메뉴 건너뛰기




Volumn 242, Issue 3, 2006, Pages 627-633

A probabilistic approach to compact steady-state kinetic equations for enzymic reactions

Author keywords

Probability; Reaction graph; Scheme simplification

Indexed keywords

ENZYME ACTIVITY; KINETICS; PROBABILITY;

EID: 33747880296     PISSN: 00225193     EISSN: 10958541     Source Type: Journal    
DOI: 10.1016/j.jtbi.2006.03.022     Document Type: Article
Times cited : (5)

References (18)
  • 1
    • 0014429144 scopus 로고
    • A simple method for derivation of rate equations for enzyme-catalyzed reactions under the rapid equilibrium assumption or combined assumptions of equilibrium and steady state
    • Cha S. A simple method for derivation of rate equations for enzyme-catalyzed reactions under the rapid equilibrium assumption or combined assumptions of equilibrium and steady state. J. Biol. Chem. 243 (1968) 820-825
    • (1968) J. Biol. Chem. , vol.243 , pp. 820-825
    • Cha, S.1
  • 2
    • 50549159930 scopus 로고
    • The kinetics of enzyme-catalyzed reactions with two or more substrates or I. Nomenclature and rate equations
    • Cleland W.W. The kinetics of enzyme-catalyzed reactions with two or more substrates or I. Nomenclature and rate equations. Biochim. Biophys. Acta 67 (1963) 104-137
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 104-137
    • Cleland, W.W.1
  • 3
    • 0024971003 scopus 로고
    • Graphic rules in steady and non-steady state enzyme kinetics
    • Chou K.-Ch. Graphic rules in steady and non-steady state enzyme kinetics. J. Biol. Chem. 264 (1989) 12074-12079
    • (1989) J. Biol. Chem. , vol.264 , pp. 12074-12079
    • Chou, K.-Ch.1
  • 4
    • 0028071544 scopus 로고
    • Kinetics of processive nucleic acid polymerases and nucleases
    • Chou K.-C., Kezdy F.J., and Reusser F. Kinetics of processive nucleic acid polymerases and nucleases. Anal. Biochem. 221 (1994) 217-230
    • (1994) Anal. Biochem. , vol.221 , pp. 217-230
    • Chou, K.-C.1    Kezdy, F.J.2    Reusser, F.3
  • 6
    • 0017370629 scopus 로고
    • An automated method for deriving steady-state rate equations
    • Cornish-Bowden A. An automated method for deriving steady-state rate equations. Biochem. J. 165 (1977) 55-59
    • (1977) Biochem. J. , vol.165 , pp. 55-59
    • Cornish-Bowden, A.1
  • 8
    • 0037016666 scopus 로고    scopus 로고
    • Bacteriophage T4 Dam DNA-[N6-adenine]methyltransferase. Kinetic evidence for a catalytically essential conformational change in the ternary complex
    • Evdokimov A.A., Zinoviev V.V., Malygin E.G., Schlagman S.L., and Hattman S. Bacteriophage T4 Dam DNA-[N6-adenine]methyltransferase. Kinetic evidence for a catalytically essential conformational change in the ternary complex. J. Biol. Chem. 277 (2002) 279-286
    • (2002) J. Biol. Chem. , vol.277 , pp. 279-286
    • Evdokimov, A.A.1    Zinoviev, V.V.2    Malygin, E.G.3    Schlagman, S.L.4    Hattman, S.5
  • 9
    • 0014244669 scopus 로고
    • A systematic approach to kinetic studies of multi-substrate enzyme systems
    • Fisher J.R., and Hoagland Jr. V.D. A systematic approach to kinetic studies of multi-substrate enzyme systems. Adv. Biol. Med. Phys. 12 (1968) 163-211
    • (1968) Adv. Biol. Med. Phys. , vol.12 , pp. 163-211
    • Fisher, J.R.1    Hoagland Jr., V.D.2
  • 10
    • 33947472850 scopus 로고
    • A schematic method of deriving the rate laws for enzyme-catalyzed reactions
    • King E.L., and Altman C. A schematic method of deriving the rate laws for enzyme-catalyzed reactions. J. Phys. Chem. 60 (1956) 1375-1378
