메뉴 건너뛰기




Volumn 52, Issue 3, 1996, Pages 433-437

New constraints between kinetic parameters explain the (un)identifiability of enzymatic rate constants

Author keywords

enzyme kinetics; Haldanes; identifiability; parameter estimation; rate constants

Indexed keywords

CALCULATIONS; CONSTRAINT THEORY; MATHEMATICAL MODELS; PARAMETER ESTIMATION;

EID: 0030571276     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19961105)52:3<433::AID-BIT10>3.0.CO;2-K     Document Type: Article
Times cited : (12)

References (16)
  • 1
    • 0000303856 scopus 로고
    • The kinetics of α-chymotrypsin reactions in the presence of added nucleophiles
    • Bender, M. L., Clement, G. E., Gunter, C. R., Kézdy, F. J. 1964. The kinetics of α-chymotrypsin reactions in the presence of added nucleophiles. J. Am. Chem. Soc. 86: 3697-3703.
    • (1964) J. Am. Chem. Soc. , vol.86 , pp. 3697-3703
    • Bender, M.L.1    Clement, G.E.2    Gunter, C.R.3    Kézdy, F.J.4
  • 2
    • 0026955780 scopus 로고
    • Determination of equilibrium and individual rate constants for sublilisin-calalyzed transesterification in anhydrous environment
    • Chatterjee, S., Russell, A. J. 1992. Determination of equilibrium and individual rate constants for sublilisin-calalyzed transesterification in anhydrous environment. Biotechnol. Bioeng. 40: 1069-1077.
    • (1992) Biotechnol. Bioeng. , vol.40 , pp. 1069-1077
    • Chatterjee, S.1    Russell, A.J.2
  • 3
    • 0025021607 scopus 로고
    • Applications of graph theory to enzyme kinetics and protein folding kinetics. Steady and non-steady-state systems
    • Chou, K. C. 1990. Applications of graph theory to enzyme kinetics and protein folding kinetics. Steady and non-steady-state systems. Biophys. Chem. 35: 1-24.
    • (1990) Biophys. Chem. , vol.35 , pp. 1-24
    • Chou, K.C.1
  • 4
    • 50549159930 scopus 로고
    • The kinetics of enzyme-catalyzed reactions with two or more substrates and products
    • Cleland, W. W. 1963. The kinetics of enzyme-catalyzed reactions with two or more substrates and products. Biochim. Biophys. Acta 67: 104-137
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 104-137
    • Cleland, W.W.1
  • 5
    • 0020391390 scopus 로고
    • An analysis of Haldane relationships
    • Cleland, W. W. 1982. An analysis of Haldane relationships. Meth. Enz. 87: 366-369.
    • (1982) Meth. Enz. , vol.87 , pp. 366-369
    • Cleland, W.W.1
  • 7
    • 0014473526 scopus 로고
    • Kinetic studies of yeast nucleoside diphosphate kinase
    • Garces, E., Cleland, W. W. 1969. Kinetic studies of yeast nucleoside diphosphate kinase. Biochemistry 8: 633-640.
    • (1969) Biochemistry , vol.8 , pp. 633-640
    • Garces, E.1    Cleland, W.W.2
  • 8
    • 0018698179 scopus 로고
    • Use of alternative substrates to probe multisubstrate enzyme mechanisms
    • Huang, C. Y. 1979. Use of alternative substrates to probe multisubstrate enzyme mechanisms. Meth. Enz. 63: 486-500.
    • (1979) Meth. Enz. , vol.63 , pp. 486-500
    • Huang, C.Y.1
  • 9
    • 0023800011 scopus 로고
    • Calculation of rate and equilibrium constants for a ping-pong mechanism from steady-state data
    • Jardetzky, T. S., Seville, M. 1988. Calculation of rate and equilibrium constants for a ping-pong mechanism from steady-state data. Biochemistry 27: 6758-6763.
    • (1988) Biochemistry , vol.27 , pp. 6758-6763
    • Jardetzky, T.S.1    Seville, M.2
  • 10
    • 33947472850 scopus 로고
    • A schematic method of deriving the rate laws for enzyme-catalyzed reactions
    • King, E. L., Altman, C. 1956. A schematic method of deriving the rate laws for enzyme-catalyzed reactions. J. Phys. Chem. 60: 1375-1378.
    • (1956) J. Phys. Chem. , vol.60 , pp. 1375-1378
    • King, E.L.1    Altman, C.2
  • 11
    • 0020440235 scopus 로고
    • Regression analysis, experimental error, and statistical criteria in the design and analysis of experiments for discrimination between rival kinetic models
    • Mannervik, B. 1982. Regression analysis, experimental error, and statistical criteria in the design and analysis of experiments for discrimination between rival kinetic models. Meth. Enz. 87: 370-390.
    • (1982) Meth. Enz. , vol.87 , pp. 370-390
    • Mannervik, B.1
  • 12
    • 0020430338 scopus 로고
    • Kinetic examination of enzyme mechanisms involving branched reaction pathways - A detailed consideration of multifunctional glucose-6-phosphatase
    • Nordlie, R. C. 1982. Kinetic examination of enzyme mechanisms involving branched reaction pathways - A detailed consideration of multifunctional glucose-6-phosphatase. Meth. Enz. 87: 319-353.
    • (1982) Meth. Enz. , vol.87 , pp. 319-353
    • Nordlie, R.C.1
  • 13
    • 0041129019 scopus 로고
    • Isoptope exchange methods for elucidating enzymic catalysis
    • Purich, D. L. 1980. Isoptope exchange methods for elucidating enzymic catalysis. Meth. Enz. 64: 3-46.
    • (1980) Meth. Enz. , vol.64 , pp. 3-46
    • Purich, D.L.1
  • 14
    • 0028764977 scopus 로고
    • Kinetic analysis of enzymatic chiral resolution by progress curve analysis
    • Rakels, J. L. L., Romein, B., Straathof, A. J. J., Heijnen, J. J. 1994. Kinetic analysis of enzymatic chiral resolution by progress curve analysis. Biotechnol. Bioeng. 43: 411-422.
    • (1994) Biotechnol. Bioeng. , vol.43 , pp. 411-422
    • Rakels, J.L.L.1    Romein, B.2    Straathof, A.J.J.3    Heijnen, J.J.4
  • 16
    • 0009440057 scopus 로고
    • Identifiability of state space models
    • Springer-Verlag, Berlin
    • Walter, E. 1982. Identifiability of state space models. Lecture notes in biomathematics, vol. 46. Springer-Verlag, Berlin.
    • (1982) Lecture Notes in Biomathematics , vol.46
    • Walter, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.