메뉴 건너뛰기




Volumn 587, Issue 17, 2013, Pages 2725-2730

The origins of enzyme kinetics

Author keywords

Henri; Kinetics; Menten; Michaelis; Steady state

Indexed keywords

COMPETITIVE INHIBITION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; MICHAELIS MENTEN KINETICS; PH; PRIORITY JOURNAL; REACTION TIME; REVIEW; STEADY STATE;

EID: 84883051895     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2013.06.009     Document Type: Review
Times cited : (78)

References (69)
  • 1
    • 0001284812 scopus 로고
    • Enzyme action
    • A.J. Brown Enzyme action J. Chem. Soc. 81 1902 373 388
    • (1902) J. Chem. Soc. , vol.81 , pp. 373-388
    • Brown, A.J.1
  • 2
    • 0001705279 scopus 로고
    • Théorie générale de l'action de quelques diastases
    • V. Henri Théorie générale de l'action de quelques diastases C. R. Hebd. Seances Acad. Sci. 135 1902 916 919
    • (1902) C. R. Hebd. Seances Acad. Sci. , vol.135 , pp. 916-919
    • Henri, V.1
  • 4
    • 0000870544 scopus 로고
    • Kinetik der Invertinwirkung
    • L. Michaelis, and M.L. Menten Kinetik der Invertinwirkung Biochem. Z. 49 1913 333 369
    • (1913) Biochem. Z. , vol.49 , pp. 333-369
    • Michaelis, L.1    Menten, M.L.2
  • 7
    • 0000292524 scopus 로고
    • A note on the kinetics of enzyme action
    • G.E. Briggs, and J.B.S. Haldane 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
  • 9
    • 0000374873 scopus 로고
    • A letter of Mr. Isaac Newton, Professor of the Mathematics in the University of Cambridge; Containing his new theory about light and colors
    • I. Newton A letter of Mr. Isaac Newton, Professor of the Mathematics in the University of Cambridge; containing his new theory about light and colors Philos. Trans. R. Soc. 80 1671/72 3075 3087
    • (1671) Philos. Trans. R. Soc. , vol.80 , pp. 3075-3087
    • Newton, I.1
  • 10
    • 84980061775 scopus 로고
    • Über das Gesetz, nach welchem die Enwirkung de Säuren und Rohrzucker stattfindet
    • 499-526
    • L.F. Wilhelmy Über das Gesetz, nach welchem die Enwirkung de Säuren und Rohrzucker stattfindet Poggendorf's Ann. Phys. Chem. 81 1850 413 433 499-526
    • (1850) Poggendorf's Ann. Phys. Chem. , vol.81 , pp. 413-433
    • Wilhelmy, L.F.1
  • 12
    • 67650666133 scopus 로고
    • Sur la papaïne: Nouvelle contribution à l'histoire des ferments solubles
    • A. Wurtz Sur la papaïne: nouvelle contribution à l'histoire des ferments solubles C. R. Hebd. Seances Acad. Sci. 91 1880 787 791
    • (1880) C. R. Hebd. Seances Acad. Sci. , vol.91 , pp. 787-791
    • Wurtz, A.1
  • 13
    • 0001675978 scopus 로고
    • Invertase: A contribution to the history of an enzyme or unorganised ferment
    • C. O'Sullivan, and F.W. Tompson Invertase: a contribution to the history of an enzyme or unorganised ferment J. Chem. Soc. (Trans.) 57 1890 834 931
    • (1890) J. Chem. Soc. (Trans.) , vol.57 , pp. 834-931
    • O'Sullivan, C.1    Tompson, F.W.2
  • 14
    • 84887262673 scopus 로고
    • Influence of oxygen and concentration on alcohol fermentation
    • A.J. Brown Influence of oxygen and concentration on alcohol fermentation J. Chem. Soc. (Trans.) 61 1892 361 385
    • (1892) J. Chem. Soc. (Trans.) , vol.61 , pp. 361-385
    • Brown, A.J.1
  • 15
    • 80053394442 scopus 로고    scopus 로고
    • The original Michaelis constant: Translation of the 1913 Michaelis-Menten paper
    • K.A. Johnson, and R.S. Goody The original Michaelis constant: translation of the 1913 Michaelis-Menten paper Biochemistry 50 2011 8264 8269
    • (2011) Biochemistry , vol.50 , pp. 8264-8269
    • Johnson, K.A.1    Goody, R.S.2
  • 18
    • 84883054802 scopus 로고    scopus 로고
    • The kinetics of invertin action
    • in press
    • T.R.C. Boyde, The kinetics of invertin action, FEBS Lett., in press (2013).
