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• W1597091566 abstract "Abstract Evidence concerning conformational changes in aspartate transcarbamylase of Escherichia coli is reviewed in order to evaluate the level of structural organization at which the changes relevant to allosteric behavior take place, and to assess the contribution of each kind of subunit to this behavior. It is suggested that the conformational change responsible for allosteric behavior is a slight quaternary rearrangement, rather than a tertiary structural change which modifies the active centers. A functional unit is postulated which consists of two catalytic chains separated by a dimer of the regulatory chains. The conformational change resulting in allosteric behavior is generated by the pivoting of the regulatory dimer between two positions, in one of which the two catalytic sites are blocked by the dimer. In the catalytically active conformation the blocking portions of the regulatory dimer become exposed. The unit is symmetrical and acts in a concerted manner. This hypothesis accounts for the observations that (a) both homotropic and heterotropic effects depend on the integrity of the regulatory subunits; (b) the intact, isolated catalytic trimer is incapable of allosteric behavior; (c) in the T state not only is there no catalytic activity, but the active sites cannot bind substrate; (d) the reactivity of thiol groups and peptide bonds of the regulatory subunit is increased when substrate is bound to the catalytic subunit; and (e) upon treatment with mercurials the enzyme dissociates into regulatory dimers and catalytic trimers, rather than into mixed protomers. Depending on the manner in which three such functional units are linked together to form the complete oligomer, the allosteric properties can be amplified and can yield either concerted or sequential behavior. The properties of two such oligomers are discussed." @default.
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• W1597091566 date "1971-02-01" @default.
• W1597091566 modified "2023-10-11" @default.
• W1597091566 title "Conformational Changes in Aspartate Transcarbamylase" @default.
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• W1597091566 doi "https://doi.org/10.1016/s0021-9258(18)62476-7" @default.
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