Munday M R
Department of Pharmaceutical and Biological Chemistry, School of Pharmacy, University of London, 29-39 Brunswick Square, UK.
Biochem Soc Trans. 2002 Nov;30(Pt 6):1059-64. doi: 10.1042/bst0301059.
Acetyl-CoA carboxylase (ACC) plays a critical role in the regulation of fatty acid metabolism and its two isoforms, ACCalpha and ACCbeta, appear to have distinct functions in the control of fatty acid synthesis and fatty acid oxidation, respectively. They are regulated by similar short-term mechanisms of allosteric activation by citrate, and reversible phosphorylation and inactivation, and there is clearly interaction between these mechanisms. AMP-activated protein kinase is the important physiological ACC kinase for both isoforms and yet there is a potential physiological role for cAMP-dependent protein kinase in the hormonally mediated inactivation of ACCalpha, and phosphorylation of ACCbeta in its unique N-terminus.
乙酰辅酶A羧化酶（ACC）在脂肪酸代谢调节中起关键作用，其两种同工型ACCα和ACCβ似乎在脂肪酸合成和脂肪酸氧化的控制中分别具有不同功能。它们受到类似的短期变构激活机制（由柠檬酸激活）、可逆磷酸化和失活的调节，并且这些机制之间存在明显的相互作用。AMP激活的蛋白激酶是两种同工型重要的生理性ACC激酶，但cAMP依赖性蛋白激酶在激素介导的ACCα失活以及ACCβ独特N端的磷酸化过程中可能具有生理作用。
