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Volumn 108, Issue 34, 2011, Pages 14115-14120

Catalysis by dihydrofolate reductase and other enzymes arises from electrostatic preorganization, not conformational motions

Author keywords

[No Author keywords available]

Indexed keywords

DIHYDROFOLATE REDUCTASE;

EID: 80052149070     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1111252108     Document Type: Article
Times cited : (174)

References (33)
  • 2
    • 0029102089 scopus 로고
    • Dynamics of the dihydrofolate-reductase folate complex - Catalytic sites and regions known to undergo conformational change exhibit diverse dynamical features
    • Epstein DM, Benkovic SJ, Wright PE (1995) Dynamics of the dihydrofolate-reductase folate complex - catalytic sites and regions known to undergo conformational change exhibit diverse dynamical features. Biochemistry 34:11037-11048.
    • (1995) Biochemistry , vol.34 , pp. 11037-11048
    • Epstein, D.M.1    Benkovic, S.J.2    Wright, P.E.3
  • 3
    • 0031443372 scopus 로고    scopus 로고
    • Evidence for a functional role of the dynamics of glycine-121 of Escherichia coli dihydrofolate reductase obtained from kinetic analysis of a site-directed mutant
    • DOI 10.1021/bi9716231
    • Cameron CE, Benkovic SJ (1997) Evidence for a functional role of the dynamics of glycine-121 of Escherichia coli dihydrofolate reductase obtained from kinetic analysis of a site-directed mutant. Biochemistry 36:15792-15800. (Pubitemid 28027379)
    • (1997) Biochemistry , vol.36 , Issue.50 , pp. 15792-15800
    • Cameron, C.E.1    Benkovic, S.J.2
  • 4
    • 77951226274 scopus 로고    scopus 로고
    • At the dawn of the 21st century: Is dynamics the missing link for understanding enzyme catalysis?
    • Kamerlin SCL, Warshel A (2010) At the dawn of the 21st century: Is dynamics the missing link for understanding enzyme catalysis? Proteins 78:1339-1375.
    • (2010) Proteins , vol.78 , pp. 1339-1375
    • Kamerlin, S.C.L.1    Warshel, A.2
  • 5
    • 36849039429 scopus 로고    scopus 로고
    • A hierarchy of timescales in protein dynamics is linked to enzyme catalysis
    • DOI 10.1038/nature06407, PII NATURE06407
    • Henzler-Wildman KA, et al. (2007) A hierarchy of timescales in protein dynamics is linked to enzyme catalysis. Nature 450:913-916. (Pubitemid 350231333)
    • (2007) Nature , vol.450 , Issue.7171 , pp. 913-916
    • Henzler-Wildman, K.A.1    Lei, M.2    Thai, V.3    Kerns, S.J.4    Karplus, M.5    Kern, D.6
  • 6
    • 79953823548 scopus 로고    scopus 로고
    • A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis
    • Bhabha G, et al. (2011) A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis. Science 332:234-238.
    • (2011) Science , vol.332 , pp. 234-238
    • Bhabha, G.1
  • 7
    • 71449103005 scopus 로고    scopus 로고
    • Hidden alternative structures of proline isomerase essential for catalysis
    • Fraser JS, et al. (2009) Hidden alternative structures of proline isomerase essential for catalysis. Nature 462:669-673.
    • (2009) Nature , vol.462 , pp. 669-673
    • Fraser, J.S.1
  • 8
    • 77749239790 scopus 로고    scopus 로고
    • Ketosteroid isomerase provides further support to the idea that enzymes work by electrostatic preorganization
    • Kamerlin SCL, Sharma PK, Chu ZT, Warshel A (2010) Ketosteroid isomerase provides further support to the idea that enzymes work by electrostatic preorganization. Proc Natl Acad Sci USA 107:4075-4080.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 4075-4080
    • Kamerlin, S.C.L.1    Sharma, P.K.2    Chu, Z.T.3    Warshel, A.4
  • 10
    • 0000230329 scopus 로고
    • Energetics of enzyme catalysis
    • Warshel A (1978) Energetics of enzyme catalysis. Proc Natl Acad Sci USA 75:5250-5254.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 5250-5254
    • Warshel, A.1
  • 12
    • 34249104188 scopus 로고    scopus 로고
