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- W200714430 abstract "This chapter discusses the molecular models that attempt to provide a correlation of the kinetic properties of the protein with its structural architecture. Recent reviews that have covered other aspects of the regulatory control—such as the interaction of metabolic pathways, various types of end product inhibition, and the evidence for conformational changes—should be consulted for other aspects of these subjects. Two comprehensive molecular theories capable of explaining allosteric regulation in quantitative terms have been proposed. This chapter describes these models and presents an evaluation of their present status and future use. The control of enzyme action can occur in a number of ways—by product inhibition, by the depletion of substrate, by the failure to synthesize an enzyme, by covalent modification, or by destruction of the enzyme. Although all these mechanisms are available and used by the cell, perhaps the most ubiquitous and efficient process for the regulation of complex metabolic sequences is by the use of effector molecules that are not themselves consumed in the reaction. When it was recognized that the flexibility of an enzyme was an essential feature in its action, the way was paved for the understanding at the molecular level of the process of regulation of enzyme activity by effector molecules that are not themselves consumed in that specific reaction. This led in turn to the elaboration of the concept of a distinct separate site, which played a role in the feedback regulation so prevalent in bacterial systems." @default.
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- W200714430 title "Conformational Aspects of Enzyme Regulation" @default.
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- W200714430 doi "https://doi.org/10.1016/b978-0-12-152801-0.50006-7" @default.
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