메뉴 건너뛰기




Volumn 51, Issue 30, 2012, Pages 5894-5902

Conformational selection or induced fit? A critical appraisal of the kinetic mechanism

Author keywords

[No Author keywords available]

Indexed keywords

APPROACH TO EQUILIBRIUM; BIOLOGICAL MACROMOLECULE; COMPETING MECHANISMS; CONFORMATIONAL ISOMERIZATION; CONFORMATIONAL SELECTION; CONFORMATIONAL TRANSITIONS; GLUCOKINASE; INDUCED FIT; KINETIC MECHANISM; KINETIC PROPERTIES; LIGAND BINDING; LIGAND CONCENTRATION; LIGAND DISSOCIATION; LIGAND RECOGNITION; RAPID EQUILIBRIUM; TWO-STEP MECHANISMS;

EID: 84864462749     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi3006913     Document Type: Article
Times cited : (263)

References (44)
  • 1
    • 4544381198 scopus 로고    scopus 로고
    • Biochemical mechanisms of drug action: What does it take for success?
    • Swinney, D. C. (2004) Biochemical mechanisms of drug action: What does it take for success? Nat. Rev. Drug Discovery 3, 801-808
    • (2004) Nat. Rev. Drug Discovery , vol.3 , pp. 801-808
    • Swinney, D.C.1
  • 2
    • 0004244695 scopus 로고
    • University Science Books, Mill Valley, CA.
    • Wyman, J. and Gill, S. J. (1990) Binding and Linkage, University Science Books, Mill Valley, CA.
    • (1990) Binding and Linkage
    • Wyman, J.1    Gill, S.J.2
  • 4
    • 69549120472 scopus 로고    scopus 로고
    • Conformational selection or induced fit: A flux description of reaction mechanism
    • Hammes, G. G., Chang, Y. C., and Oas, T. G. (2009) Conformational selection or induced fit: A flux description of reaction mechanism Proc. Natl. Acad. Sci. U.S.A. 106, 13737-13741
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 13737-13741
    • Hammes, G.G.1    Chang, Y.C.2    Oas, T.G.3
  • 5
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod, J., Wyman, J., and Changeux, J. P. (1965) On the nature of allosteric transitions: A plausible model J. Mol. Biol. 12, 88-118
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 6
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • Koshland, D. E., Jr., Nemethy, G., and Filmer, D. (1966) Comparison of experimental binding data and theoretical models in proteins containing subunits Biochemistry 5, 365-385
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • Koshland Jr., D.E.1    Nemethy, G.2    Filmer, D.3
  • 7
    • 0001858251 scopus 로고
    • Application of a Theory of Enzyme Specificity to Protein Synthesis
    • Koshland, D. E. (1958) Application of a Theory of Enzyme Specificity to Protein Synthesis Proc. Natl. Acad. Sci. U.S.A. 44, 98-104
    • (1958) Proc. Natl. Acad. Sci. U.S.A. , vol.44 , pp. 98-104
    • Koshland, D.E.1
  • 8
    • 80053539881 scopus 로고    scopus 로고
    • Conformational selection or induced fit? 50 years of debate resolved
    • Changeux, J. P. and Edelstein, S. (2011) Conformational selection or induced fit? 50 years of debate resolved Biol. Rep. 3, 19
    • (2011) Biol. Rep. , vol.3 , pp. 19
    • Changeux, J.P.1    Edelstein, S.2
  • 9
    • 77949587817 scopus 로고    scopus 로고
    • From induced fit to conformational selection: A continuum of binding mechanism controlled by the timescale of conformational transitions
    • Zhou, H. X. (2010) From induced fit to conformational selection: A continuum of binding mechanism controlled by the timescale of conformational transitions Biophys. J. 98, L15-L17
    • (2010) Biophys. J. , vol.98
    • Zhou, H.X.1
  • 11
    • 44049103958 scopus 로고    scopus 로고
    • Residence time of receptor-ligand complexes and its effect on biological function
    • Tummino, P. J. and Copeland, R. A. (2008) Residence time of receptor-ligand complexes and its effect on biological function Biochemistry 47, 5481-5492
    • (2008) Biochemistry , vol.47 , pp. 5481-5492
    • Tummino, P.J.1    Copeland, R.A.2
  • 13
    • 55549109430 scopus 로고    scopus 로고
    • Role of induced fit in enzyme specificity: A molecular forward/reverse switch
    • Johnson, K. A. (2008) Role of induced fit in enzyme specificity: A molecular forward/reverse switch J. Biol. Chem. 283, 26297-26301
