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Volumn 1697, Issue 1-2, 2004, Pages 279-287

Models for biological phosphoryl transfer

Author keywords

Adenosine triphosphate; ATP; Catalysis; Cooperativity; Hydrogen bond; LFER; Linear free energy relationship; NDP; NTP; Nucleoside diphosphate; Nucleoside triphosphate; Phosphatase; Phosphate ester hydrolysis; PP1; Protein phosphatase 1; PTFE; Transition state

Indexed keywords

ISOENZYME; MAGNESIUM; PHOSPHATASE; PHOSPHATE; PHOSPHORUS DERIVATIVE;

EID: 1542328903     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2003.11.031     Document Type: Conference Paper
Times cited : (58)

References (32)
  • 1
    • 23044505158 scopus 로고
    • Mechanism and catalysis of nucleophilic substitution in phosphate esters
    • Thatcher G.R.J., Kluger R. Mechanism and catalysis of nucleophilic substitution in phosphate esters. Adv. Phys. Org. Chem. 25:1989;99-265.
    • (1989) Adv. Phys. Org. Chem. , vol.25 , pp. 99-265
    • Thatcher, G.R.J.1    Kluger, R.2
  • 3
    • 0033102133 scopus 로고    scopus 로고
    • Mechanistic alternatives in phosphate monoester hydrolysis: What conclusions can be drawn from available experimental data?
    • Åqvist J., Kolmodin K., Florian J., Warshel A. Mechanistic alternatives in phosphate monoester hydrolysis: what conclusions can be drawn from available experimental data? Chem. Biol. 6:1999;R71-R80.
    • (1999) Chem. Biol. , vol.6 , pp. 71-R80
    • Åqvist, J.1    Kolmodin, K.2    Florian, J.3    Warshel, A.4
  • 4
    • 0034654214 scopus 로고    scopus 로고
    • The substrate-assisted general base catalysis model for phosphate monoester hydrolysis: Evaluation using reactivity comparisons
    • Admiraal S., Herschlag D. The substrate-assisted general base catalysis model for phosphate monoester hydrolysis: evaluation using reactivity comparisons. J. Am. Chem. Soc. 122:2000;2145-2148.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 2145-2148
    • Admiraal, S.1    Herschlag, D.2
  • 5
    • 0030724727 scopus 로고    scopus 로고
    • Mechanisms of signaling and related enzymes
    • Mildvan A. Mechanisms of signaling and related enzymes. Proteins. 4:1997;401-416.
    • (1997) Proteins , vol.4 , pp. 401-416
    • Mildvan, A.1
  • 6
    • 0035543093 scopus 로고    scopus 로고
    • The depth of chemical time and the power of enzymes as catalysts
    • Wolfenden R., Snider M.J. The depth of chemical time and the power of enzymes as catalysts. Acc. Chem. Res. 34:2001;938-945.
    • (2001) Acc. Chem. Res. , vol.34 , pp. 938-945
    • Wolfenden, R.1    Snider, M.J.2
  • 7
    • 0032528058 scopus 로고    scopus 로고
    • Spontaneous hydrolysis of glycosides
    • Wolfenden R., Lu X., Young G. Spontaneous hydrolysis of glycosides. J. Am. Chem. Soc. 120:1998;6814-6815.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 6814-6815
    • Wolfenden, R.1    Lu, X.2    Young, G.3
  • 9
    • 12444255826 scopus 로고
    • Evidence that metaphosphate monoanion is not an intermediate in solvolysis reactions in aqueous solution
    • Herschlag D., Jencks W.P. Evidence that metaphosphate monoanion is not an intermediate in solvolysis reactions in aqueous solution. J. Am. Chem. Soc. 111:1989;7579-7586.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 7579-7586
    • Herschlag, D.1    Jencks, W.P.2
  • 10
    • 33947333789 scopus 로고
    • The reactivity of phosphate esters. Monoester hydrolysis
    • Kirby A.J., Varvoglis A.G. The reactivity of phosphate esters. Monoester hydrolysis. J. Am. Chem. Soc. 89:1967;415-423.
    • (1967) J. Am. Chem. Soc. , vol.89 , pp. 415-423
    • Kirby, A.J.1    Varvoglis, A.G.2
  • 11
    • 0032481372 scopus 로고
    • Spontaneous hydrolysis of ionised phosphate monoesters and diesters and the proficiencies of phosphatases and phosphodiesterases as catalysts
