Sel'kov E E, Dynnik S N
Biofizika. 1976 Mar-Apr;21(2):214-9.
A mathematical model has been investigated of a reversible flow-through reaction S1 reversible S2 catalyzed by an olygomeric enzyme E(R,T) the protomers of which undergo concerted conformational transitions R reversible T. The isosteric activation of olygomer E by product S2 binding preferably to protomer active sites in conformation R is shown to be a possible cause of hysteresis in the quasi-stationary input characteristic of the reaction, v (s2). The latter determines the rate law of the reaction, provided the concentration of S2 is a quasi-stationary one. The hysteresis of the characteristic v (s1) gives rise to multiple steady states and self-oscillations in the reaction.
研究了一种数学模型,该模型描述了由寡聚酶E(R,T)催化的可逆流通反应S1⇌S2,其单体经历协同构象转变R⇌T。结果表明,产物S2优先结合到构象R中的单体活性位点上对寡聚体E进行等排激活,这可能是反应准稳态输入特性v(s2)出现滞后现象的原因。如果S2的浓度为准稳态,则后者决定了反应的速率定律。特性v(s1)的滞后导致反应中出现多个稳态和自振荡。