Abstract
A two-state model of an enzyme with an allosteric regulatory site capable of metabolizing the regulatory ligand. Simplified mathematical treatments of transient and steady state kinetics of an activator and its competitive inhibition as applied to adenylyl cyclases.
Highlights
The simplest model that can account fotrhe existence rate with which substrate is converted into product, giving of a system inwhich allosteric activation of an enzyme rise to so-called “V-systems” (1, 2)
Sented includethe option that theallosteric ligandbind- The simplest possible model of a V-system is one in which ing sitebe capable of metabolizingthe ligand in a the enzyme exists in only two preferred conformations with manner independent of microscopic reversibility prin- differing h, values and in which the role of the ligand is to ciples and thermodynamic equilibrium laws that gov- stabilize one of these conformations
Simulations v/Vmax= E ' / E I + E'I./E, (6) We explored properties of the two-statemodel with respect with E', ElL,and E t representing concentrationsof free active state of the enzyme, active state of the enzyme with ligand bound to it, and toetanlzyme, respectively.Due to thceircular arrangement of a two-state model such as shown in Scheme
Summary
The simplest model that can account fotrhe existence rate with which substrate is converted into product, giving of a system inwhich allosteric activation of an enzyme rise to so-called “V-systems” (1, 2). If the ligand stabilizes ern all other reaction rates of the two-state model.
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