pestis, the agent of plague, J. Biol. Chem. 278, 41734-41741.
    • (2003) J. Biol. Chem. , vol.278 , pp. 41734-41741
    • Liang, F.1    Huang, Z.2    Lee, S.-Y.3    Liang, J.4    Ivanov, M.I.5    Alonso, A.6    Bliska, J.B.7    Lawrence, D.S.8    Mustelin, T.9    Zhang, Z.-Y.10
  • 13
    • 0028176050 scopus 로고
    • Dissecting the catalytic mechanism of protein tyrosine phosphatases
    • 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.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 1624-1627
    • Zhang, Z.-Y.1    Wang, Y.2    Dixon, J.E.3
  • 14
    • 0028239771 scopus 로고
    • The nature of the rate-determining steps of the Yersinia protein tyrosine phosphatase-catalyzed reactions
    • Zhang, Z.-Y., Malachowski, W. P., Van Etten, R. L., and Dixon, J. E. (1994) The nature of the rate-determining steps of the Yersinia protein tyrosine phosphatase-catalyzed reactions, J. Biol. Chem. 269, 8140-8145.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8140-8145
    • Zhang, Z.-Y.1    Malachowski, W.P.2    Van Etten, R.L.3    Dixon, J.E.4
  • 15
    • 0027058169 scopus 로고
    • Expression, purification, and physicochemical characterization of a recombinant Yersinia protein tyrosine phosphatase
    • Zhang, Z.-Y., Clemens, J. C., Schubert, H. L., Stuckey, J. A., Fischer, M. W. F., Hume, D. M., Saper, M. A., and Dixon, J. E. (1992) Expression, purification, and physicochemical characterization of a recombinant Yersinia protein tyrosine phosphatase, J. Biol. Chem. 267, 23759-23766.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23759-23766
    • Zhang, Z.-Y.1    Clemens, J.C.2    Schubert, H.L.3    Stuckey, J.A.4    Fischer, M.W.F.5    Hume, D.M.6    Saper, M.A.7    Dixon, J.E.8
  • 16
    • 0021077311 scopus 로고
    • Inorganic phosphate determination in the presence of a labile organic phosphate: Assay for carbamyl phosphate phosphatase activity
    • Black, M. J., and Jones, M. E. (1983) Inorganic phosphate determination in the presence of a labile organic phosphate: assay for carbamyl phosphate phosphatase activity, Anal. Biochem. 135, 233-238.
    • (1983) Anal. Biochem. , vol.135 , pp. 233-238
    • Black, M.J.1    Jones, M.E.2
  • 17
    • 0036177176 scopus 로고    scopus 로고
    • Isotope effects in the study of phosphoryl and sulfuryl transfer reactions
    • Hengge, A. C. (2002) Isotope effects in the study of phosphoryl and sulfuryl transfer reactions, Acc. Chem. Res. 35, 105-112.
    • (2002) Acc. Chem. Res. , vol.35 , pp. 105-112
    • Hengge, A.C.1
  • 18
    • 0025945823 scopus 로고
    • Evidence for protein-tyrosine phosphatase catalysis proceeding via a cysteine-phosphate intermediate
    • Guan, K. L., and Dixon, J. E. (1991) Evidence for protein-tyrosine phosphatase catalysis proceeding via a cysteine-phosphate intermediate, J. Biol. Chem. 266, 17026-17030.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17026-17030
    • Guan, K.L.1    Dixon, J.E.2
  • 19
    • 0000630849 scopus 로고
    • Isolation and structural elucidation of a novel phosphocysteine intermediate in the LAR protein tyrosine phosphatase enzymatic pathway
    • Cho, H., Krishnaraj, R., Kitas, E., Bannwarth, W., Walsh, C. T., and Anderson, K. S. (1992) Isolation and structural elucidation of a novel phosphocysteine intermediate in the LAR protein tyrosine phosphatase enzymatic pathway, J. Am. Chem. Soc. 114, 7296-7298.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 7296-7298
    • Cho, H.1    Krishnaraj, R.2    Kitas, E.3    Bannwarth, W.4    Walsh, C.T.5    Anderson, K.S.6
  • 20
    • 0028903589 scopus 로고
    • The catalytic role of aspartic acid-92 in a human dual-specific protein-tyrosine-phosphatase
    • 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.
