Topic
Acyl-CoA
About: Acyl-CoA is a research topic. Over the lifetime, 527 publications have been published within this topic receiving 25134 citations. The topic is also known as: Acyl Coenzyme A.
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TL;DR: It was concluded that both the long hydrocarbon chain and CoA moiety of long chain fatty acyl CoA's are necessary for inhibition of DNA polymerase activity.
1 citations
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TL;DR: In this article , a fluorescence resonance energy transfer (FRET) sensor was developed for LC-acyl-CoAs based on the allosterically regulated interaction between α/β hydrolase domain-containing 5 (ABHD5) and Perilipin 5.
Abstract: Intracellular long-chain acyl-coenzyme As (LC-acyl-CoAs) are thought to be under tight spatial and temporal controls, yet the ability to image LC-acyl-CoAs in live cells is lacking. Here, we developed a fluorescence resonance energy transfer (FRET) sensor for LC-acyl-CoAs based on the allosterically regulated interaction between α/β hydrolase domain-containing 5 (ABHD5) and Perilipin 5. The genetically encoded sensor rapidly detects intracellular LC-acyl-CoAs generated from exogenous and endogenous fatty acids (FAs), as well as synthetic ABHD5 ligands. Stimulation of lipolysis in brown adipocytes elevated intracellular LC-acyl-CoAs in a cyclic fashion, which was eliminated by inhibiting PNPLA2 (ATGL), the major triglyceride lipase. Interestingly, inhibition of LC-acyl-CoA transport into mitochondria elevated intracellular LC-acyl-CoAs and dampened their cycling. Together, these observations reveal an intimate feedback control between LC-acyl-CoA generation from lipolysis and utilization in mitochondria. We anticipate that this sensor will be an important tool to dissect intracellular LC-acyl-CoA dynamics as well to discover novel synthetic ABHD5 ligands.
1 citations
01 May 1987
TL;DR: Alkaline hydrolysis of fatty acyl CoA's prior to measurement of WS radioactivity permits more accurate assessment of beta-oxidation of Hep-G2 cells, and the present method reflects a more accurate and sensitive measurement of oxidation rates.
Abstract: Hep-G2 cells oxidize (1-/sup 14/C)palmitic acid (C16) and (1-/sup 14/C) lignoceric acid (C24) via beta-oxidation to /sup 14/CO/sub 2/ and water-soluble (WS) products. After perchloric acid precipitation and chloroform-methanol extraction, the WS fraction contained labelled oxidation products as well as fatty acyl CoA's, thus, measurement of WS radioactivity is an overestimate of Hep-G2 beta-oxidation. Alkaline hydrolysis of fatty acyl CoA's prior to measurement of WS radioactivity permits more accurate assessment of beta-oxidation. Using this method, the optimal pH for oxidation of each fatty acid to WS products by Hep-G2 cells was 9.0, while /sup 14/CO/sub 2/ production was maximal at pH 7.0. To determine the subcellular location of beta-oxidation, mitochondria (M) were partially separated from peroxisomes (P) on linear Nycodenz gradients. In Hep-G2 cells, oxidation of both C16 and C24 was observed mainly in fractions enriched in succinate dehydrogenase, an M marker enzyme. In contrast, both P and M of rat liver oxidized these fatty acids. However, when Hep-G2 cells were fractionated on discontinuous sucrose gradients, C16 and C24 were oxidized by both P and M fractions. They conclude that beta-oxidation of both long (C16) and very long (C24) chain fatty acids occurs in P as well as in Mmore » of Hep-G2 cells, and the present method reflects a more accurate and sensitive measurement of oxidation rates.« less
1 citations
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01 Jan 1997TL;DR: Carnitine acetyltransferase is involved in the transport of activated acetyl moieties from the mitochondrion and in the reversible reaction Carnitine + short- chain acyl CoA short-chain acylcarnitines + CoASH.
Abstract: Carnitine acetyltransferase ( CAT ) is known to exist in plant mitochondria (spe review [ 2 ]). CAT catalyses the reversible reaction Carnitine + short-chain acyl CoA short-chain acylcarnitine + CoASH and is involved in the transport of activated acetyl moieties from the mitochondrion.
1 citations
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TL;DR: The synthesis of cholesteryl oleate by acyl coenzyme A: cholesterol-O-acyltransferase (EC 2.3.1) from rat liver mitochondria and microsomes in the presence of long chain branched fatty acids was investigated and these acids neither inhibit the formation of ch LDL, nor do they serve as substrate for the enzyme.
1 citations