메뉴 건너뛰기




Volumn 79, Issue 4, 2008, Pages 1010-1019

The total quasi-steady-state approximation for complex enzyme reactions

Author keywords

Enzyme kinetics; Reverse engineering; Signal transduction

Indexed keywords

BIOCHEMISTRY; ENZYME KINETICS; POLYNOMIAL APPROXIMATION; REENGINEERING; REVERSE ENGINEERING; SIGNAL TRANSDUCTION;

EID: 56949083528     PISSN: 03784754     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.matcom.2008.02.009     Document Type: Article
Times cited : (34)

References (24)
  • 3
    • 0029681614 scopus 로고    scopus 로고
    • Extending the quasi-steady state approximation by changing variables
    • Borghans J., de Boer R., and Segel L. Extending the quasi-steady state approximation by changing variables. Bull. Math. Biol. 58 (1996) 43-63
    • (1996) Bull. Math. Biol. , vol.58 , pp. 43-63
    • Borghans, J.1    de Boer, R.2    Segel, L.3
  • 4
    • 0000292524 scopus 로고
    • A note on the kinetics of enzyme action
    • Briggs G.E., and Haldane J.B.S. A note on the kinetics of enzyme action. Biochem. J. 19 (1925) 338-339
    • (1925) Biochem. J. , vol.19 , pp. 338-339
    • Briggs, G.E.1    Haldane, J.B.S.2
  • 5
    • 0030972112 scopus 로고    scopus 로고
    • The activating dual phosphorylation of MAPK by MEK is nonprocessive
    • Burack W.R., and Sturgill T.W. The activating dual phosphorylation of MAPK by MEK is nonprocessive. Biochemistry 36 (1997) 5929-5933
    • (1997) Biochemistry , vol.36 , pp. 5929-5933
    • Burack, W.R.1    Sturgill, T.W.2
  • 6
    • 0030746219 scopus 로고    scopus 로고
    • Mechanistic studies of the dual phosphorylation of mitogen-activated protein kinase
    • Ferrell J.E., and Bhatt R.R. Mechanistic studies of the dual phosphorylation of mitogen-activated protein kinase. J. Biol. Chem. 272 (1997) 19008-19016
    • (1997) J. Biol. Chem. , vol.272 , pp. 19008-19016
    • Ferrell, J.E.1    Bhatt, R.R.2
  • 7
    • 0001424903 scopus 로고
    • An amplified sensitivity arising from covalent modification in biological systems
    • Goldbeter A., and Koshland Jr. D.E. An amplified sensitivity arising from covalent modification in biological systems. Proc. Natl. Acad. Sci. 78 (1981) 6840-6844
    • (1981) Proc. Natl. Acad. Sci. , vol.78 , pp. 6840-6844
    • Goldbeter, A.1    Koshland Jr., D.E.2
  • 8
    • 7144222730 scopus 로고
    • Recherches sur la loi de l'action de la sucrase
    • Henri V. Recherches sur la loi de l'action de la sucrase. C. R. Hebd. Acad. Sci. 133 (1901) 891-899
    • (1901) C. R. Hebd. Acad. Sci. , vol.133 , pp. 891-899
    • Henri, V.1
  • 9
    • 0346328093 scopus 로고
    • Uber das gesetz der wirkung des invertins
    • Henri V. Uber das gesetz der wirkung des invertins. Z. Phys. Chem. 39 (1901) 194-216
    • (1901) Z. Phys. Chem. , vol.39 , pp. 194-216
    • Henri, V.1
  • 10
    • 0001705279 scopus 로고
    • Théorie générale de l'action de quelques diastases
    • Henri V. Théorie générale de l'action de quelques diastases. C. R. Hebd. Acad. Sci. 135 (1902) 916-919
    • (1902) C. R. Hebd. Acad. Sci. , vol.135 , pp. 916-919
    • Henri, V.1
  • 11
    • 0842288229 scopus 로고    scopus 로고
    • Signaling switches and bistability arising from multisite phosphorylation in protein kinase cascades
    • Markevich N.I., Hoek J.B., and Kholodenko B.N. Signaling switches and bistability arising from multisite phosphorylation in protein kinase cascades. J. Cell Biol. 164 (2004) 353-359
    • (2004) J. Cell Biol. , vol.164 , pp. 353-359
    • Markevich, N.I.1    Hoek, J.B.2    Kholodenko, B.N.3
  • 12
    • 0000870544 scopus 로고
    • Die kinetik der invertinwirkung
    • Michaelis L., and Menten M.L. Die kinetik der invertinwirkung. Biochem. Z. 49 (1913) 333-369