    • (2008) J. Biol. Chem. , vol.283 , pp. 26297-26301
    • Johnson, K.A.1
  • 14
    • 77953509941 scopus 로고    scopus 로고
    • Engineering thrombin for selective specificity toward protein C and PAR1
    • Marino, F., Pelc, L. A., Vogt, A., Gandhi, P. S., and Di Cera, E. (2010) Engineering thrombin for selective specificity toward protein C and PAR1 J. Biol. Chem. 285, 19145-19152
    • (2010) J. Biol. Chem. , vol.285 , pp. 19145-19152
    • Marino, F.1    Pelc, L.A.2    Vogt, A.3    Gandhi, P.S.4    Di Cera, E.5
  • 15
    • 81855199864 scopus 로고    scopus 로고
    • Crystal structures of prethrombin-2 reveal alternative conformations under identical solution conditions and the mechanism of zymogen activation
    • Pozzi, N., Chen, Z., Zapata, F., Pelc, L. A., Barranco-Medina, S., and Di Cera, E. (2011) Crystal structures of prethrombin-2 reveal alternative conformations under identical solution conditions and the mechanism of zymogen activation Biochemistry 50, 10195-10202
    • (2011) Biochemistry , vol.50 , pp. 10195-10202
    • Pozzi, N.1    Chen, Z.2    Zapata, F.3    Pelc, L.A.4    Barranco-Medina, S.5    Di Cera, E.6
  • 16
    • 0031053519 scopus 로고    scopus 로고
    • Inhibitory mechanism of serpins. Identification of steps involving the active-site serine residue of the protease
    • Stone, S. R. and Le Bonniec, B. F. (1997) Inhibitory mechanism of serpins. Identification of steps involving the active-site serine residue of the protease J. Mol. Biol. 265, 344-362
    • (1997) J. Mol. Biol. , vol.265 , pp. 344-362
    • Stone, S.R.1    Le Bonniec, B.F.2
  • 17
    • 0037438708 scopus 로고    scopus 로고
    • Dissecting substrate recognition by thrombin using the inactive mutant S195A
    • Krem, M. M. and Di Cera, E. (2003) Dissecting substrate recognition by thrombin using the inactive mutant S195A Biophys. Chem. 100, 315-323
    • (2003) Biophys. Chem. , vol.100 , pp. 315-323
    • Krem, M.M.1    Di Cera, E.2
  • 18
    • 0020490418 scopus 로고
    • P-Aminobenzamidine as a fluorescent probe for the active site of serine proteases
    • Evans, S. A., Olson, S. T., and Shore, J. D. (1982) p-Aminobenzamidine as a fluorescent probe for the active site of serine proteases J. Biol. Chem. 257, 3014-3017
    • (1982) J. Biol. Chem. , vol.257 , pp. 3014-3017
    • Evans, S.A.1    Olson, S.T.2    Shore, J.D.3
  • 20
    • 0030810220 scopus 로고    scopus 로고
    • Kinetic pathway for the slow to fast transition of thrombin. Evidence of linked ligand binding at structurally distinct domains
    • Lai, M. T., Di Cera, E., and Shafer, J. A. (1997) Kinetic pathway for the slow to fast transition of thrombin. Evidence of linked ligand binding at structurally distinct domains J. Biol. Chem. 272, 30275-30282
    • (1997) J. Biol. Chem. , vol.272 , pp. 30275-30282
    • Lai, M.T.1    Di Cera, E.2    Shafer, J.A.3
  • 21
    • 33745150728 scopus 로고    scopus 로고
    • Glucose-induced conformational changes in glucokinase mediate allosteric regulation: Transient kinetic analysis
    • Heredia, V. V., Thomson, J., Nettleton, D., and Sun, S. (2006) Glucose-induced conformational changes in glucokinase mediate allosteric regulation: Transient kinetic analysis Biochemistry 45, 7553-7562
    • (2006) Biochemistry , vol.45 , pp. 7553-7562
    • Heredia, V.V.1    Thomson, J.2    Nettleton, D.3    Sun, S.4
  • 22
    • 33846809257 scopus 로고    scopus 로고
    • A pre-steady state analysis of ligand binding to human glucokinase: Evidence for a preexisting equilibrium
    • Kim, Y. B., Kalinowski, S. S., and Marcinkeviciene, J. (2007) A pre-steady state analysis of ligand binding to human glucokinase: Evidence for a preexisting equilibrium Biochemistry 46, 1423-1431
    • (2007) Biochemistry , vol.46 , pp. 1423-1431
    • Kim, Y.B.1    Kalinowski, S.S.2    Marcinkeviciene, J.3
  • 23
    • 67049098985 scopus 로고    scopus 로고
    • Binding kinetics of glucose and allosteric activators to human glucokinase reveal multiple conformational states