    • Wolfenden R., Ridgway C., Young G. Spontaneous hydrolysis of ionised phosphate monoesters and diesters and the proficiencies of phosphatases and phosphodiesterases as catalysts. J. Am. Chem. Soc. 120:1988;833-834.
    • (1988) J. Am. Chem. Soc. , vol.120 , pp. 833-834
    • Wolfenden, R.1    Ridgway, C.2    Young, G.3
  • 12
    • 0030858487 scopus 로고    scopus 로고
    • - attack in phosphate ester hydrolysis is not fully justified
    • - attack in phosphate ester hydrolysis is not fully justified. J. Am. Chem. Soc. 119:1997;5473-5474.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 5473-5474
    • Florián, J.1    Warshel, A.2
  • 13
    • 0035928522 scopus 로고    scopus 로고
    • Base-catalysed phosphate diester hydrolysis
    • Williams N.H., Wyman P. Base-catalysed phosphate diester hydrolysis. Chem. Commun. 2001;1268-1269.
    • (2001) Chem. Commun. , pp. 1268-1269
    • Williams, N.H.1    Wyman, P.2
  • 14
    • 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., Wolfenden R. The rate of hydrolysis of phosphomonoester dianions and the exceptional catalytic proficiencies of protein and inositol phosphatases. Proc. Natl. Acad. Sci. U. S. A. 100:2003;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
  • 15
    • 0035952318 scopus 로고    scopus 로고
    • Protein phosphatase 1 catalyses the direct hydrolytic cleavage of phosphate monoester in a ternary complex mechanism
    • Sanvoisin J., Gani D. Protein phosphatase 1 catalyses the direct hydrolytic cleavage of phosphate monoester in a ternary complex mechanism. Bioorg. Med. Chem. Lett. 11:2001;471-474.
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 471-474
    • Sanvoisin, J.1    Gani, D.2
  • 17
    • 0001431264 scopus 로고    scopus 로고
    • Binuclear metallohydrolases
    • Wilcox D.E. Binuclear metallohydrolases. Chem. Rev. 96:1996;2435-2458.
    • (1996) Chem. Rev. , vol.96 , pp. 2435-2458
    • Wilcox, D.E.1
  • 18
    • 0037022815 scopus 로고    scopus 로고
    • Alkaline phosphatase revisited: Hydrolysis of alkyl phosphates
    • O'Brien P.J., Herschlag D. Alkaline phosphatase revisited: hydrolysis of alkyl phosphates. Biochemistry. 41:2002;3207-3225.
    • (2002) Biochemistry , vol.41 , pp. 3207-3225
    • O'Brien, P.J.1    Herschlag, D.2
  • 19
    • 0033553145 scopus 로고    scopus 로고
    • A structural and functional model of dinuclear metallophosphatases
    • Williams N.H., Lebuis A.-M., Chin J. A structural and functional model of dinuclear metallophosphatases. J. Am. Chem. Soc. 121:1999;3341-3348.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 3341-3348
    • Williams, N.H.1    Lebuis, A.-M.2    Chin, J.3
  • 20
    • 0032547320 scopus 로고    scopus 로고
    • Reactivity of phosphate diesters doubly coordinated to a dinuclear cobalt (III) complex: Dependence of the reactivity on the basicity of the leaving group
    • Williams N.H., Cheung W., Chin J. Reactivity of phosphate diesters doubly coordinated to a dinuclear cobalt (III) complex: dependence of the reactivity on the basicity of the leaving group. J. Am. Chem. Soc. 120:1998;8079-8087.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 8079-8087
    • Williams, N.H.1    Cheung, W.2    Chin, J.3
  • 21
    • 0001191611 scopus 로고
    • Effective charge and Leffler's index as mechanistic tools for reactions in solution
    • Williams A. Effective charge and Leffler's index as mechanistic tools for reactions in solution. Acc. Chem. Res. 17:1984;425-430.
    • (1984) Acc. Chem. Res. , vol.17 , pp. 425-430
    • Williams, A.1
  • 22
    • 0037132609 scopus 로고    scopus 로고
    • An altered mechanism of hydrolysis for a metal-complexed phosphate diester
    • Humphry T., Forconi M., Williams N.H., Hengge A.C. An altered mechanism of hydrolysis for a metal-complexed phosphate diester. J. Am. Chem. Soc. 124:2002;14860-14861.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 14860-14861
