Journal Article10.1016/0303-2647(89)90003-8
Interdependence between cooperativity and control coefficients.
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TL;DR: It is demonstrated that the best control of the cycle is reached when the irreversible reaction catalyzed by AMP deaminase follows a rate law that corresponds to a rational function of 2:2 degree with respect to AMP concentration.
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Abstract: Influence of the concentration of internal metabolites on the control coefficient (defined as fractional change in flux per fractional change in enzyme activity) and regulatory properties of a given enzyme have been studied theoretically using a cyclic model of three enzymes. This model is useful to investigate the properties of the flux control coefficient for an enzyme following different rate equations. Enzymes can have high or low values of control coefficient irrespective of the type of kinetic equation, but the results obtained show that the sensitivity of these values to substrate variations is strongly dependent on its rate equation. These results help identify which kinetic equation allows the best control of a given metabolic pathway. These results have been applied to the purine nucleotide cycle. It is demonstrated that the best control of the cycle is reached when the irreversible reaction catalyzed by AMP deaminase follows a rate law that corresponds to a rational function of 2 : 2 degree with respect to AMP concentration.
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Citations
Advances in metabolic control analysis
James C. Liao,Javier Delgado +1 more
TL;DR: Both the theoretical and experimental aspects of this analysis are reviewed, with an emphasis on recent developments and issues commonly discussed in the literature.
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A kinetic study of a ternary cycle between adenine nucleotides.
TL;DR: A kinetic study of a moiety‐conserved ternary cycle between the adenine nucleotides showed that there is a threshold value of the S‐acetyl coenzyme A synthetase/adenylate kinase ratio, above which the cycle stops because all the recycling substrate has been accumulated as AMP, never reaching the steady state.
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An approach to the in vitro study of the UTP/UDPglucose/UDP moeity-conserved cycle
TL;DR: That such an experimental ternary substrate cycle actually exhibits a low sensitivity to any perturbation, addresses the issue to knowing if the same property is likely to occur in vivo, or, in other words, do large moiety-conserved cycles act as metabolic buffers?
1
Proteomics and models for enzyme cooperativity.
TL;DR: The type of cooperativity that will be the focus of this review is “allosteric cooperativity”, which has been used to describe a ligand-enzyme interaction, which results in a measurable conformational change in proximal and distal regions of that protein.
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•Journal Article
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Henrik Kacser,J A Burns +1 more
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