    • (2013) FEBS Lett.
    • Boyde, T.R.C.1
  • 20
    • 4243243129 scopus 로고
    • Études enzymatiques. II. sur la mesure et l'importance de la concentration des ions hydrogène dans les réactions enzymatiques
    • S.P.L. Sørensen Études enzymatiques. II. Sur la mesure et l'importance de la concentration des ions hydrogène dans les réactions enzymatiques C. R. Trav. Lab. Carlsberg 8 1909 1 168
    • (1909) C. R. Trav. Lab. Carlsberg , vol.8 , pp. 1-168
    • Sørensen, S.P.L.1
  • 21
    • 84883051964 scopus 로고
    • Hutchinson Ross Stroudsburg, PA
    • H.C. Friedmann Enzymes 1981 Hutchinson Ross Stroudsburg, PA
    • (1981) Enzymes
    • Friedmann, H.C.1
  • 22
    • 84988074926 scopus 로고
    • Symbolism and terminology in enzyme kinetics. Recommendations 1981
    • International Union of Biochemistry
    • International Union of Biochemistry Symbolism and terminology in enzyme kinetics. Recommendations 1981 Eur. J. Biochem. 128 1982 281 291
    • (1982) Eur. J. Biochem. , vol.128 , pp. 281-291
  • 23
    • 0014806767 scopus 로고
    • Similarities and differences in kinetics of the Michaelis scheme and the Henri scheme
    • R.O. Viale Similarities and differences in kinetics of the Michaelis scheme and the Henri scheme J. Theor. Biol. 27 1970 377 385
    • (1970) J. Theor. Biol. , vol.27 , pp. 377-385
    • Viale, R.O.1
  • 24
    • 30344466032 scopus 로고    scopus 로고
    • The mechanism distinguishability problem in biochemical kinetics: The single-enzyme, single-substrate reaction as a case study
    • S. Schnell, M.J. Chappell, N.D. Evans, and M.R. Roussel The mechanism distinguishability problem in biochemical kinetics: the single-enzyme, single-substrate reaction as a case study C. R. Biol. 329 2006 51 61
    • (2006) C. R. Biol. , vol.329 , pp. 51-61
    • Schnell, S.1    Chappell, M.J.2    Evans, N.D.3    Roussel, M.R.4
  • 25
    • 0014118746 scopus 로고
    • Specificity and stereospecificity of α-chymotrypsin
    • D.W. Ingles, and J.R. Knowles Specificity and stereospecificity of α-chymotrypsin Biochem. J. 104 1967 369 377
    • (1967) Biochem. J. , vol.104 , pp. 369-377
    • Ingles, D.W.1    Knowles, J.R.2
  • 26
    • 0007589020 scopus 로고
    • The mode of action of urease and of enzymes in general
    • D.D. Van Slyke, and G.E. Cullen The mode of action of urease and of enzymes in general J. Biol. Chem. 19 1914 141 180
    • (1914) J. Biol. Chem. , vol.19 , pp. 141-180
    • Van Slyke, D.D.1    Cullen, G.E.2
  • 27
    • 0011992730 scopus 로고
    • The time dimension in steady-state kinetics: A simplified representation of control coefficients
    • A. Cornish-Bowden The time dimension in steady-state kinetics: a simplified representation of control coefficients Biochem. Educ. 15 1987 144 146
    • (1987) Biochem. Educ. , vol.15 , pp. 144-146
    • Cornish-Bowden, A.1
  • 28
    • 84882439244 scopus 로고
    • The effect of hydrogen ion concentration and of inhibiting substances on urease. Further study on the mode of enzyme action
    • D.D. Van Slyke, and G. Zacharias The effect of hydrogen ion concentration and of inhibiting substances on urease. Further study on the mode of enzyme action J. Biol. Chem. 19 1914 181 210
    • (1914) J. Biol. Chem. , vol.19 , pp. 181-210
    • Van Slyke, D.D.1    Zacharias, G.2
  • 29
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • D.E. Koshland Application of a theory of enzyme specificity to protein synthesis Proc. Natl. Acad. Sci. USA 44 1958 98 104
    • (1958) Proc. Natl. Acad. Sci. USA , vol.44 , pp. 98-104
    • Koshland, D.E.1
  • 30
    • 0010595278 scopus 로고
    • The development of enzyme kinetics
    • P.D. Boyer, H. Lardy, K. Myrbäck, second ed. Academic Press
    • H.L. Segal The development of enzyme kinetics P.D. Boyer, H. Lardy, K. Myrbäck, The Enzymes second ed. 1959 Academic Press 1 48
    • (1959) The Enzymes , pp. 1-48
    • Segal, H.L.1
  • 31
    • 84883055956 scopus 로고    scopus 로고
    • Before Michaelis and Menten: Victor Henri's equation
    • in press
    • Mazat, J.P., Before Michaelis and Menten: Victor Henri's equation, FEBS J., in press (2013).