    • Humphry, T.1    Forconi, M.2    Williams, N.H.3    Hengge, A.C.4
  • 23
    • 0023118846 scopus 로고
    • Kinetic and magnetic resonance studies of active-site mutants of staphylococcal nuclease: Factors contributing to catalysis
    • Serpersu E.H., Shortle D., Mildvan A.S. Kinetic and magnetic resonance studies of active-site mutants of staphylococcal nuclease: factors contributing to catalysis. Biochemistry. 26:1987;1289-1300.
    • (1987) Biochemistry , vol.26 , pp. 1289-1300
    • Serpersu, E.H.1    Shortle, D.2    Mildvan, A.S.3
  • 25
    • 0029583122 scopus 로고
    • Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate
    • Egloff M.-P., Cohen P.T.W., Reinemer P., Barford D. Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate. J. Mol. Biol. 254:1995;942-959.
    • (1995) J. Mol. Biol. , vol.254 , pp. 942-959
    • Egloff, M.-P.1    Cohen, P.T.W.2    Reinemer, P.3    Barford, D.4
  • 26
    • 0001603677 scopus 로고
    • Requirements for general acid-base catalysis of complex reactions
    • Jencks W.P. Requirements for general acid-base catalysis of complex reactions. J. Am. Chem. Soc. 94:1972;4731-4732.
    • (1972) J. Am. Chem. Soc. , vol.94 , pp. 4731-4732
    • Jencks, W.P.1
  • 27
    • 0000351076 scopus 로고
    • Isotope and kinetic studies of the mechanism of hydrolysis of salicyl phosphate. Intramolecular general acid catalysis
    • Bender M.L., Lawlor J.M. Isotope and kinetic studies of the mechanism of hydrolysis of salicyl phosphate. Intramolecular general acid catalysis. J. Am. Chem. Soc. 85:1963;3010-3017.
    • (1963) J. Am. Chem. Soc. , vol.85 , pp. 3010-3017
    • Bender, M.L.1    Lawlor, J.M.2
  • 28
    • 33947474357 scopus 로고
    • Hydroxyl group catalysis: III. the nature of neighbouring hydroxyl group assistance in the alkaline hydrolysis of the ester bond
    • Bruice T.C., Fife T.H. Hydroxyl group catalysis: III. The nature of neighbouring hydroxyl group assistance in the alkaline hydrolysis of the ester bond. J. Am. Chem. Soc. 84:1962;1973-1979.
    • (1962) J. Am. Chem. Soc. , vol.84 , pp. 1973-1979
    • Bruice, T.C.1    Fife, T.H.2
  • 29
    • 0033572706 scopus 로고    scopus 로고
    • External transesterification of ribonucleotide esters naturally catalyzed by large ribozymes
    • Roussev C.D., Ivanova G.D., Bratovanova E.K., Vassilev N.G., Petkov D.D. External transesterification of ribonucleotide esters naturally catalyzed by large ribozymes. J. Am. Chem. Soc. 121:1999;11267-11272.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 11267-11272
    • Roussev, C.D.1    Ivanova, G.D.2    Bratovanova, E.K.3    Vassilev, N.G.4    Petkov, D.D.5
  • 30
    • 0036495885 scopus 로고    scopus 로고
    • Mimicking metallophosphatases: Revealing a role for an OH group with no libido
    • Forconi M., Williams N.H. Mimicking metallophosphatases: revealing a role for an OH group with no libido. Angew. Chem., Int. Ed. Engl. 41:2002;849-852.
    • (2002) Angew. Chem., Int. Ed. Engl. , vol.41 , pp. 849-852
    • Forconi, M.1    Williams, N.H.2
  • 31
    • 0029410712 scopus 로고
    • Mapping the transition state for ATP hydrolysis: Implications for enzymatic catalysis
    • Admiraal S.J., Herschlag D. Mapping the transition state for ATP hydrolysis: implications for enzymatic catalysis. Chem. Biol. 2:1995;729-739.
    • (1995) Chem. Biol. , vol.2 , pp. 729-739
    • Admiraal, S.J.1    Herschlag, D.2
  • 32
    • 0034614085 scopus 로고    scopus 로고
    • Magnesium (II) catalysed ATP hydrolysis of ATP
    • Williams N.H. Magnesium (II) catalysed ATP hydrolysis of ATP. J. Am. Chem. Soc. 122:2000;12023-12024.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 12023-12024
    • Williams, N.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.