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Volumn 44, Issue 31, 2005, Pages 10443-10448

A definitive mechanism for chorismate mutase

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ENERGY; ELECTROSTATICS; ESCHERICHIA COLI; MOLECULAR DYNAMICS; PHASE TRANSITIONS; REACTION KINETICS; THERMODYNAMIC PROPERTIES; WATER;

EID: 23244446189     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050886p     Document Type: Article
Times cited : (54)

References (30)
  • 1
    • 0036009145 scopus 로고    scopus 로고
    • A view at the millennium: The efficiency of enzymatic catalysis
    • Bruice, T. C. (2002) A view at the millennium: The efficiency of enzymatic catalysis, Acc. Chem. Res. 35, 139-148.
    • (2002) Acc. Chem. Res. , vol.35 , pp. 139-148
    • Bruice, T.C.1
  • 2
    • 0001298143 scopus 로고
    • On the mechanism of chorismate mutase reaction
    • Guilford, W. J., Copley, S. D., and Knowles, J. R. (1987) On the mechanism of chorismate mutase reaction, J. Am. Chem. Soc. 109, 5013-5019.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 5013-5019
    • Guilford, W.J.1    Copley, S.D.2    Knowles, J.R.3
  • 3
    • 0001138032 scopus 로고
    • The conformational equilibrium of chorismate in solution: Implication for the mechanism of the nonenzymatic and the enzyme-catalyzed rearrangement of chorismate to prephenate
    • Copley, S. D., and Knowles, J. R. (1987) The conformational equilibrium of chorismate in solution: Implication for the mechanism of the nonenzymatic and the enzyme-catalyzed rearrangement of chorismate to prephenate, J. Am. Chem. Soc. 109, 5008-5013.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 5008-5013
    • Copley, S.D.1    Knowles, J.R.2
  • 4
    • 0040362704 scopus 로고    scopus 로고
    • Chemical basis for enzyme catalysis
    • Bruice, T. C., and Benkovic, S. J. (2000) Chemical basis for enzyme catalysis, Biochemistry 39, 6267-6274.
    • (2000) Biochemistry , vol.39 , pp. 6267-6274
    • Bruice, T.C.1    Benkovic, S.J.2
  • 5
    • 0037022251 scopus 로고    scopus 로고
    • The mechanism of catalysis of the chorismate to prephenate reaction by the Escherichia coli mutase enzyme
    • Hur, S., and Bruice, T. C. (2002) The mechanism of catalysis of the chorismate to prephenate reaction by the Escherichia coli mutase enzyme, Proc. Natl. Acad. Sci. U.S.A. 99, 1176-1181.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 1176-1181
    • Hur, S.1    Bruice, T.C.2
  • 6
    • 0038634537 scopus 로고    scopus 로고
    • Comparison of formation of reactive conformers (NACs) for the Claisen rearrangement of chorismate to prephenate in water and in the E. coli mutase: The efficiency of the enzyme catalysis
    • Hur, S., and Bruice, T. C. (2003) Comparison of formation of reactive conformers (NACs) for the Claisen rearrangement of chorismate to prephenate in water and in the E. coli mutase: The efficiency of the enzyme catalysis, J. Am. Chem. Soc. 125, 5964.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 5964
    • Hur, S.1    Bruice, T.C.2
  • 7
    • 0142091405 scopus 로고    scopus 로고
    • The near attack conformation approach to the study of the chorismate to prephenate reaction
    • Hur, S., and Bruice, T. C. (2003) The near attack conformation approach to the study of the chorismate to prephenate reaction, Proc. Natl. Acad. Sci. U.S.A. 100, 12015-12020.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 12015-12020
    • Hur, S.1    Bruice, T.C.2
  • 8
    • 0029109922 scopus 로고
    • Atomic-structure of the buried catalytic pocket of Escherichia coli chorismate mutase
    • Lee, A. Y., Karplus, P. A., Ganem, B., and Clardy, J. (1995) Atomic-structure of the buried catalytic pocket of Escherichia coli chorismate mutase, J. Am. Chem. Soc. 117, 3627.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 3627
    • Lee, A.Y.1    Karplus, P.A.2    Ganem, B.3    Clardy, J.4
  • 9
    • 0029789767 scopus 로고    scopus 로고
    • The mechanism of the Claisen rearrangement: Déjà vu all over again
    • Ganem, B. (1996) The mechanism of the Claisen rearrangement: Déjà vu all over again, Angew. Chem., Int. Ed. 35, 936-945.
