Preconditioning: An Obligatory Step in the Biosynthesis of Oligomeric Enzymes and its Promotion by Allosteric Ligands

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Abstract
An obligatory intermediate in the biosynthesis of oligomeric enzymes is an unstable species, catalytically inactive, that must undergo a conformational transition to yield the thermodynamically more stable active enzyme. This maturation process, which we term preconditioning, represents a rate limiting step in enzyme formation. We propose that allosteric ligands can specifically enhance the rate of preconditioning. This is in contrast to their role in the modulation of enzyme activity, where they stabilize either an active or inactive conformation of the protein in a freely reversible equilibrium. An effect on preconditioning may have been the original role of many allosteric ligands and could subsequently have evolved into the allosteric regulation of enzyme activity. Specific examples are cited to support our hypothesis.

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