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Volumn 105, Issue 2-3, 2003, Pages 559-572

Thermodynamic and extrathermodynamic requirements of enzyme catalysis

Author keywords

Binding; Enzyme catalysis; Inhibition; Thermodynamics; Transition state

Indexed keywords

CARBON DIOXIDE; CHORISMIC ACID; ENZYME; ENZYME INHIBITOR; GLYCINE; GLYCOLIC ACID DERIVATIVE; GLYCOSIDE; HYDROGEN; PEPTIDE; PHOSPHATASE; PHOSPHODIESTERASE; PURINE; SOLVENT; TRIOSEPHOSPHATE ISOMERASE; WATER;

EID: 0141448966     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(03)00066-8     Document Type: Article
Times cited : (71)

References (59)
  • 1
    • 0141551446 scopus 로고
    • P.D. Boyer, H. Lardy, & K. Myrbäck. New York: Academic Press
    • Segal H.I. Boyer P.D., Lardy H., Myrbäck K. The Enzymes, vol. 1. 2nd ed. 1959;1-48 Academic Press, New York.
    • (1959) The Enzymes, vol. 1 2nd ed. , pp. 1-48
    • Segal, H.I.1
  • 5
    • 0003035923 scopus 로고
    • Strain and conformation change in enzymatic catalysis
    • N.O. Kaplan, & E.P. Kennedy. New York: Academic Press. p. 273
    • Jencks W.P. Strain and conformation change in enzymatic catalysis. Kaplan N.O., Kennedy E.P. Current Aspects of Biochemical Energetics. 1966;Academic Press, New York. p. 273.
    • (1966) Current Aspects of Biochemical Energetics
    • Jencks, W.P.1
  • 6
    • 0014681301 scopus 로고
    • Transition states for enzyme catalysis
    • Wolfenden R. Transition states for enzyme catalysis. Nature. 223:1969;704.
    • (1969) Nature , vol.223 , pp. 704
    • Wolfenden, R.1
  • 7
    • 0002903441 scopus 로고
    • Analog approaches to the transition state in enzyme reactions
    • Wolfenden R. Analog approaches to the transition state in enzyme reactions. Acc. Chem. Res. 5:1972;10-18.
    • (1972) Acc. Chem. Res. , vol.5 , pp. 10-18
    • Wolfenden, R.1
  • 8
    • 0016239830 scopus 로고
    • Enzyme catalysis: Conflicting requirements of substrate access and transition state affinity
    • Wolfenden R. Enzyme catalysis: conflicting requirements of substrate access and transition state affinity. Mol. Cell. Biochem. 3:1974;207.
    • (1974) Mol. Cell. Biochem. , vol.3 , pp. 207
    • Wolfenden, R.1
  • 9
    • 0015101706 scopus 로고
    • Entropic contributions to rate accelerations in enzymes and intramolecular reactions and the chelate effect
    • Page M.L., Jencks W.P. Entropic contributions to rate accelerations in enzymes and intramolecular reactions and the chelate effect. Proc. Natl. Acad. Sci. USA. 68:1971;1678.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 1678
    • Page, M.L.1    Jencks, W.P.2
  • 10
    • 0015924871 scopus 로고
    • Enzymatic catalysis and transition-state theory
    • Lienhard G.E. Enzymatic catalysis and transition-state theory. Science. 180:1973;149.
    • (1973) Science , vol.180 , pp. 149
    • Lienhard, G.E.1
  • 12
    • 0021049880 scopus 로고
    • Waterlogged molecules
    • Wolfenden R. Waterlogged molecules. Science. 222:1983;1087.
    • (1983) Science , vol.222 , pp. 1087
    • Wolfenden, R.1
  • 13
    • 0017072736 scopus 로고
    • Transition-state analogs for thiamin pyrophosphate-dependent enzymes
    • Gutowski J.A., Lienhard G.E. Transition-state analogs for thiamin pyrophosphate-dependent enzymes. J. Biol. Chem. 251:1976;2863.
    • (1976) J. Biol. Chem. , vol.251 , pp. 2863
    • Gutowski, J.A.1    Lienhard, G.E.2
  • 14
    • 0019327232 scopus 로고
    • Specific and potent inhibition of spermidine synthase by the transition-state analog S-adenosyl-3-thio-1,8-diaminooctane
    • Tang K.C., Pegg A.E., Coward J.K. Specific and potent inhibition of spermidine synthase by the transition-state analog S-adenosyl-3-thio-1,8-diaminooctane. Biochem. Biophys. Res. Commun. 96:1980;1371.
    • (1980) Biochem. Biophys. Res. Commun. , vol.96 , pp. 1371
    • Tang, K.C.1    Pegg, A.E.2    Coward, J.K.3
  • 16
    • 0040362704 scopus 로고    scopus 로고
    • Chemical basis for enzyme catalysis
    • Bruice T.C., Benkovic S.J. Chemical basis for enzyme catalysis. Biochemistry. 39:2000;6267.
    • (2000) Biochemistry , vol.39 , pp. 6267
    • Bruice, T.C.1    Benkovic, S.J.2
  • 18