    • The catalytic effect of dihydrofolate reductase and its mutants is determined by reorganization energies
    • DOI 10.1021/bi700201w
    • Liu H, Warshel A (2007) The catalytic effect of dihydrofolate reductase and its mutants is determined by reorganization energies. Biochemistry 46:6011-6025. (Pubitemid 46799163)
    • (2007) Biochemistry , vol.46 , Issue.20 , pp. 6011-6025
    • Liu, H.1    Warshel, A.2
  • 13
    • 0000969221 scopus 로고
    • Dynamics of enzymatic reactions
    • Warshel A (1984) Dynamics of enzymatic reactions. Proc Natl Acad Sci USA 81:444-448.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 444-448
    • Warshel, A.1
  • 14
    • 34547456661 scopus 로고    scopus 로고
    • Origin of the temperature dependence of isotope effects in enzymatic reactions: The case of dihydrofolate reductase
    • DOI 10.1021/jp070938f
    • Liu H, Warshel A (2007) Origin of the temperature dependence of isotope effects in enzymatic reactions: The case of dihydrofolate reductase. J Phys ChemB 111:7852-7861. (Pubitemid 47169697)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.27 , pp. 7852-7861
    • Liu, H.1    Warshel, A.2
  • 15
    • 37349007321 scopus 로고    scopus 로고
    • On the relationship between thermal stability and catalytic power of enzymes
    • DOI 10.1021/bi701732a
    • Roca M, Liu H, Messer B, Warshel A (2007) On the relationship between thermal stability and catalytic power of enzymes. Biochemistry 46:15076-15088. (Pubitemid 350308899)
    • (2007) Biochemistry , vol.46 , Issue.51 , pp. 15076-15088
    • Roca, M.1    Liu, H.2    Messer, B.3    Warshel, A.4
  • 16
    • 43049134414 scopus 로고    scopus 로고
    • The energetics of the primary proton transfer in bacteriorhodopsin revisited: It is a sequential light induced charge separation after all
    • Braun-Sand S, Sharma PK, Chu ZT, Pisliakov AV, Warshel A (2008) The energetics of the primary proton transfer in bacteriorhodopsin revisited: It is a sequential light induced charge separation after all. Biochim Biophys Acta 1777:441-452.
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 441-452
    • Braun-Sand, S.1    Sharma, P.K.2    Chu, Z.T.3    Pisliakov, A.V.4    Warshel, A.5
  • 17
    • 0344736689 scopus 로고    scopus 로고
    • Converting conformational changes to electrostatic energy in molecular motors: The energetics of ATP synthase
    • Štrajbl M, Shurki A, Warshel A (2003) Converting conformational changes to electrostatic energy in molecular motors: The energetics of ATP synthase. Proc Natl Acad Sci USA 100:14834-14839.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 14834-14839
    • Štrajbl, M.1    Shurki, A.2    Warshel, A.3
  • 18
    • 70350453758 scopus 로고    scopus 로고
    • Enzyme millisecond conformational dynamics do not catalyze the chemical step
    • Pisliakov AV, Cao J, Kamerlin SCL, Warshel A (2009) Enzyme millisecond conformational dynamics do not catalyze the chemical step. Proc Natl Acad Sci USA 106:17359-17364.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 17359-17364
    • Pisliakov, A.V.1    Cao, J.2    Kamerlin, S.C.L.3    Warshel, A.4
  • 19
    • 33646935697 scopus 로고    scopus 로고
    • Dynamical contributions to enzyme catalysis: Critical tests of a popular hypothesis
    • DOI 10.1021/cr040427e
    • Olsson MHM, Parson WW, Warshel A (2006) Dynamical contributions to enzyme catalysis: Critical tests of a popular hypothesis. Chem Rev 106:1737-1756. (Pubitemid 43792778)
    • (2006) Chemical Reviews , vol.106 , Issue.5 , pp. 1737-1756
    • Olsson, M.H.M.1    Parson, W.W.2    Warshel, A.3
  • 20
    • 0033988897 scopus 로고    scopus 로고
    • Redistribution and loss of side chain entropy upon formation of a calmodulin-peptide complex
    • DOI 10.1038/71280
    • Lee AL, Kinnear SA, Wand JA (2000) Redistribution and loss of side chain entropy upon formation of a calmodulin-peptide complex. Nat Struct Biol 7:72-77. (Pubitemid 30043252)
