enzymatic rate law for modulated unireactant enzymes enzymatic rate law for irreversible allosteric inhibition <n0:math xmlns:n0="http://www.w3.org/1998/Math/MathML"> <n2:semantics xmlns:n2="http://biomodels.net/SBO/" definitionURL="http://biomodels.net/SBO/#SBO:0000062"> <n2:lambda> <n2:bvar> <n2:ci definitionURL="http://biomodels.net/SBO/#SBO:0000515"> substrate </n2:ci> </n2:bvar> <n2:bvar> <n2:ci definitionURL="http://biomodels.net/SBO/#SBO:0000521"> Inhibitor </n2:ci> </n2:bvar> <n2:bvar> <n2:ci definitionURL="http://biomodels.net/SBO/#SBO:0000324"> V </n2:ci> </n2:bvar> <n2:bvar> <n2:ci definitionURL="http://biomodels.net/SBO/#SBO:0000282"> Ks </n2:ci> </n2:bvar> <n2:bvar> <n2:ci definitionURL="http://biomodels.net/SBO/#SBO:0000189"> n </n2:ci> </n2:bvar> <n2:bvar> <n2:ci definitionURL="http://biomodels.net/SBO/#SBO:0000281"> L </n2:ci> </n2:bvar> <n2:bvar> <n2:ci definitionURL="http://biomodels.net/SBO/#SBO:0000261"> Ki </n2:ci> </n2:bvar> <n2:apply> <n2:divide /> <n2:apply> <n2:times /> <n2:ci> V </n2:ci> <n2:ci> substrate </n2:ci> <n2:apply> <n2:power /> <n2:apply> <n2:plus /> <n2:ci> Ks </n2:ci> <n2:ci> substrate </n2:ci> </n2:apply> <n2:apply> <n2:minus /> <n2:ci> n </n2:ci> <n2:cn> 1 </n2:cn> </n2:apply> </n2:apply> </n2:apply> <n2:apply> <n2:plus /> <n2:apply> <n2:times /> <n2:ci> L </n2:ci> <n2:apply> <n2:power /> <n2:apply> <n2:times /> <n2:ci> Ks </n2:ci> <n2:apply> <n2:plus /> <n2:cn> 1 </n2:cn> <n2:apply> <n2:divide /> <n2:ci> Inhibitor </n2:ci> <n2:ci> Ki </n2:ci> </n2:apply> </n2:apply> </n2:apply> <n2:ci> n </n2:ci> </n2:apply> </n2:apply> <n2:apply> <n2:power /> <n2:apply> <n2:plus /> <n2:ci> Ks </n2:ci> <n2:ci> substrate </n2:ci> </n2:apply> <n2:ci> n </n2:ci> </n2:apply> </n2:apply> </n2:apply> </n2:lambda> </n2:semantics> </n0:math> Enzymatic rate law which follows from the allosteric concerted model (symmetry model or MWC model).This states that enzyme subunits can assume one of two conformational states (relaxed or tense), and that the state of one subunit is shared or enforced on the others. The binding of a ligand to a site other than that bound by the substrate (active site) can shift the conformation from one state to the other. L represents the equilibrium constant between active and inactive states of the enzyme, and n represents the number of binding sites for the substrate and inhibitor.