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Volumn 46, Issue 17, 2003, Pages 3703-3708

A comparison of phosphonothioic acids with phosphonic acids as phosphatase inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; ANION; BACTERIAL ENZYME; ESTER DERIVATIVE; ORGANOPHOSPHATE; OXYGEN; PHOSPHATASE; PHOSPHATE; PHOSPHONIC ACID DERIVATIVE; PHOSPHONOTHIOIC ACID DERIVATIVE; PHOSPHOPROTEIN PHOSPHATASE 2C; PHOSPHOROTHIOIC ACID DERIVATIVE; PHOSPHORUS DERIVATIVE; PLACENTA ENZYME; PROTEIN PHOSPHATASE LAMBDA; PROTEIN SERINE THREONINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE; SULFUR; THIOL DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0042231985     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm030106f     Document Type: Article
Times cited : (27)

References (37)
  • 1
    • 0035413605 scopus 로고    scopus 로고
    • Protein phosphatases - A phylogenetic perspective
    • Kennelly, P. Protein Phosphatases-A Phylogenetic Perspective. Chem. Rev. 2001, 101, 2291-2312.
    • (2001) Chem. Rev. , vol.101 , pp. 2291-2312
    • Kennelly, P.1
  • 2
    • 0035413612 scopus 로고    scopus 로고
    • Histidine phosphorylation and two-component signaling in eukaryotic cells
    • Saito, H. Histidine Phosphorylation and Two-Component Signaling in Eukaryotic Cells. Chem. Rev. 2001, 101, 2497-2510.
    • (2001) Chem. Rev. , vol.101 , pp. 2497-2510
    • Saito, H.1
  • 3
    • 0035413604 scopus 로고    scopus 로고
    • Molecular reactions of protein phosphatases-insights from structure and chemistry
    • Jackson, M. D.; Denu, J. M. Molecular reactions of protein phosphatases-insights from structure and chemistry. Chem. Rev. 2001, 101, 2313-2340.
    • (2001) Chem. Rev. , vol.101 , pp. 2313-2340
    • Jackson, M.D.1    Denu, J.M.2
  • 4
    • 0035413607 scopus 로고    scopus 로고
    • Structural basis for control by phosphorylation
    • Johnson, L. N.; Lewis, R. J. Structural Basis for Control by Phosphorylation. Chem. Rev. 2001, 101, 2209-2242.
    • (2001) Chem. Rev. , vol.101 , pp. 2209-2242
    • Johnson, L.N.1    Lewis, R.J.2
  • 5
    • 0035413606 scopus 로고    scopus 로고
    • Kinetic and catalytic mechanisms of protein kinases
    • Adams, J. A. Kinetic and Catalytic Mechanisms of Protein Kinases. Chem. Rev. 2001, 101, 2271-2290.
    • (2001) Chem. Rev. , vol.101 , pp. 2271-2290
    • Adams, J.A.1
  • 6
    • 0026703858 scopus 로고
    • A general method for the preparation of benzylic α,α-difluorophosphonic acids; nonhydrolyzable mimetics of phosphotyrosine
    • Smyth, M. S.; Ford, H. F.; Burke, T. R. A general method for the preparation of benzylic α,α-difluorophosphonic acids; nonhydrolyzable mimetics of phosphotyrosine. Tetrahedron Lett. 1992, 33, 4137-4140.
    • (1992) Tetrahedron Lett. , vol.33 , pp. 4137-4140
    • Smyth, M.S.1    Ford, H.F.2    Burke, T.R.3
  • 7
    • 0028785789 scopus 로고
    • Why is phosphonodifluoromethyl phenylalanine a more potent inhibitory moiety than phosphonomethyl phenylalanine toward protein-tyrosine phosphatases?
    • Chen, L.; Wu, L.; Otaka, A.; Smyth, M. S.; Roller, P. P.; Burke, T. R., Jr.; den Hertog, J.; Zhang, Z. Y. Why is phosphonodifluoromethyl phenylalanine a more potent inhibitory moiety than phosphonomethyl phenylalanine toward protein-tyrosine phosphatases? Biochem. Biophys. Res. Commun. 1995, 216, 976-984.
    • (1995) Biochem. Biophys. Res. Commun. , vol.216 , pp. 976-984
    • Chen, L.1    Wu, L.2    Otaka, A.3    Smyth, M.S.4    Roller, P.P.5    Burke T.R., Jr.6    Den Hertog, J.7    Zhang, Z.Y.8
  • 8
    • 0002173005 scopus 로고
    • Phosphate ester hydrolysis
    • Academic Press: New York
    • Gerlt, J. A. Phosphate Ester Hydrolysis. The Enzymes, 3rd ed.; Academic Press: New York, 1992; Vol. 20, pp 95-139.