    • 0004253933 scopus 로고
    • E.R. Blout, F.A. Bovey, M. Goodman, & M. Lotan. New York: Wiley
    • Levitt M. Blout E.R., Bovey F.A., Goodman M., Lotan M. Peptides, Polypeptides and Proteins. 1974;99-140 Wiley, New York.
    • (1974) Peptides, Polypeptides and Proteins , pp. 99-140
    • Levitt, M.1
  • 19
    • 0001261805 scopus 로고
    • Some aspects of the thermodynamics and mechanism of enzymic catalysis
    • P.D. Boyer, H. Lardy, & K. Myrbäck. New York: Academic Press
    • Lumry R. Some aspects of the thermodynamics and mechanism of enzymic catalysis. Boyer P.D., Lardy H., Myrbäck K. The Enzymes, vol. 1. 2nd ed. 1959;157-232 Academic Press, New York.
    • (1959) The Enzymes, vol. 1 2nd ed. , pp. 157-232
    • Lumry, R.1
  • 21
    • 0037177245 scopus 로고    scopus 로고
    • Catalysis by entropic effects alone: The action of cytidine deaminase on 5,6-dihydrocytidine
    • Snider M.J., Wolfenden R. Catalysis by entropic effects alone: the action of cytidine deaminase on 5,6-dihydrocytidine. Biochemistry. 41:2002;3925.
    • (2002) Biochemistry , vol.41 , pp. 3925
    • Snider, M.J.1    Wolfenden, R.2
  • 22
    • 0141439930 scopus 로고    scopus 로고
    • Enzymatic hydration of an olefin: The burden borne by fumarase
    • Bearne S.L., Wolfenden R. Enzymatic hydration of an olefin: the burden borne by fumarase. J. Am. Chem. Soc. 120:1997;833.
    • (1997) J. Am. Chem. Soc. , vol.120 , pp. 833
    • Bearne, S.L.1    Wolfenden, R.2
  • 23
    • 0028228418 scopus 로고
    • The entropic cost of bound water in crystals and biomolecules
    • Dunitz J.D. The entropic cost of bound water in crystals and biomolecules. Science. 264:1994;670.
    • (1994) Science , vol.264 , pp. 670
    • Dunitz, J.D.1
  • 24
    • 0035949442 scopus 로고    scopus 로고
    • Site-bound water and the shortcomings of a less than perfect transition-state analogue inhibitor
    • Snider M.J., Wolfenden R. Site-bound water and the shortcomings of a less than perfect transition-state analogue inhibitor. Biochemistry. 40:2001;11364.
    • (2001) Biochemistry , vol.40 , pp. 11364
    • Snider, M.J.1    Wolfenden, R.2
  • 27
    • 0016904563 scopus 로고
    • Transition-state analogue inhibitors and enzyme catalysis
    • Wolfenden R. Transition-state analogue inhibitors and enzyme catalysis. Annu. Rev. Biophys. Bioeng. 5:1976;271.
    • (1976) Annu. Rev. Biophys. Bioeng. , vol.5 , pp. 271
    • Wolfenden, R.1
  • 29
    • 0031688282 scopus 로고    scopus 로고
    • Enzymatic transition states and transition state analog complexes
    • Schramm V.L. Enzymatic transition states and transition state analog complexes. Annu. Rev. Biochem. 67:1998;693.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 693
    • Schramm, V.L.1
  • 30
  • 34
    • 0029967409 scopus 로고    scopus 로고
    • Enzyme-substrate complexes of adenosine and cytidine deaminases: Absence of accumulation of water adducts
    • Shih P., Wolfenden R. Enzyme-substrate complexes of adenosine and cytidine deaminases: absence of accumulation of water adducts. Biochemistry. 35:1996;4697.
    • (1996) Biochemistry , vol.35 , pp. 4697
    • Shih, P.1    Wolfenden, R.2
  • 36
    • 0024974086 scopus 로고
    • The contribution of a single hydroxyl group to transition state discrimination by adenosine deaminase
    • Kati W.M., Wolfenden R. The contribution of a single hydroxyl group to transition state discrimination by adenosine deaminase. Biochemistry. 28:1989;7919.
    • (1989) Biochemistry , vol.28 , pp. 7919
    • Kati, W.M.1    Wolfenden, R.2
  • 39
    • 0000589080 scopus 로고
    • Mechanisms of transfer enzymes
    • P.D. Boyer, H. Lardy, & K. Jr. Myrbäck. New York: Academic Press
    • Koshland D.E. Mechanisms of transfer enzymes. Boyer P.D., Lardy H., Myrbäck K. Jr. The Enzymes, vol. 1. 2nd ed. 1959;305-345 Academic Press, New York.
    • (1959) The Enzymes, vol. 1 2nd ed. , pp. 305-345
    • Koshland, D.E.1
  • 40
    • 0014944184 scopus 로고
    • Changes in absorption spectrum and crystal structure of triosephosphate isomerase brought about by 2-phosphoglycollate, a potential transition-state analogue inhibitor
