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Equilibrium analysis of allosteric interactions shows zero-order effects

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Title Equilibrium analysis of allosteric interactions shows zero-order effects
 
Creator MUTALIK, VK
SINGH, AP
EDWARDS, JS
VENKATESH, KV
 
Subject interconvertible enzyme cascades
coli aspartate transcarbamoylase
covalent modification
biochemical systems
protein-kinase
cell
ultrasensitivity
cooperativity
amplification
sensitivity
allosteric protein
cooperativity
hill coefficient
sensitivity amplification
modularity
atcase
 
Description The binding of effector to an allosteric protein exhibits a non-Michaelis-Menten behavior, resulting in either ultrasensitive or subsensitive response. In the present work, a modular approach has been developed to determine the response curve for allosteric systems at higher concentration of allosteric enzyme than that of effector (zero-order sensitivity, as observed in enzyme cascades) by equilibrium analysis. The analysis shows that, in an allosteric system, the zero-order effect can make the response ultrasensitive or subsensitive with respect to the enzyme concentration. The response is dependent on the number of binding sites, cooperativity, and the total effector concentration. The framework was further applied to a well studied allosteric protein, the Escherichia coli aspartate transcarbamoylase. The predictions are found to be consistent with the reported experimental data.
 
Publisher HUMANA PRESS INC
 
Date 2011-07-31T07:36:27Z
2011-12-26T12:52:53Z
2011-12-27T05:39:51Z
2011-07-31T07:36:27Z
2011-12-26T12:52:53Z
2011-12-27T05:39:51Z
2004
 
Type Article
 
Identifier CELL BIOCHEMISTRY AND BIOPHYSICS, 41(2), 179-192
1085-9195
http://dx.doi.org/10.1385/CBB:41:2:179
http://dspace.library.iitb.ac.in/xmlui/handle/10054/8031
http://hdl.handle.net/10054/8031
 
Language en