    • (1992) The Enzymes, 3rd Ed. , vol.20 , pp. 95-139
    • Gerlt, J.A.1
  • 9
    • 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.; Zhang, Z.-Y. Impaired transition state complementarity in the hydrolysis of O-arylphosphorothioates by protein-tyrosine phosphatases. Biochemistry 1999, 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
  • 10
    • 0001719195 scopus 로고
    • Relative reactivities of p-nitrophenyl phosphate and phosphorothioate toward alkaline phosphatase and in aqueous hydrolysis
    • Breslow, R.; Katz, I. Relative reactivities of p-nitrophenyl phosphate and phosphorothioate toward alkaline phosphatase and in aqueous hydrolysis. J. Am. Chem. Soc. 1968, 90, 7376-7377.
    • (1968) J. Am. Chem. Soc. , vol.90 , pp. 7376-7377
    • Breslow, R.1    Katz, I.2
  • 11
    • 0029117035 scopus 로고
    • The nature of the transition state for enzyme-catalyzed phosphoryl transfer. Hydrolysis of O-aryl phosphorothioates by alkaline phosphatase
    • Hollfelder, F.; Herschlag, D. The nature of the transition state for enzyme-catalyzed phosphoryl transfer. Hydrolysis of O-aryl phosphorothioates by alkaline phosphatase. Biochemistry 1995, 34, 12255-12264.
    • (1995) Biochemistry , vol.34 , pp. 12255-12264
    • Hollfelder, F.1    Herschlag, D.2
  • 12
    • 0022418143 scopus 로고
    • Bond order and charge localization in nucleoside phosphorothioates
    • Frey, P. A.; Sammons, D. Bond order and charge localization in nucleoside phosphorothioates. Science 1985, 228, 541-545.
    • (1985) Science , vol.228 , pp. 541-545
    • Frey, P.A.1    Sammons, D.2
  • 13
    • 0001085352 scopus 로고
    • Sulfur does not form double bonds in phosphorothioate anions
    • Liang, C.; Allen, L. C. Sulfur does not form double bonds in phosphorothioate anions. J. Am. Chem. Soc. 1987, 109, 6449-6453.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 6449-6453
    • Liang, C.1    Allen, L.C.2
  • 14
    • 0035937857 scopus 로고    scopus 로고
    • Crystal structure of alkaline phosphatase from human placenta at 1.8 Å resolution. Implication for a substrate specificity
    • Le Du, M. H.; Stigbrand, T.; Taussig, M. J.; Menez, A.; Stura, E. A. Crystal structure of alkaline phosphatase from human placenta at 1.8 Å resolution. Implication for a substrate specificity. J. Biol. Chem. 2001, 276, 9158-9165.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9158-9165
    • Le Du, M.H.1    Stigbrand, T.2    Taussig, M.J.3    Menez, A.4    Stura, E.A.5
  • 15
    • 0025777694 scopus 로고
    • Reaction mechanism of alkaline phosphatase based on crystal structures
    • Kim, E. E.; Wyckoff, H. W. Reaction mechanism of alkaline phosphatase based on crystal structures. J. Mol. Biol. 1991, 218, 449-464.
    • (1991) J. Mol. Biol. , vol.218 , pp. 449-464
    • Kim, E.E.1    Wyckoff, H.W.2
  • 16
    • 0031893253 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatases: Biological function, structural characteristics, and mechanism of catalysis
    • Zhang, Z.-Y. Protein-tyrosine phosphatases: biological function, structural characteristics, and mechanism of catalysis. CRC Crit. Rev. Biochem. Mol. Biol. 1998, 33, 1-52.
    • (1998) CRC Crit. Rev. Biochem. Mol. Biol. , vol.33 , pp. 1-52
    • Zhang, Z.-Y.1
  • 18
    • 0042891822 scopus 로고
    • Heteroorganic substances. LII. Amidothiophosphonic acids and their derivatives
    • Almasi, L.; Fenesan, I.; Biro, V. Heteroorganic substances. LII. Amidothiophosphonic acids and their derivatives. J. Prakt. Chemie 1979, 321, 913-920.
