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Volumn 37, Issue 4, 2004, Pages 394-401

Understanding enzyme structure and function in terms of the shifting specificity model

Author keywords

Enzyme catalysis; Haldane; Shifting specificity model

Indexed keywords

CATALYSIS; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME STABILITY; MODEL; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN FOLDING; REVIEW; STRUCTURE ANALYSIS; X RAY ANALYSIS;

EID: 4444256908     PISSN: 12258687     EISSN: None     Source Type: Journal    
DOI: 10.5483/bmbrep.2004.37.4.394     Document Type: Review
Times cited : (8)

References (17)
  • 1
    • 0036908425 scopus 로고    scopus 로고
    • The stability curve of bovine adenosine deaminase is bimodal
    • Andersen, E. and Britt, B. M. (2002) The stability curve of bovine adenosine deaminase is bimodal. J. Biomolec. Struct. Dynamics 20, 375-380.
    • (2002) J. Biomolec. Struct. Dynamics , vol.20 , pp. 375-380
    • Andersen, E.1    Britt, B.M.2
  • 2
    • 0023442217 scopus 로고
    • Protein stability curves
    • Becktel, W. J. and Schellman, J. A. (1987) Protein stability curves. Biopolymers 26, 1859-1877.
    • (1987) Biopolymers , vol.26 , pp. 1859-1877
    • Becktel, W.J.1    Schellman, J.A.2
  • 3
    • 0027432797 scopus 로고
    • A shifting specificity model for enzyme catalysis
    • Britt, B. M. (1993) A shifting specificity model for enzyme catalysis. J. Theor. Biol. 164, 181-190.
    • (1993) J. Theor. Biol. , vol.164 , pp. 181-190
    • Britt, B.M.1
  • 4
    • 0031434907 scopus 로고    scopus 로고
    • For enzymes, bigger is better
    • Britt, B. M. (1997) For enzymes, bigger is better. Biophys. Chem. 69, 63-70.
    • (1997) Biophys. Chem. , vol.69 , pp. 63-70
    • Britt, B.M.1
  • 5
    • 0034850277 scopus 로고    scopus 로고
    • Binding thermodynamics of the transition state analogue coformycin and of the ground state analogue 1-deazaadenosine to bovine adenosine deaminase
    • Castro, C. and Britt, B. M. (2001) Binding thermodynamics of the transition state analogue coformycin and of the ground state analogue 1-deazaadenosine to bovine adenosine deaminase. J. Enz. Inhibition 16, 217-232.
    • (2001) J. Enz. Inhibition , vol.16 , pp. 217-232
    • Castro, C.1    Britt, B.M.2
  • 6
    • 0033528657 scopus 로고    scopus 로고
    • Thermodynamic stability of a cold-active α-amylase from the antartic bacterium Alteromonas haloplanctis
    • Feller, G., dAmico, D. and Gerday, C. (1999) Thermodynamic stability of a cold-active α-amylase from the antartic bacterium Alteromonas haloplanctis. Biochemistry 38, 4613-4619.
    • (1999) Biochemistry , vol.38 , pp. 4613-4619
    • Feller, G.1    DAmico, D.2    Gerday, C.3
  • 7
    • 84892166712 scopus 로고
    • Einfluss der configuration auf die Wirkung der enzyme
    • Fischer, E. (1894) Einfluss der configuration auf die Wirkung der enzyme. Ber. Dt. Chem. Ges. 27, 2985-2993.
    • (1894) Ber. Dt. Chem. Ges. , vol.27 , pp. 2985-2993
    • Fischer, E.1
  • 8
    • 0004214524 scopus 로고
    • Green and Co., London, UK
    • Haldane, J. B. S. (1930) Enzymes, Green and Co., London, UK.
    • (1930) Enzymes
    • Haldane, J.B.S.1
  • 9
    • 0033791659 scopus 로고    scopus 로고
    • Critical analysis of antibody catalysis