    • (1996) Angew. Chem., Int. Ed. , vol.35 , pp. 936-945
    • Ganem, B.1
  • 10
    • 1542286225 scopus 로고    scopus 로고
    • Chorismate mutase of Thermus thermophilus is a monofunctional AroH class enzyme inhibited by tyrosine
    • Helmstaedt, K., Heinrich, G., Merkl, R., and Braus, G. H. (2004) Chorismate mutase of Thermus thermophilus is a monofunctional AroH class enzyme inhibited by tyrosine, Arch. Microbiol. 181, 195-203.
    • (2004) Arch. Microbiol. , vol.181 , pp. 195-203
    • Helmstaedt, K.1    Heinrich, G.2    Merkl, R.3    Braus, G.H.4
  • 12
    • 1542779956 scopus 로고    scopus 로고
    • Self-consistent-charge density-functional tight-binding method for simulation of complex materials properties
    • Elstner, M., Porezag, D., Jungnickel, G., Elsner, J., Haugk, M., Fraucnhcim, T., Suhai, S., and Seifert, G. (1998) Self-consistent-charge density-functional tight-binding method for simulation of complex materials properties, Phys. Rev. B 58, 7260-7268.
    • (1998) Phys. Rev. B , vol.58 , pp. 7260-7268
    • Elstner, M.1    Porezag, D.2    Jungnickel, G.3    Elsner, J.4    Haugk, M.5    Fraucnhcim, T.6    Suhai, S.7    Seifert, G.8
  • 13
    • 0035138648 scopus 로고    scopus 로고
    • A QM/MM implementation of the self-consistent charge density functional tight binding (SCC-DFTB) method
    • Cui, Q., Elsstner, M., Kaxias, E., Frauenheim, T., and Karplus, M. (2001) A QM/MM implementation of the self-consistent charge density functional tight binding (SCC-DFTB) method, J. Phys. Chem. B 105, 569-585.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 569-585
    • Cui, Q.1    Elsstner, M.2    Kaxias, E.3    Frauenheim, T.4    Karplus, M.5
  • 14
    • 0031561292 scopus 로고    scopus 로고
    • Continuum treatment of long-range interactions in free energy calculations. Application to protein-ligand binding
    • Simonson, T., Archontis, G., and Karplus, M. (1997) Continuum treatment of long-range interactions in free energy calculations. Application to protein-ligand binding, J. Phys. Chem. B 101, 8349.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 8349
    • Simonson, T.1    Archontis, G.2    Karplus, M.3
  • 15
    • 84986492477 scopus 로고
    • Atomic charges derived from semipirical methods
    • Besler, B. H., Merz, K. M., and Kollman, P. A. (1990) Atomic charges derived from semipirical methods, J. Comput. Chem. 11, 431.
    • (1990) J. Comput. Chem. , vol.11 , pp. 431
    • Besler, B.H.1    Merz, K.M.2    Kollman, P.A.3
  • 17
    • 3042524904 scopus 로고
    • A well-behaved electrostatic potential based method using charge restrained for deriving atomic charges: The RESP model
    • Bayly, C. I., Cieplak, P., and Cornell, W. D. (1993) A well-behaved electrostatic potential based method using charge restrained for deriving atomic charges: The RESP model, J. Phys. Chem. 97, 10269.
    • (1993) J. Phys. Chem. , vol.97 , pp. 10269
    • Bayly, C.I.1    Cieplak, P.2    Cornell, W.D.3
  • 18
    • 0035961478 scopus 로고    scopus 로고
    • A hybrid potential reaction path and free energy study of chorismate mutase reactions
    • Marti, S., Andres, J., Moliner, V., Silla, E., Tunon, I., Vertran, J., and Filed, M. J. (2001) A hybrid potential reaction path and free energy study of chorismate mutase reactions, J. Am. Chem. Soc. 123, 1709-1712
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 1709-1712
    • Marti, S.1    Andres, J.2    Moliner, V.3    Silla, E.4    Tunon, I.5    Vertran, J.6    Filed, M.J.7
  • 19
    • 0033518886 scopus 로고    scopus 로고
    • Heavy atom isotope effects reveal a highly polarized transition state for chorismate mutase
    • Gustin, D. J., Mattei, P., Kast, P., Wiest, O., Lee, L., Cleland, W. W., and Hilvert, D. (1999) Heavy atom isotope effects reveal a highly polarized transition state for chorismate mutase, J. Am. Chem. Soc. 121, 1756-1757.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 1756-1757
    • Gustin, D.J.1    Mattei, P.2    Kast, P.3    Wiest, O.4    Lee, L.5    Cleland, W.W.6    Hilvert, D.7
  • 20
    • 33644486708 scopus 로고    scopus 로고
    • Personal communication
    • Cleland, W. W. (2005) Personal communication.