    • (2013) FEBS J.
    • Mazat, J.P.1
  • 32
    • 0000944312 scopus 로고
    • Die Wirkung der Wasserstoffionen auf das Invertin
    • L. Michaelis, and H. Davidsohn Die Wirkung der Wasserstoffionen auf das Invertin Biochem. Z. 35 1911 386 412
    • (1911) Biochem. Z. , vol.35 , pp. 386-412
    • Michaelis, L.1    Davidsohn, H.2
  • 35
    • 7144247197 scopus 로고
    • Die Wirkungsbedingenungen der Maltase aus Bierhefe: III. Über die Natur der verschiedenartigen Hemmungen der Fermentwirkungen
    • L. Michaelis, and P. Rona Die Wirkungsbedingenungen der Maltase aus Bierhefe: III. Über die Natur der verschiedenartigen Hemmungen der Fermentwirkungen Biochem. Z. 60 1914 62 78
    • (1914) Biochem. Z. , vol.60 , pp. 62-78
    • Michaelis, L.1    Rona, P.2
  • 36
    • 7144241686 scopus 로고
    • Über die verschiedenartige Natur der Hemmungen der Invertasewirkung
    • L. Michaelis, and H. Pechstein Über die verschiedenartige Natur der Hemmungen der Invertasewirkung Biochem. Z. 60 1914 79 90
    • (1914) Biochem. Z. , vol.60 , pp. 79-90
    • Michaelis, L.1    Pechstein, H.2
  • 37
    • 50549159930 scopus 로고
    • Kinetics of enzyme-catalyzed reactions with two or more substrates or products. 1. Nomenclature and rate equations
    • W.W. Cleland Kinetics of enzyme-catalyzed reactions with two or more substrates or products. 1. Nomenclature and rate equations Biochim. Biophys. Acta 67 1963 104 137
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 104-137
    • Cleland, W.W.1
  • 39
    • 24644449504 scopus 로고    scopus 로고
    • nternational Union of Pure and Applied Chemistry Quantities third ed. RSC Publishing Cambridge
    • International Union of Pure and Applied Chemistry Quantities Units and Symbols in Physical Chemistry third ed. 2007 RSC Publishing Cambridge
    • (2007) Units and Symbols in Physical Chemistry
  • 40
    • 80052027829 scopus 로고    scopus 로고
    • Kinetics of starch hydrolysis and glucose mutarotation studied by NMR chemical exchange saturation transfer (CEST)
    • A.C. Dona, G. Pages, and P.W. Kuchel Kinetics of starch hydrolysis and glucose mutarotation studied by NMR chemical exchange saturation transfer (CEST) Carbohydr. Polym. 86 2011 1525 1532
    • (2011) Carbohydr. Polym. , vol.86 , pp. 1525-1532
    • Dona, A.C.1    Pages, G.2    Kuchel, P.W.3
  • 42
    • 0021503325 scopus 로고
    • Integrated rate equations for enzyme-catalysed first-order and second-order reactions
    • E.A. Boeker Integrated rate equations for enzyme-catalysed first-order and second-order reactions Biochem. J. 223 1984 15 22
    • (1984) Biochem. J. , vol.223 , pp. 15-22
    • Boeker, E.A.1
  • 43
    • 0022425432 scopus 로고
    • Integrated rate equations for irreversible enzyme-catalysed first-order and second-order reactions
    • E.A. Boeker Integrated rate equations for irreversible enzyme-catalysed first-order and second-order reactions Biochem. J. 226 1985 29 35
    • (1985) Biochem. J. , vol.226 , pp. 29-35
    • Boeker, E.A.1
  • 44
    • 0016767575 scopus 로고
    • Use of the direct linear plot for determining initial velocities
    • A. Cornish-Bowden Use of the direct linear plot for determining initial velocities Biochem. J. 149 1975 305 312
    • (1975) Biochem. J. , vol.149 , pp. 305-312
    • Cornish-Bowden, A.1
  • 45
    • 0032899689 scopus 로고    scopus 로고
    • Parameter estimation using a direct solution of the integrated Michaelis-Menten equation
    • C.T. Goudar, J.R. Sonnad, and R.G. Duggleby Parameter estimation using a direct solution of the integrated Michaelis-Menten equation Biochim. Biophys. Acta 1429 1999 377 383