    • (1995) Biochemistry , vol.34 , pp. 3396-3403
    • Denu, J.M.1    Zhou, G.2    Guo, Y.3    Dixon, J.E.4
  • 22
    • 0033554393 scopus 로고    scopus 로고
    • Impaired transition state complementarity in the hydrolysis of O-arylphosphorothioates by protein-tyrosine phosphatases
    • Zhang, Y.-L., Hollfelder, F., Gordon, S. J., Chen, L., Keng, Y.-F., Wu, L., Herschlag, D., and Zhang, Z.-Y. (1999) Impaired transition state complementarity in the hydrolysis of O-arylphosphorothioates by protein-tyrosine phosphatases, Biochemistry 38, 12111-12123.
    • (1999) Biochemistry , vol.38 , pp. 12111-12123
    • Zhang, Y.-L.1    Hollfelder, F.2    Gordon, S.J.3    Chen, L.4    Keng, Y.-F.5    Wu, L.6    Herschlag, D.7    Zhang, Z.-Y.8
  • 23
    • 0032731882 scopus 로고    scopus 로고
    • Does positive charge at the active site of a phosphatase cause a change in mechanism? The effect of the conserved arginine on the transition state for enzymatic phosphoryl transfer in the protein-tyrosine phosphatase from Yersinia
    • Hoff, R. H., Wu, L., Zhou, B., Zhang, Z.-Y., and Hengge, A. C. (1999) Does positive charge at the active site of a phosphatase cause a change in mechanism? The effect of the conserved arginine on the transition state for enzymatic phosphoryl transfer in the protein-tyrosine phosphatase from Yersinia, J. Am. Chem. Soc. 121, 9514-9521.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 9514-9521
    • Hoff, R.H.1    Wu, L.2    Zhou, B.3    Zhang, Z.-Y.4    Hengge, A.C.5
  • 24
    • 0030888923 scopus 로고    scopus 로고
    • 18O isotope effects support a concerted mechanism for ribonuclease A
    • 18O isotope effects support a concerted mechanism for ribonuclease A, J. Am. Chem. Soc. 119, 2319-2320.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 2319-2320
    • Sowa, G.A.1    Hengge, A.C.2    Cleland, W.W.3
  • 25
    • 0034609567 scopus 로고    scopus 로고
    • Dual-specific Cdc25B phosphatase: In search of the catalytic acid
    • Chen, W., Wilborn, M., and Rudolph, J. (2000) Dual-specific Cdc25B phosphatase: in search of the catalytic acid, Biochemistry 39, 10781-10789.
    • (2000) Biochemistry , vol.39 , pp. 10781-10789
    • Chen, W.1    Wilborn, M.2    Rudolph, J.3
  • 26
    • 0030028068 scopus 로고    scopus 로고
    • The active-site specificity of the Yersinia protein-tyrosine phosphatase
    • Dunn, D., Chen, L., Lawrence, D. S., and Zhang, Z.-Y. (1996) The active-site specificity of the Yersinia protein-tyrosine phosphatase, J. Biol. Chem. 271, 168-173.
    • (1996) J. Biol. Chem. , vol.271 , pp. 168-173
    • Dunn, D.1    Chen, L.2    Lawrence, D.S.3    Zhang, Z.-Y.4
  • 27
    • 0029015718 scopus 로고
    • Kinetic and mechanistic characterization of a mammalian protein tyrosine phosphatase, PTP1
    • Zhang, Z.-Y. (1995) Kinetic and mechanistic characterization of a mammalian protein tyrosine phosphatase, PTP1, J. Biol. Chem. 270, 11199-11204.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11199-11204
    • Zhang, Z.-Y.1
  • 28
    • 0032577020 scopus 로고    scopus 로고
    • Walden-inversion enforced transition state stabilization in a protein tyrosine phosphatase
    • Alhambra, C., Wu, L., Zhang, Z.-Y., and Gao, J. (1998) Walden-inversion enforced transition state stabilization in a protein tyrosine phosphatase, J. Am. Chem. Soc. 120, 3858-3866.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 3858-3866
    • Alhambra, C.1    Wu, L.2    Zhang, Z.-Y.3    Gao, J.4
  • 29
    • 0035844731 scopus 로고    scopus 로고
    • The mechanism of the phosphoryl transfer catalyzed by Yersinia protein-tyrosine phosphatase: A computational and isotope effect study
    • Czyryca, P. G., and Hengge, A. C. (2001) The mechanism of the phosphoryl transfer catalyzed by Yersinia protein-tyrosine phosphatase: a computational and isotope effect study, Biochim. Biophys. Acta 1547, 245-253.
