AbstractA novel statistical procedure [S. Zwanzig, Math. Opsforsch. Statist. Ser. Statist.11, 23–47 (1980)] is applied to discriminate between kinetic models of enzyme reactions. Two examples are elucidated on the basis of numerically simulated data: 1.(a) Discrimination between a Michaelis-Menten-model and a Hill-equation2.(b) Discrimination between competitive and noncompetitive inhibition of a two-substrate reaction.Next the proposed method is applied to assess a kinetic model of the allosteric enzyme phosphofructokinase from the malarial parasite Plasmodium berghei. It is demonstrated that the novel procedure allows a more sensitive discrimination as it is obtained with alternative statistical tests
This chapter introduces the kinetic models of metabolism followed by examples on the construction of...
BackgroundThe mechanistic description of enzyme kinetics in a dynamic model of metabolism requires s...
In a coupled system of two enzyme-catalysed reactions the concentration of the final product follows...
AbstractA novel statistical procedure [S. Zwanzig, Math. Opsforsch. Statist. Ser. Statist.11, 23–47 ...
AbstractA novel statistical procedure is applied to discriminate between several alternative kinetic...
<div><p>Systems biology relies heavily on the construction of quantitative models of biochemical net...
[eng] The evaluation of individual rate constants involved in any reaction mechanism of an enzymatic...
A theoretical analysis of the distinguishability problem of two rival models of the single enzyme-si...
The proper calibration of models describing enzyme kinetics can be quite challenging. In the literat...
A new criterion is applied for characterization of the kinetic design of enzymes that should be favo...
AbstractThis paper gives a critical account of the two major programs so far published specifically ...
Objective: The study of enzyme kinetics invariably combines mathematics, chemistry and biology. Expe...
International audienceThis chapter describes a practical procedure to dissect metabolic systems, sim...
Enzyme inhibition studies are conducted to characterize enzymes and to examine drug-drug interaction...
theoretical equations to enzyme kinetic data without prior knowledge of weights or error distributio...
This chapter introduces the kinetic models of metabolism followed by examples on the construction of...
BackgroundThe mechanistic description of enzyme kinetics in a dynamic model of metabolism requires s...
In a coupled system of two enzyme-catalysed reactions the concentration of the final product follows...
AbstractA novel statistical procedure [S. Zwanzig, Math. Opsforsch. Statist. Ser. Statist.11, 23–47 ...
AbstractA novel statistical procedure is applied to discriminate between several alternative kinetic...
<div><p>Systems biology relies heavily on the construction of quantitative models of biochemical net...
[eng] The evaluation of individual rate constants involved in any reaction mechanism of an enzymatic...
A theoretical analysis of the distinguishability problem of two rival models of the single enzyme-si...
The proper calibration of models describing enzyme kinetics can be quite challenging. In the literat...
A new criterion is applied for characterization of the kinetic design of enzymes that should be favo...
AbstractThis paper gives a critical account of the two major programs so far published specifically ...
Objective: The study of enzyme kinetics invariably combines mathematics, chemistry and biology. Expe...
International audienceThis chapter describes a practical procedure to dissect metabolic systems, sim...
Enzyme inhibition studies are conducted to characterize enzymes and to examine drug-drug interaction...
theoretical equations to enzyme kinetic data without prior knowledge of weights or error distributio...
This chapter introduces the kinetic models of metabolism followed by examples on the construction of...
BackgroundThe mechanistic description of enzyme kinetics in a dynamic model of metabolism requires s...
In a coupled system of two enzyme-catalysed reactions the concentration of the final product follows...