    • Johnson L., Wolfenden R. Changes in absorption spectrum and crystal structure of triosephosphate isomerase brought about by 2-phosphoglycollate, a potential transition-state analogue inhibitor. J. Mol. Biol. 47:1970;93.
    • (1970) J. Mol. Biol. , vol.47 , pp. 93
    • Johnson, L.1    Wolfenden, R.2
  • 42
    • 0028057520 scopus 로고
    • Cytidine deaminase: 2.3-Å crystal structure of an enzyme-transition-state analog complex
    • Betts L., Xiang S., Short S.A., Wolfenden R., Carter C.W. Jr. Cytidine deaminase: 2.3-Å crystal structure of an enzyme-transition-state analog complex. J. Mol. Biol. 235:1994;635.
    • (1994) J. Mol. Biol. , vol.235 , pp. 635
    • Betts, L.1    Xiang, S.2    Short, S.A.3    Wolfenden, R.4    Carter C.W., Jr.5
  • 43
  • 45
    • 0030887895 scopus 로고    scopus 로고
    • The structure of the cytidine deaminase-product complex provides evidence for efficient proton transfer and ground-state destabilization
    • Xiang S., Short S.A., Wolfenden R., Carter C.W. Jr. The structure of the cytidine deaminase-product complex provides evidence for efficient proton transfer and ground-state destabilization. Biochemistry. 36:1997;4768.
    • (1997) Biochemistry , vol.36 , pp. 4768
    • Xiang, S.1    Short, S.A.2    Wolfenden, R.3    Carter C.W., Jr.4
  • 46
    • 0026746306 scopus 로고
    • A transition state in pieces: Major contributions of entropic effects to ligand binding by adenosine deaminase
    • Kati W.M., Acheson S.A., Wolfenden R. A transition state in pieces: major contributions of entropic effects to ligand binding by adenosine deaminase. Biochemistry. 31:1992;7356.
    • (1992) Biochemistry , vol.31 , pp. 7356
    • Kati, W.M.1    Acheson, S.A.2    Wolfenden, R.3
  • 47
    • 0032566330 scopus 로고    scopus 로고
    • Substrate connectivity effects in the transition state for cytidine deaminase
    • Carlow D.C., Wolfenden R. Substrate connectivity effects in the transition state for cytidine deaminase. Biochemistry. 37:1998;11873.
    • (1998) Biochemistry , vol.37 , pp. 11873
    • Carlow, D.C.1    Wolfenden, R.2
  • 48
    • 0032435359 scopus 로고    scopus 로고
    • Effects of substrate binding determinants on the transition state for orotidine 5′-monophosphate decarboxylase
    • Miller B.G., Traut T.W., Wolfenden R. Effects of substrate binding determinants on the transition state for orotidine 5′-monophosphate decarboxylase. Bioorg. Chem. 26:1998;283.
    • (1998) Bioorg. Chem. , vol.26 , pp. 283
    • Miller, B.G.1    Traut, T.W.2    Wolfenden, R.3
  • 49
  • 53
    • 0019321956 scopus 로고
    • Transition-state affinity jump chromatography
    • Andersson L., Wolfenden R. Transition-state affinity jump chromatography. J. Biol. Chem. 255:1980;11106.
    • (1980) J. Biol. Chem. , vol.255 , pp. 11106
    • Andersson, L.1    Wolfenden, R.2
  • 56
    • 0030037715 scopus 로고    scopus 로고
    • Rates of uncatalyzed hydrolysis of peptide bonds in neutral solution, and the transition state affinities of proteases
    • Radzicka A., Wolfenden R. Rates of uncatalyzed hydrolysis of peptide bonds in neutral solution, and the transition state affinities of proteases. J. Am. Chem. Soc. 118:1996;6105.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 6105
    • Radzicka, A.1    Wolfenden, R.2
  • 57
    • 0032481372 scopus 로고    scopus 로고
    • Spontaneous hydrolysis of ionized phosphate monoesters and diester and the proficiencies of phosphatases and phosphodiesterases as catalysts
    • Wolfenden R., Ridgway C., Young G. Spontaneous hydrolysis of ionized phosphate monoesters and diester and the proficiencies of phosphatases and phosphodiesterases as catalysts. J. Am. Chem. Soc. 120:1998;833.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 833
    • Wolfenden, R.1    Ridgway, C.2    Young, G.3
  • 59
    • 0035997393 scopus 로고    scopus 로고
    • Catalytic proficiency: The unusual case of OMP decarboxylase
    • Miller B.G., Wolfenden R. Catalytic proficiency: the unusual case of OMP decarboxylase. Annu. Rev. Biochem. 71:2002;847.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 847
    • Miller, B.G.1    Wolfenden, R.2


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