    • (2001) Biochim. Biophys. Acta , vol.1547 , pp. 245-253
    • Czyryca, P.G.1    Hengge, A.C.2
  • 30
    • 0032489458 scopus 로고    scopus 로고
    • Altering the nucleophile specificity of a protein-tyrosine phosphatase-catalyzed reaction: Probing the function of the invariant glutamine residues
    • Zhao, Y., Wu, L., Noh, S. J., Guan, K.-L., and Zhang, Z.-Y. (1998) Altering the nucleophile specificity of a protein-tyrosine phosphatase-catalyzed reaction: probing the function of the invariant glutamine residues, J. Biol. Chem. 273, 5484-5492.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5484-5492
    • Zhao, Y.1    Wu, L.2    Noh, S.J.3    Guan, K.-L.4    Zhang, Z.-Y.5
  • 31
    • 0034635121 scopus 로고    scopus 로고
    • The Effects on General Acid Catalysis from Mutations of the Invariant Tryptophan and Arginine Residues in the Protein-Tyrosine Phosphatase from Yersinia
    • Hoff, R. H., Hengge, A. C., Wu, L., Keng, Y.-F., and Zhang, Z.-Y. (2000) The Effects on General Acid Catalysis from Mutations of the Invariant Tryptophan and Arginine Residues in the Protein-Tyrosine Phosphatase from Yersinia, Biochemistry 39, 46-54.
    • (2000) Biochemistry , vol.39 , pp. 46-54
    • Hoff, R.H.1    Hengge, A.C.2    Wu, L.3    Keng, Y.-F.4    Zhang, Z.-Y.5
  • 32
    • 0029620544 scopus 로고
    • Mechanisms of phosphoryl and acyl transfer
    • Cleland, W. W., and Hengge, A. C. (1995) Mechanisms of phosphoryl and acyl transfer, FASEB J. 9, 1585-1594.
    • (1995) FASEB J. , vol.9 , pp. 1585-1594
    • Cleland, W.W.1    Hengge, A.C.2
  • 33
    • 0001158302 scopus 로고
    • Transition-state structures for phosphoryl-transfer reactions of p-nitrophenyl phosphate
    • Hengge, A. C., Edens, W. A., and Elsing, H. (1994) Transition-state structures for phosphoryl-transfer reactions of p-nitrophenyl phosphate, J. Am. Chem. Soc. 116, 5045-5049.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 5045-5049
    • Hengge, A.C.1    Edens, W.A.2    Elsing, H.3
  • 34
    • 33845375092 scopus 로고
    • 18O isotope effects on the deprotonation of phosphate and phosphate esters and the anomeric effect on deprotonation of glucose-6-phosphate
    • 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.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 2759-2761
    • Knight, W.B.1    Weiss, P.M.2    Cleland, W.W.3
  • 35
    • 0037058883 scopus 로고    scopus 로고
    • Catalytic mechanism of Cdc25
    • Rudolph, J. (2002) Catalytic mechanism of Cdc25, Biochemistry 41, 14613-14623.
    • (2002) Biochemistry , vol.41 , pp. 14613-14623
    • Rudolph, J.1
  • 36
    • 0001981310 scopus 로고
    • The mechanism of phosphoryl transfer
    • (Gandour, R. D., and Schowen, R. L., Eds.), Plenum Press, New York
    • Benkovic, S. J., and Schray, K. J. (1978) The mechanism of phosphoryl transfer, in Transition States of Biochemical Processes (Gandour, R. D., and Schowen, R. L., Eds.) pp 493-527, Plenum Press, New York.
    • (1978) Transition States of Biochemical Processes , pp. 493-527
    • Benkovic, S.J.1    Schray, K.J.2
  • 37
    • 23044505158 scopus 로고
    • Mechanism and catalysis of nucleophilic substitution in phosphate esters
    • Thatcher, G. R. J., and Kluger, R. (1989) Mechanism and catalysis of nucleophilic substitution in phosphate esters, Adv. Phys. Org. Chem. 25, 99-265.
    • (1989) Adv. Phys. Org. Chem. , vol.25 , pp. 99-265
    • Thatcher, G.R.J.1    Kluger, R.2
  • 38
    • 0000144108 scopus 로고
    • Concerted or stepwise mechanisms for acyl transfer reactions of p-nitrophenyl acetate? Transition state structures from isotope effects
    • 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.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 11256-11263
    • Hengge, A.C.1    Hess, R.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.