    • Hilvert, D. (2000) Critical analysis of antibody catalysis. Annu. Rev. Biochem. 69, 751-793.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 751-793
    • Hilvert, D.1
  • 10
    • 0029793086 scopus 로고    scopus 로고
    • Off-the-shelf proteins that rival tailor-made antibodies as catalysts
    • Hollfelder, F., Kirby, A. J. and Tawfik, D. S. (1996) Off-the-shelf proteins that rival tailor-made antibodies as catalysts. Nature 383, 60-63.
    • (1996) Nature , vol.383 , pp. 60-63
    • Hollfelder, F.1    Kirby, A.J.2    Tawfik, D.S.3
  • 11
    • 0016624901 scopus 로고
    • Binding energy, specificity, and enzymic catalysis: The circe effect
    • Jencks, W. P. (1975) Binding energy, specificity, and enzymic catalysis: the circe effect. Adv. Enzymol. Rel. Mol. Biol. 43, 219-410.
    • (1975) Adv. Enzymol. Rel. Mol. Biol. , vol.43 , pp. 219-410
    • Jencks, W.P.1
  • 12
    • 0002449434 scopus 로고
    • The active site and enzyme action
    • Koshland, D. E. (1960) The active site and enzyme action. Adv. Enzymol. 22, 45-95.
    • (1960) Adv. Enzymol. , vol.22 , pp. 45-95
    • Koshland, D.E.1
  • 13
    • 0037431959 scopus 로고    scopus 로고
    • Low-temperature-induced structural changes in human lysozyme elucidated by three-dimensional NMR spectroscopy
    • Kumeta, H., Miura, A., Kobashigawa, Y., Miura, K., Oka, C., Nemoto, N., Nitta, K. and Tsuda, S. (2003) Low-temperature-induced structural changes in human lysozyme elucidated by three-dimensional NMR spectroscopy. Biochemistry 42, 1209-1216.
    • (2003) Biochemistry , vol.42 , pp. 1209-1216
    • Kumeta, H.1    Miura, A.2    Kobashigawa, Y.3    Miura, K.4    Oka, C.5    Nemoto, N.6    Nitta, K.7    Tsuda, S.8
  • 14
    • 0035960641 scopus 로고    scopus 로고
    • Thermodynamic differences among homologous thermophilic and mesophilic proteins
    • Kumar, S., Tsai, C. J. and Nussinov, R. (2001) Thermodynamic differences among homologous thermophilic and mesophilic proteins. Biochemistry 40, 14152-14165.
    • (2001) Biochemistry , vol.40 , pp. 14152-14165
    • Kumar, S.1    Tsai, C.J.2    Nussinov, R.3
  • 15
    • 0026716610 scopus 로고
    • Analysis of ground state and transition state effects in enzyme catalysis
    • Menger, F. M. (1992) Analysis of ground state and transition state effects in enzyme catalysis. Biochemistry 31, 5368-5373.
    • (1992) Biochemistry , vol.31 , pp. 5368-5373
    • Menger, F.M.1
  • 16
    • 0037171140 scopus 로고    scopus 로고
    • Revisiting volume changes in pressure-induced protein unfolding
    • Royer, C. A. (2002) Revisiting volume changes in pressure-induced protein unfolding. Biochim. Biophys. Acta 1595, 201-209.
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 201-209
    • Royer, C.A.1
  • 17
    • 0036023103 scopus 로고    scopus 로고
    • Direct measurement of local and global contributions in the binding of coformycin to bovine adenosine deaminase
    • Strohmeyer, E. A., Beckley, J. R. and Britt, B. M. (2002) Direct measurement of local and global contributions in the binding of coformycin to bovine adenosine deaminase J. Enzyme Inhibit. 17, 77-86.
    • (2002) J. Enzyme Inhibit. , vol.17 , pp. 77-86
    • Strohmeyer, E.A.1    Beckley, J.R.2    Britt, B.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.