    • (1979) J. Prakt. Chemie , vol.321 , pp. 913-920
    • Almasi, L.1    Fenesan, I.2    Biro, V.3
  • 19
    • 0042970006 scopus 로고
    • Application of the Hammett equation to the theory of tautomeric equilibrium. Thiono-thiolo tautomerism of thiophosphoric compounds
    • Kabachnik, M. I.; Mastryukova, T. A.; Shipov, A. E.; Melent'eva, T. A. Application of the Hammett equation to the theory of tautomeric equilibrium. Thiono-thiolo tautomerism of thiophosphoric compounds. Doklady Akad. Nauk S.S.S.R. 1959, 124, 1061-1064.
    • (1959) Doklady Akad. Nauk S.S.S.R. , vol.124 , pp. 1061-1064
    • Kabachnik, M.I.1    Mastryukova, T.A.2    Shipov, A.E.3    Melent'eva, T.A.4
  • 20
    • 0037467695 scopus 로고    scopus 로고
    • A convenient synthesis of phosphonothioic acids
    • Swierczek, K.; Peters, J.; Hengge, A. C. A convenient synthesis of phosphonothioic acids. Tetrahedron 2003, 59, 595-599.
    • (2003) Tetrahedron , vol.59 , pp. 595-599
    • Swierczek, K.1    Peters, J.2    Hengge, A.C.3
  • 21
    • 0041889617 scopus 로고
    • Monodealcoylation d'esters phosphoriques et phosphoniques par les thiolates et thiophenates
    • Savignac, P.; Lavielle, G. Monodealcoylation d'esters phosphoriques et phosphoniques par les thiolates et thiophenates. Bull. Soc. Chim. Fr. 1978, 1506-1508.
    • (1978) Bull. Soc. Chim. Fr. , pp. 1506-1508
    • Savignac, P.1    Lavielle, G.2
  • 22
    • 0029027830 scopus 로고
    • Convenient "one-pot" synthesis of chlorophosphonates, chlorophosphates and chlorophosphoramides from the corresponding benzyl esters
    • Saady, M.; Lebeau, L.; Mioskowski, C. Convenient "One-Pot" Synthesis of Chlorophosphonates, Chlorophosphates and Chlorophosphoramides from the Corresponding Benzyl Esters. Tetrahedron Lett. 1995, 36, 4785-4786.
    • (1995) Tetrahedron Lett. , vol.36 , pp. 4785-4786
    • Saady, M.1    Lebeau, L.2    Mioskowski, C.3
  • 23
    • 0028561861 scopus 로고
    • The chemistry of phosphapeptides: Formation of functionalized phosphonochloridates under mild conditions and their reaction with alcohols and amines
    • Malachowski, W. P.; Coward, J. K. The Chemistry of Phosphapeptides: Formation of Functionalized Phosphonochloridates under Mild Conditions and Their Reaction with Alcohols and Amines. J. Org. Chem. 1994, 59, 7616-7624.
    • (1994) J. Org. Chem. , vol.59 , pp. 7616-7624
    • Malachowski, W.P.1    Coward, J.K.2
  • 24
    • 0041388733 scopus 로고
    • Der oxidative abbau von thiophosphin-thiophosphon- und thiophosphorsaureestern mit hypochlorit
    • Horner, L.; Gerhard, J. Der Oxidative Abbau von Thiophosphin-Thiophosphon- und Thiophosphorsaureestern mit Hypochlorit. Phosphorus Sulfur 1985, 22, 13-21.
    • (1985) Phosphorus Sulfur , vol.22 , pp. 13-21
    • Horner, L.1    Gerhard, J.2
  • 25
    • 0007920842 scopus 로고
    • Preparation and determination of apparent dissociation constants of some alkylphosphonic and dialkylphosphinic acids
    • Crofts, P. C.; Kosolapoff, G. M. Preparation and Determination of Apparent Dissociation Constants of Some Alkylphosphonic and Dialkylphosphinic Acids. J. Am. Chem. Soc. 1975, 75, 3379-3383.
    • (1975) J. Am. Chem. Soc. , vol.75 , pp. 3379-3383
    • Crofts, P.C.1    Kosolapoff, G.M.2
  • 26
    • 33748428561 scopus 로고
    • The preparation and properties of phosphonic acids
    • Freedman, L. D.; Doak, G. O. The Preparation And Properties Of Phosphonic Acids. Chem. Rev. 1957, 57, 479-523.