    • (2005)
    • Cleland, W.W.1
  • 21
    • 0000167881 scopus 로고
    • Insights into chorismate mutase catalysis from a combined QM/MM simulation of the enzyme reaction
    • Lyne, P. D., Mulholland, A. J., and Richards, W. G. (1995) Insights into chorismate mutase catalysis from a combined QM/MM simulation of the enzyme reaction, J. Am. Chem. Soc. 117, 11345-11350.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 11345-11350
    • Lyne, P.D.1    Mulholland, A.J.2    Richards, W.G.3
  • 22
    • 0015819741 scopus 로고
    • Transition-state stabilization and enzymatic catalysis. Kinetic and molecular orbital studies of the rearrangement of chorismate to prephenate
    • Andrews, P. R., Smith, D., and Young, I. G. (1973) Transition-state stabilization and enzymatic catalysis. Kinetic and molecular orbital studies of the rearrangement of chorismate to prephenate, Biochemistry 12, 3492-3498.
    • (1973) Biochemistry , vol.12 , pp. 3492-3498
    • Andrews, P.R.1    Smith, D.2    Young, I.G.3
  • 23
    • 0035979270 scopus 로고    scopus 로고
    • Substrate comformational transitions in the active site of chorismate mutase: Their role in the catalytic mechanism
    • Guo, H., Cui, Q., Lipscomb, W. N., and Karplus, M. (2001) Substrate comformational transitions in the active site of chorismate mutase: Their role in the catalytic mechanism, Proc. Natl. Acad. Sci. U.S.A. 98, 9032-9037.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 9032-9037
    • Guo, H.1    Cui, Q.2    Lipscomb, W.N.3    Karplus, M.4
  • 25
    • 0037153275 scopus 로고    scopus 로고
    • Reaction mechanism of chorismate mutase studied by the combined potentials of quantum mechanics and molecular mechanics
    • Lee, Y. S., Worthington, S. W., Krauss, M., and Brooks, B. R. (2002) Reaction mechanism of chorismate mutase studied by the combined potentials of quantum mechanics and molecular mechanics, J. Phys. Chem. B 106, 12059-12065.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 12059-12065
    • Lee, Y.S.1    Worthington, S.W.2    Krauss, M.3    Brooks, B.R.4
  • 26
    • 0038547896 scopus 로고    scopus 로고
    • Investigation of solvent effects for the Claisen rearrangement of chorismate to prephenate: Mechanistic interpretation via near attack conformations
    • Repasky, M. P., Guimaraes, C. R. W., Chandrasekhar, J., Tirado-Rives, J., and Jorgensen, W. L. (2003) Investigation of solvent effects for the Claisen rearrangement of chorismate to prephenate: Mechanistic interpretation via near attack conformations, J. Am. Chem. Soc. 125, 6663-6672.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6663-6672
    • Repasky, M.P.1    Guimaraes, C.R.W.2    Chandrasekhar, J.3    Tirado-Rives, J.4    Jorgensen, W.L.5
  • 27
    • 0038615889 scopus 로고    scopus 로고
    • Contributions of conformational compression and preferential transition state stabilization to the rate enhancement by chorismate mutase
    • Guimaraes, C. R. W., Repasky, M. P., Chandrasekhar, J., Tirado-Rives, J., and Jorgensen, W. L. (2003) Contributions of conformational compression and preferential transition state stabilization to the rate enhancement by chorismate mutase, J. Am. Chem. Soc. 125, 6892-6899.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6892-6899
    • Guimaraes, C.R.W.1    Repasky, M.P.2    Chandrasekhar, J.3    Tirado-Rives, J.4    Jorgensen, W.L.5
  • 28
    • 0033118836 scopus 로고    scopus 로고
    • Bacillus subtilis chorismate mutase is partially diffusion-controlled
    • Mattel, P., Kast, P., and Hivlert, D. (1999) Bacillus subtilis chorismate mutase is partially diffusion-controlled, Eur. J. Biochem. 261, 25-32.
    • (1999) Eur. J. Biochem. , vol.261 , pp. 25-32
    • Mattel, P.1    Kast, P.2    Hivlert, D.3
  • 30
    • 2342565009 scopus 로고    scopus 로고
    • Transition state stabilization and substrate strain in enzyme catalysis: Ab initio QM/MM modelling of the chorismate mutase reaction
    • Ranaghan, K. E., Ridder, L., Szefczyk, B., Hermann, J. C., and Mulholland, A. J. (2004) Transition state stabilization and substrate strain in enzyme catalysis: Ab initio QM/MM modelling of the chorismate mutase reaction, Org. Biornol. Chem. 2, 968-980.
    • (2004) Org. Biornol. Chem. , vol.2 , pp. 968-980
    • Ranaghan, K.E.1    Ridder, L.2    Szefczyk, B.3    Hermann, J.C.4    Mulholland, A.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.