Varón R, Havsteen B H, Molina-Alarcón M, Szedlacsek S E, García-Moreno M, García-Cánovas F
Departamento de Química-Física, Escuela Universitaria Politécnica, Universidad de Castilla-La Mancha, Albacete, Spain.
Int J Biochem. 1994 Jun;26(6):787-97. doi: 10.1016/0020-711x(94)90108-2.
A kinetic analysis of the closed bicyclic enzyme cascades is presented. 1. It includes the dependence on time from the onset of the reaction, of the concentration of the modified and unmodified enzyme species involved and the time course equations of the modificational fractions of the interconvertible enzymes. 2. The transient phase equations obtained allow the definition of new regulatory modification properties. 3. The expressions for concentrations of the unmodified and modified forms of the interconvertible enzymes, as well as those of the fractional modifications in the steady state are derived as particular cases of the general equations. 4. These steady state expressions coincide with those obtained by other authors. 5. The analytical results obtained are discussed in relation to the Escherichia coli glutamine synthetase cascade.
本文对封闭的双环酶级联反应进行了动力学分析。1. 它包括反应开始后,所涉及的修饰和未修饰酶种类的浓度随时间的变化,以及可相互转化酶的修饰分数的时间进程方程。2. 所得到的瞬态阶段方程允许定义新的调节修饰特性。3. 作为一般方程的特殊情况,推导出了可相互转化酶的未修饰和修饰形式的浓度表达式,以及稳态下的分数修饰表达式。4. 这些稳态表达式与其他作者得到的表达式一致。5. 结合大肠杆菌谷氨酰胺合成酶级联反应对所获得的分析结果进行了讨论。