Models of Enzyme Kinetics

MODELS OF ENZYME KINETICS 10.2.1 Michaelis-Menten Model... 

Such a mechanism is also used for the simplest model of enzyme kinetics—the Michaelis-Menten model. 

In addition to the thermodynamic constraints on the reaction kinetics, a number of assumptions (including quasi-equilibrium binding and quasi-steady state assumptions) are often invoked in computer modeling of enzyme kinetics. Analysis of enzyme kinetics is treated in greater depth in Chapter 4. 

See. for example. I. H. Segel, Enzyme Kinetics. New York Wiley. 1975 C. F. Lam, Techniques for the Analysis and Modelling of Enzyme Kinetic Mechanisms. Chichester Research Studies Press-Wiley, 1981. 

Early applications of the transform-both-sides approach generally were done to transform a nonlinear problem into a linear one. One of the most common examples is found in enzyme kinetics. Given the Michae-lis-Menten model of enzyme kinetics... 

Aminoacylase kinetics may be used as an example for demonstrating the measurement and modeling of enzyme kinetics. This reaction is of industrial importance in... 

CST reactors have been more widely adopted, partly due to the possibility of concentration polarization control, and partly due to the easy modeling of enzyme kinetic behavior. In the literature, comprehensive mathematical descriptions of the kinetic behavior of enzymes located in CSTR UF units are reported 9 1-0 as far as low-molecular-weight substrates are concerned. 

The equations of enzyme kinetics provide a quantitative way of desaibing the dependence of enzyme rate on substrate concentration. The simplest of these equations, the Michaelis-Menten equation, relates the initial velocity (Vj) to the concentration of substrate [S] and the two parametCTS and (Equation 9.1) The of the enzyme is the maximal velocity that can be achieved at an infinite concentration of substrate, and the of the enzyme for a substrate is the concentration of substrate required to reach Vz V iax- The Michaelis-Menten model of enzyme kinetics applies to a simple reaction in which the enzyme and substrate form an enzyme-substrate complex (ES) that can dissociate back to the free enzyme and substrate. The initial velocity of product formation, Vj, is proportionate to the concentration of enzyme-substrate complexes [ES]. As substrate concentration is increased, the concentration of enzyme-substrate complexes increases, and the reaction rate inaeases proportionately. 

Another interpretation of relies on the assumptions of the original Michaelis-Menten model of enzyme kinetics. Recall Equation 6.4 ... 

Reflect and Apply What is the relationship between a transition-state analog and the induced-fit model of enzyme kinetics ... 

Outline the Michaelis-Menten model of enzyme kinetics and describe the molecular nature of each of its components. 

Lam, C.F. (1981) Techniques for the analysis and modeling of enzyme kinetics mechanisms, Research Studies Press, Chichester. 

Inhibitors of enzyme kinetics. The Michaelis-Menten model of enzyme kinetics gives the reaction velocity V in terms of a maximum rate I max as... 

Li, B., Li, B. Quasi-steady-slate laws in reversible model of enzyme kinetics. J. Math. Chem. 51, 2668-2686 (2013)... 

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