Regulation of mammalian acetyl-CoA carboxylase
Regulation of mammalian acetyl-CoA carboxylase
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DOI：
10.1042/bst0301059
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发表时间：
2002-11-01
影响因子：
3.9
通讯作者：
Munday, MR
中科院分区：
文献类型：
--
作者：
Munday, MR
乙酰辅酶A羧化酶(ACC)在调节脂肪酸代谢中起着重要作用，其两种异构体ACCalpha和ACCbeta分别在控制脂肪酸合成和脂肪酸氧化中具有不同的功能。它们受到类似的短期机制的调节，如柠檬酸对变构的激活，以及可逆的磷酸化和失活，这些机制之间存在明显的相互作用。AMP激活的蛋白激酶是这两种异构体重要的生理性ACC激酶，但cAMP依赖的蛋白激酶在激素介导的ACCalpha失活和ACCbeta在其独特的N端的磷酸化中具有潜在的生理作用。
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.