    • (1956) J. Phys. Chem. , vol.60 , pp. 1375-1378
    • King, E.L.1    Altman, C.2
  • 11
    • 33747877546 scopus 로고    scopus 로고
    • Knorre, D.G., Malygin, E.G., 1972. Probabilistic method for deriving the kinetic equation for an isotope exchange at equilibrium for enzyme-catalyzed reactions. Dokl. Akad. Nauk. SSSR (Reports of the Academy of Sciences of the USSR) 207, 1391-1394.
  • 12
    • 0017621573 scopus 로고
    • Derivation of the kinetic equations of steady state enzymatic reactions with use of multistage specific rates of conversions of enzyme forms
    • (Translated from Biofizika XXII, 15-20, 1977)
    • Malygin E.G. Derivation of the kinetic equations of steady state enzymatic reactions with use of multistage specific rates of conversions of enzyme forms. Biophysics 22 (1977) 11-17 (Translated from Biofizika XXII, 15-20, 1977)
    • (1977) Biophysics , vol.22 , pp. 11-17
    • Malygin, E.G.1
  • 13
    • 0037844861 scopus 로고    scopus 로고
    • DNA (cytosine-N4-)- and -(adenine-N6-)-methyltransferases have different kinetic mechanisms but the same reaction route. A comparison of M.BamHI and T4 Dam
    • Malygin E.G., Zinoviev V.V., Evdokimov A.A., Lindstrom W.M., Reich N.O., and Hattman S. DNA (cytosine-N4-)- and -(adenine-N6-)-methyltransferases have different kinetic mechanisms but the same reaction route. A comparison of M.BamHI and T4 Dam. J. Biol. Chem. 278 (2003) 15713-15719
    • (2003) J. Biol. Chem. , vol.278 , pp. 15713-15719
    • Malygin, E.G.1    Zinoviev, V.V.2    Evdokimov, A.A.3    Lindstrom, W.M.4    Reich, N.O.5    Hattman, S.6
  • 14
    • 0023294732 scopus 로고
    • Alternative to the steady-state method: derivation of reaction rates from first-passage times and pathway probabilities
    • Ninio J. Alternative to the steady-state method: derivation of reaction rates from first-passage times and pathway probabilities. Proc. Natl Acad. Sci. USA 84 (1987) 663-667
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 663-667
    • Ninio, J.1
  • 15
    • 25944445909 scopus 로고
    • Inverse problems of chemical kinetics and thermodynamics. Systems analysis
    • Spivak S.I. Inverse problems of chemical kinetics and thermodynamics. Systems analysis. Model. Simul. (SAMS) 18-19 (1995) 107-110
    • (1995) Model. Simul. (SAMS) , vol.18-19 , pp. 107-110
    • Spivak, S.I.1
  • 16
    • 77956809530 scopus 로고
    • The kinetics of some industrial heterogeneous catalytic reactions
    • Temkin M.I. The kinetics of some industrial heterogeneous catalytic reactions. Adv. Catal. 28 (1979) 173-291
    • (1979) Adv. Catal. , vol.28 , pp. 173-291
    • Temkin, M.I.1
  • 17
    • 0037487968 scopus 로고
    • A new method for solving the problems of the stationary kinetics of enzymological reactions
    • Volkenstein M.V., and Goldstein B.N. A new method for solving the problems of the stationary kinetics of enzymological reactions. Biochim. Biophys. Acta 115 (1966) 471-477
    • (1966) Biochim. Biophys. Acta , vol.115 , pp. 471-477
    • Volkenstein, M.V.1    Goldstein, B.N.2
  • 18
    • 0021764092 scopus 로고
    • An extension of Chou's graphic rules for deriving enzyme kinetic equation to system involving parallel reaction pathways
    • Zhou G.-P., and Deng M.-H. An extension of Chou's graphic rules for deriving enzyme kinetic equation to system involving parallel reaction pathways. Biochem. J. 222 (1984) 169-176
    • (1984) Biochem. J. , vol.222 , pp. 169-176
    • Zhou, G.-P.1    Deng, M.-H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.