    • (1957) Chem. Rev. , vol.57 , pp. 479-523
    • Freedman, L.D.1    Doak, G.O.2
  • 27
    • 0033577278 scopus 로고    scopus 로고
    • Comparisons of phosphorothioate and phosphate monoester transfer reactions: Activation parameters, solvent effects, and the effect of metal ions
    • Catrina, I. E.; Hengge, A. C. Comparisons of Phosphorothioate and Phosphate Monoester Transfer Reactions: Activation Parameters, Solvent Effects, and the Effect of Metal Ions. J. Am. Chem. Soc. 1999, 121, 2156-2163.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2156-2163
    • Catrina, I.E.1    Hengge, A.C.2
  • 29
    • 0028882428 scopus 로고
    • Phosphonate inhibitors of protein-tyrosine and serine/threonine phosphatases
    • Kole, H. K.; Smyth, M. S.; Russ, P. L.; Burke, T. R. Phosphonate inhibitors of protein-tyrosine and serine/threonine phosphatases. Biochem. J. 1995, 311, 1025-1031.
    • (1995) Biochem. J. , vol.311 , pp. 1025-1031
    • Kole, H.K.1    Smyth, M.S.2    Russ, P.L.3    Burke, T.R.4
  • 30
    • 0029094754 scopus 로고
    • Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1
    • Goldberg, J.; Huang, H. B.; Kwon, Y. G.; Greengard, P.; Nairn, A. C.; Kuriyan, J. Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Nature 1995, 376, 745-753.
    • (1995) Nature , vol.376 , pp. 745-753
    • Goldberg, J.1    Huang, H.B.2    Kwon, Y.G.3    Greengard, P.4    Nairn, A.C.5    Kuriyan, J.6
  • 31
    • 0029583122 scopus 로고
    • Crystal structure of the catalytic subunit of human protein phosphatase I and its complex with tungstate
    • Egloff, M.; Cohen, P. T.; Reinemer, P.; Barford, D. Crystal structure of the catalytic subunit of human protein phosphatase I and its complex with tungstate. J. Mol. Biol 1995, 254, 942-959.
    • (1995) J. Mol. Biol. , vol.254 , pp. 942-959
    • Egloff, M.1    Cohen, P.T.2    Reinemer, P.3    Barford, D.4
  • 34
    • 0034687659 scopus 로고    scopus 로고
    • Structure of the bacteriophage lambda Ser/Thr protein phosphatase with sulfate ion bound in two coordination modes
    • Voegtli, W. C.; White, D. J.; Reiter, N. J.; Rusnak, F.; Rosenzweig, A. C. Structure of the bacteriophage lambda Ser/Thr protein phosphatase with sulfate ion bound in two coordination modes. Biochemistry 2000, 39, 15365-15374.
    • (2000) Biochemistry , vol.39 , pp. 15365-15374
    • Voegtli, W.C.1    White, D.J.2    Reiter, N.J.3    Rusnak, F.4    Rosenzweig, A.C.5
  • 35
    • 0030465532 scopus 로고    scopus 로고
    • Crystal structure of the protein serine/threonine phosphatase 2C at 2 Å resolution
    • Das, A. K.; Helps, N. R.; Cohen, P. T.; Barford, D. Crystal structure of the protein serine/threonine phosphatase 2C at 2 Å resolution. EMBO J. 1996, 15, 6798-6809.
    • (1996) EMBO J. , vol.15 , pp. 6798-6809
    • Das, A.K.1    Helps, N.R.2    Cohen, P.T.3    Barford, D.4
  • 36
    • 0033575250 scopus 로고    scopus 로고
    • Kinetic analysis of human serine/threonine protein phosphatase 2Cα
    • Fjeld, C. C.; Denu, J. M. Kinetic analysis of human serine/threonine protein phosphatase 2Cα. J. Biol. Chem. 1999, 274, 20336-20343.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20336-20343
    • Fjeld, C.C.1    Denu, J.M.2
  • 37
    • 0033602926 scopus 로고    scopus 로고
    • Interaction of bacteriophage lambda protein phosphatase with Mn(II): Evidence for the formation of a [Mn(II)]2 cluster
    • Rusnak, F.; Yu, L.; Todorovic, S.; Mertz, P. Interaction of bacteriophage lambda protein phosphatase with Mn(II): evidence for the formation of a [Mn(II)]2 cluster. Biochemistry 1999, 38, 6943-6952.
    • (1999) Biochemistry , vol.38 , pp. 6943-6952
    • Rusnak, F.1    Yu, L.2    Todorovic, S.3    Mertz, P.4


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