Bistability and the ordered bimolecular mechanism.
An equation describing the instantaneous velocity of an ordered bimolecular enzymatic reaction that exhibits inhibition by substrate and product was derived. Using kinetic constant values for horse liver alcohol dehydrogenase, the velocity expression was applied to an open-reaction system. The calculated steady-state surfaces displayed regions of bistability, which further substantiates the link between substrate inhibition and multiple steady states. This general computational approach may be applied to any system that can be described by an instantaneous velocity equation.
Raymond
K W
KW
Department of Chemistry and Biochemistry, Eastern Washington University, Cheney 99004.
Pocker
Y
Y
D000426:Alcohol Dehydrogenase / Q000037:antagonists & inhibitors / Q000378:metabolism; D000818:Animals; D004791:Enzyme Inhibitors / Q000378:metabolism; D004798:Enzymes / Q000378:metabolism*; D006736:Horses; D007700:Kinetics
D004791:Enzyme Inhibitors; D004798:Enzymes; D000426:Alcohol Dehydrogenase