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pubmed:abstractText |
We consider an isologous enzyme dimer in which the subunits, if operating independently, would obey Michaelis-Menten kinetics. However, because of neighbor interactions, the rate constants of the kinetic cycle in either subunit depend on the state (E or ES) of the other subunit. The steady-state behavior of this dimer system, with interactions, is investigated. In what is probably the most important special case, ES x ES is destabilized considerably by the neighbor interaction compared to E x ES. This leads to half-of-the-sites reactivity (one subunit is in state ES; the other subunit cycles between E and ES), negative cooperativity, and a considerable enhancement of enzyme activity relative to the activity of independent subunits.
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