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The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism.
Progress in Lipid Research ( IF 14.0 ) Pub Date : 2002-01-05 , DOI: 10.1016/s0163-7827(01)00017-0
Mary C Hunt 1 , Stefan E H Alexson
Affiliation  

Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. These enzymes are localized in almost all cellular compartments such as endoplasmic reticulum, cytosol, mitochondria and peroxisomes. Acyl-CoA thioesterases are highly regulated by peroxisome proliferator-activated receptors (PPARs), and other nutritional factors, which has led to the conclusion that they are involved in lipid metabolism. Although the physiological functions for these enzymes are not yet fully understood, recent cloning and more in-depth characterization of acyl-CoA thioesterases has assisted in discussion of putative functions for specific enzymes. Here we review the acyl-CoA thioesterases characterized to date and also address the diverse putative functions for these enzymes, such as in ligand supply for nuclear receptors, and regulation and termination of fatty acid oxidation in mitochondria and peroxisomes.

中文翻译:

酰基辅酶A硫酯酶在介导细胞内脂质代谢中发挥作用。

酰基辅酶A硫酯酶是一组催化酰基辅酶A水解为游离脂肪酸和辅酶A(CoASH)的酶,具有调节酰基辅酶A,游离脂肪酸和CoASH的细胞内水平的潜力。这些酶几乎位于所有细胞区室,例如内质网,胞质溶胶,线粒体和过氧化物酶体。酰基辅酶A硫酯酶受过氧化物酶体增殖物激活受体(PPAR)和其他营养因素的高度调节,从而得出结论,它们参与脂质代谢。尽管尚未完全了解这些酶的生理功能,但最近对酰基辅酶A硫酯酶的克隆和更深入的表征有助于讨论特定酶的假定功能。
更新日期:2019-11-01
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