By Vladimir Leskovac
ISBN-10: 0306467127
ISBN-13: 9780306467127
This publication presents a scientific creation to the sphere of enzyme-catalyzed reactions. The content material develops from monosubstrate to bisubstrate to trisubstrate reactions, concluding with nonhyperbolic fee equations and allosteric and cooperative results. since it outlines the topic in this sort of approach that it builds from easier to extra hard kinetic versions, it may be used as a textbook for college students of biochemistry and molecular biology. the writer stresses the significance of graphical illustration of kinetic versions via common use of such mathematical versions within the type of double-reciprocal plots. furthermore, exact cognizance is paid to isotope trade reviews, kinetic isotope results, and the statistical assessment of preliminary cost and ligand binding facts.
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1963) Biochim. Biophys. Acta 67, 104–137. E. S. (1965) J. Biol. Chem. 240, 863-869. S. (1942) J. Biol. Chem. 146, 85–93. Fischer, E. (1894) Ber. Dtsch. Chem. Ges. 27, 2985-2993. S. (1932) Biochem. J. 26,1406-1421. Henri, V. (1902) R. Hebd, Seances Acad. Sci. 135, 916–919. J. (1952) J. Biol. Chem. 199, 357–364. Hultin, E. (1967) Acta Chem. Scand. 21, 1575–1590. Inouye, A. S. (1967) Biochemistry 6, 1765–1777. Johanson, G. & Lumry, R. (1961) C. R. Trav. Lab. Carlsberg 32, 185–214. Lineweaver, H. & Burk, D.
In contrast, intermediates, whose bonds are fully formed, occupy the troughs in the diagram. A simple way of deriving the rate law of reaction is to consider that the transition state and the ground state are in thermodynamic equilibrium, so that the concentration of the transition state may be calculated from the difference in their energies. The overall reaction rate is then obtained by multiplying the concentration of the transition state by the rate constant for its decomposition. Transition-state theory can also be expressed in thermodynamic terms (Panchenkov & Lebedev, 1976; Moore & Pearson, 1982; Atkins & de Paula, 2002).
J. 26,1406-1421. Henri, V. (1902) R. Hebd, Seances Acad. Sci. 135, 916–919. J. (1952) J. Biol. Chem. 199, 357–364. Hultin, E. (1967) Acta Chem. Scand. 21, 1575–1590. Inouye, A. S. (1967) Biochemistry 6, 1765–1777. Johanson, G. & Lumry, R. (1961) C. R. Trav. Lab. Carlsberg 32, 185–214. Lineweaver, H. & Burk, D. (1934) J. Am. Chem. Soc. 56, 658–666. Michaelis, L. L. (1913) Biochem. Z. 49, 333–369. O’Sullivan, C. W. (1890) J. Chem. Soc. Trans. 57, 834–931. J. & Prvan, T. (1996) J. Theor. Biol. 178, 239–254.
Comprehensive Enzyme Kinetics by Vladimir Leskovac
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