    • (2000) Nature Structural Biology , vol.7 , Issue.1 , pp. 72-77
    • Lee, A.L.1    Kinnear, S.A.2    Wand, A.J.3
  • 22
    • 0034710867 scopus 로고    scopus 로고
    • How important are entropy contributions in enzymatic catalysis?
    • Villà J, et al. (2000) How important are entropy contributions in enzymatic catalysis? Proc Natl Acad Sci USA 97:11899-11904.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 11899-11904
    • Villà, J.1
  • 23
    • 79958826524 scopus 로고    scopus 로고
    • Protein dynamics and enzyme catalysis: Insight from simulations
    • McGeagh JD, Ranaghan KE, Mulholland AJ (2011) Protein dynamics and enzyme catalysis: Insight from simulations. Biochim Biophys Acta 1814:1077-1092.
    • (2011) Biochim Biophys Acta , vol.1814 , pp. 1077-1092
    • McGeagh, J.D.1    Ranaghan, K.E.2    Mulholland, A.J.3
  • 24
    • 0034919305 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for quantifying microsecond-to- millisecond motions in biological macromolecules
    • DOI 10.1016/S0076-6879(01)39315-1
    • Palmer AG, Kroenke CD, Loria JP (2001) Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules. Methods Enzymol 339:204-238. (Pubitemid 32666562)
    • (2001) Methods in Enzymology , vol.339 , pp. 204-238
    • Palmer III, A.G.1    Kroenke, C.D.2    Loria, J.P.3
  • 25
    • 33645834303 scopus 로고    scopus 로고
    • New tools provide new insights in NMR studies of protein dynamics
    • Mittermaier A, Kay LE (2006) New tools provide new insights in NMR studies of protein dynamics. Science 312:224-228.
    • (2006) Science , vol.312 , pp. 224-228
    • Mittermaier, A.1    Kay, L.E.2
  • 26
    • 34250872269 scopus 로고    scopus 로고
    • Minimalist active-site redesign: Teaching old enzymes new tricks
    • Toscano MD, Woycechowsky KJ, Hilvert D (2007) Minimalist active-site redesign: Teaching old enzymes new tricks. Angew Chem Int Ed Engl 46:4468-4470.
    • (2007) Angew Chem Int Ed Engl , vol.46 , pp. 4468-4470
    • Toscano, M.D.1    Woycechowsky, K.J.2    Hilvert, D.3
  • 27
    • 0025891413 scopus 로고
    • Electrostatic energy and macromolecular function
    • Warshel A, Åqvist J (1991) Electrostatic energy and macromolecular function. Annu Rev Biophys Chem 20:267-298.
    • (1991) Annu Rev Biophys Chem , vol.20 , pp. 267-298
    • Warshel, A.1    Åqvist, J.2
  • 28
    • 0024445808 scopus 로고
    • Dispersed polaron simulations of electron transfer in photosynthetic reaction centers
    • Warshel A, Chu ZT, Parson WW (1989) Dispersed polaron simulations of electrontransfer in photosynthetic reaction centers. Science 246:112-116. (Pubitemid 19252088)
    • (1989) Science , vol.246 , Issue.4926 , pp. 112-116
    • Warshel, A.1    Chu, Z.T.2    Parson, W.W.3
  • 29
    • 0034760077 scopus 로고    scopus 로고
    • Dynamic activation of protein function: A view emerging from nmr spectroscopy
    • Wand AJ (2001) Dynamic activation of protein function: A view emerging from nmr spectroscopy. Nat Struct Biol 8:926-931.
    • (2001) Nat Struct Biol , vol.8 , pp. 926-931
    • Wand, A.J.1
  • 30
    • 0000728542 scopus 로고
    • Microscopic and semimicroscopic calculations of electrostatic energies in proteins by the polaris and enzymix programs
    • Lee FS, Chu ZT, Warshel A (1993) Microscopic and semimicroscopic calculations of electrostatic energies in proteins by the polaris and enzymix programs. J Comput Chem 14:161-185.
    • (1993) J Comput Chem , vol.14 , pp. 161-185
    • Lee, F.S.1    Chu, Z.T.2    Warshel, A.3
  • 33
    • 0000115003 scopus 로고
    • A local reaction field method for fast evaluation of long-range electrostatic interactions in molecular simulations
    • Lee FS, Warshel A (1992) A local reaction field method for fast evaluation of long-range electrostatic interactions in molecular simulations. J Chem Phys 97:3100-3107.
    • (1992) J Chem Phys , vol.97 , pp. 3100-3107
    • Lee, F.S.1    Warshel, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.