    • (1913) Biochem. Z. , vol.49 , pp. 333-369
    • Michaelis, L.1    Menten, M.L.2
  • 13
    • 33846543728 scopus 로고    scopus 로고
    • M.G. Pedersen, A.M. Bersani, E. Bersani. The total quasi-steady-state approximation for fully competitive enzyme reactions, Bull. Math. Biol. 69 (2007) 433-457.
    • M.G. Pedersen, A.M. Bersani, E. Bersani. The total quasi-steady-state approximation for fully competitive enzyme reactions, Bull. Math. Biol. 69 (2007) 433-457.
  • 14
    • 43249083974 scopus 로고    scopus 로고
    • M.G. Pedersen, A.M. Bersani, E. Bersani. Quasi steady-state approximations in complex intracellular signal transduction networks - a word of caution, J. Math. Chem., doi:10.1007/s10910.007.9248.4, in press.
    • M.G. Pedersen, A.M. Bersani, E. Bersani. Quasi steady-state approximations in complex intracellular signal transduction networks - a word of caution, J. Math. Chem., doi:10.1007/s10910.007.9248.4, in press.
  • 15
    • 0014824563 scopus 로고
    • Time-dependent Michaelis-Menten kinetics for an enzyme-substrate-inhibitor system
    • Rubinow S.I., and Lebowitz J.L. Time-dependent Michaelis-Menten kinetics for an enzyme-substrate-inhibitor system. J. Am. Chem. Soc. 92 (1970) 3888-3893
    • (1970) J. Am. Chem. Soc. , vol.92 , pp. 3888-3893
    • Rubinow, S.I.1    Lebowitz, J.L.2
  • 17
    • 0033789559 scopus 로고    scopus 로고
    • Time-dependent closed form solutions for fully competitive enzyme reactions
    • Schnell S., and Mendoza C. Time-dependent closed form solutions for fully competitive enzyme reactions. Bull. Math. Biol. 62 (2000) 321-336
    • (2000) Bull. Math. Biol. , vol.62 , pp. 321-336
    • Schnell, S.1    Mendoza, C.2
  • 18
    • 0023734558 scopus 로고
    • On the validity of the steady state assumption of enzyme kinetics
    • Segel L.A. On the validity of the steady state assumption of enzyme kinetics. Bull. Math. Biol. 50 (1988) 579-593
    • (1988) Bull. Math. Biol. , vol.50 , pp. 579-593
    • Segel, L.A.1
  • 20
    • 85012573362 scopus 로고
    • Concentration of metabolites and binding sites. Implications in metabolic regulation
    • Academic Press, New York
    • Sols A., and Marco R. Concentration of metabolites and binding sites. Implications in metabolic regulation. Current Topics in Cellular Regulation, vol. 2 (1970), Academic Press, New York
    • (1970) Current Topics in Cellular Regulation, vol. 2
    • Sols, A.1    Marco, R.2
  • 22
    • 0344395658 scopus 로고    scopus 로고
    • Michaelis-Menten kinetics at high enzyme concentrations
    • Tzafriri A.R. Michaelis-Menten kinetics at high enzyme concentrations. Bull. Math. Biol. 65 (2003) 1111-1129
    • (2003) Bull. Math. Biol. , vol.65 , pp. 1111-1129
    • Tzafriri, A.R.1
  • 23
    • 0344393718 scopus 로고    scopus 로고
    • The total quasi-steady-state approximation is valid for reversible enzyme kinetics
    • Tzafriri A.R., and Edelman E.R. The total quasi-steady-state approximation is valid for reversible enzyme kinetics. J. Theor. Biol. 226 (2004) 303-313
    • (2004) J. Theor. Biol. , vol.226 , pp. 303-313
    • Tzafriri, A.R.1    Edelman, E.R.2
  • 24
    • 0035943595 scopus 로고    scopus 로고
    • The mechanism of dephosphorylation of extracellular signal-regulated kinase 2 by mitogen-activated protein kinase phosphatase 3
    • Zhao Y., and Zhang Z.-Y. The mechanism of dephosphorylation of extracellular signal-regulated kinase 2 by mitogen-activated protein kinase phosphatase 3. J. Biol. Chem. 276 (2001) 32382-32391
    • (2001) J. Biol. Chem. , vol.276 , pp. 32382-32391
    • Zhao, Y.1    Zhang, Z.-Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.