Pettersson G
Department of Biochemistry, University of Lund, Sweden.
Biochim Biophys Acta. 1993 Jun 24;1164(1):1-7. doi: 10.1016/0167-4838(93)90104-y.
The rate equations for a sequence of enzymic reactions conforming to Michaelis-Menten kinetics have been analyzed in order to establish what kinetic design optimizes the steady-state reaction flux for a given total concentration of enzymes and a given average magnitude of true and apparent first-order rate constants in the reaction system. Analytical solutions are presented which have been derived with the assumptions that the concentration of the first substrate in the pathway represents a fixed parameter and that no diffusional constraints come into operation. The solutions prescribe that reaction flux in the examined system becomes optimal when all of the enzymes are present at equal active-site concentrations. The optimal kinetic design of each enzyme reaction is characterized by forward (true or apparent) first-order rate constants of equal magnitude and reverse rate constants of equal magnitude. This means that the optimal kinetic design of the examined pathway is highly uniform, individual enzymes being likely to exhibit optimal V values differing by a factor less than 5 and optimal Km/[S] values falling within the range 0.3-2.
为了确定在给定的酶总浓度以及反应系统中真实和表观一级速率常数的给定平均大小情况下，哪种动力学设计能优化稳态反应通量，对符合米氏动力学的一系列酶促反应的速率方程进行了分析。给出了分析解，其推导假设为途径中第一种底物的浓度代表一个固定参数，且不存在扩散限制作用。这些解规定，当所有酶以相等的活性位点浓度存在时，所研究系统中的反应通量达到最优。每个酶促反应的最优动力学设计的特征是正向（真实或表观）一级速率常数大小相等且逆向速率常数大小相等。这意味着所研究途径的最优动力学设计高度统一，单个酶可能表现出最优V值相差小于5倍，且最优Km/[S]值在0.3 - 2范围内。
