Kim K H
Mol Cell Biochem. 1979 Dec 14;28(1-3):27-43. doi: 10.1007/BF00223358.
In this review, various experiments which establish the occurrence of covalent modification mechanisms, both in vivo and in vitro, in the control of acetyl-CoA carboxylase have been presented. It is interesting to note that phosphorylation of the carboxylase results in disaggregation of the active species. These studies indicate that aggregation and disaggregation of the enzyme are involved in the control of carboxylase activity. Our covalent modification mechanism and the allosteric control mechanism share a common ground in that both mechanisms affect the equilibrium between protomers and polymers of the enzyme. However, it is clear that the allosteric control mechanism cannot function alone under normal physiological conditions. Covalent modification of the carboxylase is prerequisite for efficient functioning of the allosteric mechanism. There are many aspects of the regulation of acetyl-CoA carboxylase which require further clarification. However, it is now established that short-term control of acetyl-CoA carboxylase involves the covalent modification mechanism.
在本综述中，已介绍了各种在体内和体外确定共价修饰机制在乙酰辅酶A羧化酶调控中发生情况的实验。值得注意的是，羧化酶的磷酸化导致活性物种解聚。这些研究表明，酶的聚集和解聚参与了羧化酶活性的调控。我们的共价修饰机制和变构调控机制有一个共同点，即两种机制都影响酶原聚体和聚合物之间的平衡。然而，很明显，变构调控机制在正常生理条件下不能单独发挥作用。羧化酶的共价修饰是变构机制有效运作的先决条件。乙酰辅酶A羧化酶调控的许多方面需要进一步阐明。然而，现在已经确定，乙酰辅酶A羧化酶的短期调控涉及共价修饰机制。