    • (1999) Biochim. Biophys. Acta , vol.1429 , pp. 377-383
    • Goudar, C.T.1    Sonnad, J.R.2    Duggleby, R.G.3
  • 46
    • 0011807944 scopus 로고
    • Kinetic analysis of enzyme reactions. I. Further considerations of enzyme inhibition and analysis of enzyme activation
    • H.L. Segal, J.F. Kachmar, and P.D. Boyer Kinetic analysis of enzyme reactions. I. Further considerations of enzyme inhibition and analysis of enzyme activation Enzymologia 15 1952 187 198
    • (1952) Enzymologia , vol.15 , pp. 187-198
    • Segal, H.L.1    Kachmar, J.F.2    Boyer, P.D.3
  • 47
    • 0001594119 scopus 로고
    • Initial steady state velocities in the evaluation of enzyme-coenzyme- substrate reaction mechanisms
    • K. Dalziel Initial steady state velocities in the evaluation of enzyme-coenzyme-substrate reaction mechanisms Acta Chem. Scand. 11 1957 1706 1723
    • (1957) Acta Chem. Scand. , vol.11 , pp. 1706-1723
    • Dalziel, K.1
  • 48
    • 0040030424 scopus 로고
    • On the determination of rate constants for coenzyme mechanisms
    • R.A. Alberty On the determination of rate constants for coenzyme mechanisms J. Am. Chem. Soc. 80 1958 1777 1782
    • (1958) J. Am. Chem. Soc. , vol.80 , pp. 1777-1782
    • Alberty, R.A.1
  • 49
    • 50549188738 scopus 로고
    • Kinetics of enzyme-catalyzed reactions with two or more substrates or products. 2. Inhibition: Nomenclature and theory
    • W.W. Cleland Kinetics of enzyme-catalyzed reactions with two or more substrates or products. 2. Inhibition: nomenclature and theory Biochim. Biophys. Acta 67 1963 173 187
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 173-187
    • Cleland, W.W.1
  • 50
    • 50549155520 scopus 로고
    • Kinetics of enzyme-catalyzed reactions with two or more substrates or products. 3. Prediction of initial velocity and inhibition patterns by inspection
    • W.W. Cleland Kinetics of enzyme-catalyzed reactions with two or more substrates or products. 3. Prediction of initial velocity and inhibition patterns by inspection Biochim. Biophys. Acta 67 1963 188 196
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 188-196
    • Cleland, W.W.1
  • 51
    • 0030800564 scopus 로고    scopus 로고
    • The reversible Hill equation: How to incorporate cooperative enzymes into metabolic models
    • J.H.S. Hofmeyr, and A. Cornish-Bowden The reversible Hill equation: how to incorporate cooperative enzymes into metabolic models Comput. Appl. Biosci. 13 1997 377 385
    • (1997) Comput. Appl. Biosci. , vol.13 , pp. 377-385
    • Hofmeyr, J.H.S.1    Cornish-Bowden, A.2
  • 52
    • 78650082704 scopus 로고    scopus 로고
    • Kinetic and thermodynamic aspects of enzyme control and regulation
    • J.M. Rohwer, and J.H.S. Hofmeyr Kinetic and thermodynamic aspects of enzyme control and regulation J. Phys. Chem. B 114 2010 16280 16289
    • (2010) J. Phys. Chem. B , vol.114 , pp. 16280-16289
    • Rohwer, J.M.1    Hofmeyr, J.H.S.2
  • 53
    • 78650080423 scopus 로고    scopus 로고
    • Specificity of non-Michaelis-Menten enzymes: Necessary information for analyzing metabolic pathways
    • A. Cornish-Bowden, and M.L. Cárdenas Specificity of non-Michaelis-Menten enzymes: necessary information for analyzing metabolic pathways J. Phys. Chem. B 114 2010 16209 16213
    • (2010) J. Phys. Chem. B , vol.114 , pp. 16209-16213
    • Cornish-Bowden, A.1    Cárdenas, M.L.2
  • 54
    • 84883054015 scopus 로고    scopus 로고
    • A note on the decomposition of the kinetics of enzyme action
    • in press
    • E. Noor, A. Flamholz, W. Liebermeister, R. Milo, A note on the decomposition of the kinetics of enzyme action, FEBS Lett., in press (2013).