    • Antoine, M., Boutin, J. A., and Ferry, G. (2009) Binding kinetics of glucose and allosteric activators to human glucokinase reveal multiple conformational states Biochemistry 48, 5466-5482
    • (2009) Biochemistry , vol.48 , pp. 5466-5482
    • Antoine, M.1    Boutin, J.A.2    Ferry, G.3
  • 26
    • 79960541421 scopus 로고    scopus 로고
    • Allostery in trypsin-like proteases suggests new therapeutic strategies
    • Gohara, D. W. and Di Cera, E. (2011) Allostery in trypsin-like proteases suggests new therapeutic strategies Trends Biotechnol. 29, 577-585
    • (2011) Trends Biotechnol. , vol.29 , pp. 577-585
    • Gohara, D.W.1    Di Cera, E.2
  • 30
  • 34
    • 0037174838 scopus 로고    scopus 로고
    • Ser(214) is crucial for substrate binding to serine proteases
    • Krem, M. M., Prasad, S., and Di Cera, E. (2002) Ser(214) is crucial for substrate binding to serine proteases J. Biol. Chem. 277, 40260-40264
    • (2002) J. Biol. Chem. , vol.277 , pp. 40260-40264
    • Krem, M.M.1    Prasad, S.2    Di Cera, E.3
  • 35
    • 24044468582 scopus 로고    scopus 로고
    • Kinetics of allosteric conformational transition of a macromolecule prior to ligand binding: Analysis of stopped-flow kinetic experiments
    • Galletto, R., Jezewska, M. J., and Bujalowski, W. (2005) Kinetics of allosteric conformational transition of a macromolecule prior to ligand binding: Analysis of stopped-flow kinetic experiments Cell Biochem. Biophys. 42, 121-144
    • (2005) Cell Biochem. Biophys. , vol.42 , pp. 121-144
    • Galletto, R.1    Jezewska, M.J.2    Bujalowski, W.3
  • 36
    • 0015152607 scopus 로고
    • Escherichia coli alkaline phosphatase. An analysis of transient kinetics
    • Halford, S. E. (1971) Escherichia coli alkaline phosphatase. An analysis of transient kinetics Biochem. J. 125, 319-327
    • (1971) Biochem. J. , vol.125 , pp. 319-327
    • Halford, S.E.1
  • 37
    • 0015223374 scopus 로고
    • Equilibrium and rate constants for the interconversion of two conformations of α-chymotrypsin. The existence of a catalytically inactive conformation at neutral pH
    • Fersht, A. R. and Requena, Y. (1971) Equilibrium and rate constants for the interconversion of two conformations of α-chymotrypsin. The existence of a catalytically inactive conformation at neutral pH J. Mol. Biol. 60, 279-290
    • (1971) J. Mol. Biol. , vol.60 , pp. 279-290
    • Fersht, A.R.1    Requena, Y.2
  • 39
  • 40
    • 24644521419 scopus 로고    scopus 로고
    • Structure and kinetics of a transient antibody binding intermediate reveal a kinetic discrimination mechanism in antigen recognition
    • James, L. C. and Tawfik, D. S. (2005) Structure and kinetics of a transient antibody binding intermediate reveal a kinetic discrimination mechanism in antigen recognition Proc. Natl. Acad. Sci. U.S.A. 102, 12730-12735
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 12730-12735
    • James, L.C.1    Tawfik, D.S.2
  • 41
    • 79851474946 scopus 로고    scopus 로고
    • Intrinsic Z-DNA is stabilized by the conformational selection mechanism of Z-DNA-binding proteins
    • Bae, S., Kim, D., Kim, K. K., Kim, Y. G., and Hohng, S. (2011) Intrinsic Z-DNA is stabilized by the conformational selection mechanism of Z-DNA-binding proteins J. Am. Chem. Soc. 133, 668-671
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 668-671
    • Bae, S.1    Kim, D.2    Kim, K.K.3    Kim, Y.G.4    Hohng, S.5
  • 42
    • 35548976322 scopus 로고    scopus 로고
    • Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR
    • Tang, C., Schwieters, C. D., and Clore, G. M. (2007) Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR Nature 449, 1078-1082
    • (2007) Nature , vol.449 , pp. 1078-1082
    • Tang, C.1    Schwieters, C.D.2    Clore, G.M.3
  • 44
    • 0037059041 scopus 로고    scopus 로고
    • A hypothesis concerning diffusion-limited protein-ligand interactions
    • van Holde, K. E. (2002) A hypothesis concerning diffusion-limited protein-ligand interactions Biophys. Chem. 101-102, 249-254
    • (2002) Biophys. Chem. , vol.101-102 , pp. 249-254
    • Van Holde, K.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.