Cooperativity and slow transitions in the regulation of oligomeric and monomeric enzymes

Abstract

Ligand-induced slow transitions (e.g., isomerizations) between different functional states (conformations) of an enzyme (a) have been observed in a number of key regulatory enzymes, (b) can account for kinetic cooperativity of even a monomeric enzyme with a single catalytic site, and (c) can be an alternative to site-site interactions (rapid interactions between substrate binding sites on different subunits) as an explanation for kinetic cooperativity of a multisubunit enzyme.