    • (2013) FEBS Lett.
    • Noor, E.1    Flamholz, A.2    Liebermeister, W.3    Milo, R.4
  • 55
    • 33947472850 scopus 로고
    • A schematic method of deriving the rate laws for enzyme-catalyzed reactions
    • E.L. King, and C. Altman 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
  • 56
    • 0017370629 scopus 로고
    • An automatic method for deriving steady-state rate equations
    • A. Cornish-Bowden An automatic 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
  • 58
    • 0005499841 scopus 로고
    • Statistical estimations in enzyme kinetics
    • G.N. Wilkinson Statistical estimations in enzyme kinetics Biochem. J. 80 1961 324 332
    • (1961) Biochem. J. , vol.80 , pp. 324-332
    • Wilkinson, G.N.1
  • 59
    • 0004184918 scopus 로고
    • Statistical analysis of enzymic steady-state rate data
    • G. Johansen, and R. Lumry Statistical analysis of enzymic steady-state rate data C. R. Trav. Lab. Carlsberg 32 1961 185 214
    • (1961) C. R. Trav. Lab. Carlsberg , vol.32 , pp. 185-214
    • Johansen, G.1    Lumry, R.2
  • 61
    • 0016232066 scopus 로고
    • Catalysis, binding and enzyme-substrate complementarity
    • A.R. Fersht Catalysis, binding and enzyme-substrate complementarity Proc. R. Soc. B - Biol. Sci. 187 1974 397 407
    • (1974) Proc. R. Soc. B - Biol. Sci. , vol.187 , pp. 397-407
    • Fersht, A.R.1
  • 62
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • H. Lineweaver, and D. Burk The determination of enzyme dissociation constants J. Am. Chem. Soc. 56 1934 658 666
    • (1934) J. Am. Chem. Soc. , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 63
    • 77957689590 scopus 로고    scopus 로고
    • Mechanistic constraints from the substrate concentration dependence of enzymatic fluctuations
    • J.R. Moffitt, Y.R. Chemla, and C. Bustamante Mechanistic constraints from the substrate concentration dependence of enzymatic fluctuations Proc. Natl. Acad. Sci. USA 107 2010 15739 15744
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 15739-15744
    • Moffitt, J.R.1    Chemla, Y.R.2    Bustamante, C.3
  • 64
    • 84883050443 scopus 로고    scopus 로고
    • Memory of Professor Leonor Michaelis in Nagoya: Great contributions to biochemistry in Japan in the first half of the 20th century
    • in press
    • T. Nagatsu, In memory of Professor Leonor Michaelis in Nagoya: great contributions to biochemistry in Japan in the first half of the 20th century, FEBS Lett., in press (2013).
    • (2013) FEBS Lett.
    • Nagatsu, T.1
  • 66
    • 84887262038 scopus 로고
    • Relationship of enteritidis-paratyphoid B infections to hyperglycemia in rabbits
    • M.L. Menten, and H.M. Manning Relationship of enteritidis-paratyphoid B infections to hyperglycemia in rabbits J. Infect. Dis. 37 1925 400 410
    • (1925) J. Infect. Dis. , vol.37 , pp. 400-410
    • Menten, M.L.1    Manning, H.M.2
  • 67
    • 0344766833 scopus 로고
    • A coupling histochemical azo dye test for alkaline phosphatase in the kidney
    • M.L. Menten, J. Junge, and M.H. Green A coupling histochemical azo dye test for alkaline phosphatase in the kidney J. Biol. Chem. 153 1944 471 477
    • (1944) J. Biol. Chem. , vol.153 , pp. 471-477
    • Menten, M.L.1    Junge, J.2    Green, M.H.3
  • 68
    • 0038858375 scopus 로고
    • Sedimentation constants and electrophoretic mobilities of adult and fetal carbonylhemoglobin
    • M.A. Andersch, D.A. Wilson, and M.L. Menten Sedimentation constants and electrophoretic mobilities of adult and fetal carbonylhemoglobin J. Biol. Chem. 153 1944 301 305
    • (1944) J. Biol. Chem. , vol.153 , pp. 301-305
    • Andersch, M.A.1    Wilson, D.A.2    Menten, M.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.