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: ACBP was the most potent intracellular fatty acyl CoA binding protein in differentially modulating the activity of microsomal ACAT to form cholesteryl esters independent of cholesterol binding/transfer ability.
63 citations
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TL;DR: The properties of enzymatic systems involved in the synthesis of long chain aldehydes and alcohols have been reviewed and fatty acid and acyl-CoA reductases are widely distributed and generate fatty alcohols for ether lipid and was ester synthesis as well as fatty aldeHydes for bacterial bioluminescence.
Abstract: The properties of enzymatic systems involved in the synthesis of long chain aldehydes and alcohols have been reviewed. Fatty acid and acyl-CoA reductases are widely distributed and generate fatty alcohols for ether lipid and wax ester synthesis as well as fatty aldehydes for bacterial bioluminescence. Fatty alcohol is generally the major product of fatty acid reduction in crude or membrane systems, although reductases which release fatty aldehydes as products have also been purified. The reduction of fatty acid proceeds through the ATP-dependent formation of acyl intermediates such as acyl-CoA and acyl protein, followed by reduction to aldehyde and alcohol with NAD(P)H. In most cases, both the rate of fatty acid conversion and acyl chain specificity of the reaction are determined at the level of reduction of the intermediate. The reduction of fatty acids represents the major pathway for the control of the synthesis of fatty aldehydes and alcohols. Several other enzymatic reactions involved in lipid degradation also release fatty aldehydes but do not appear to play an important role in long chain alcohol synthesis.
61 citations
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TL;DR: In this study, highly pure recombinant L-FABP and I-F ABP were used first to establish binding to fatty acyl-CoAs and then to examine the effects of these FABPs on microsomal phosphatidic acid synthesis.
Abstract: Rat liver fatty acid binding protein (L-FABP) and rat intestine fatty acid binding protein (I-FABP) are homologous proteins which are both found in intestinal epithelial cells. It was once well accepted that liver fatty acid binding protein bound fatty acyl-CoAs, but the recent finding of a novel acyl-CoA binding protein (ACBP) in preparations of L-FABP has challenged the role of FABPs in acyl-CoA metabolism. Prior to the discovery of ACBP, L-FABP preparations from liver were shown to modulate the rate of fatty acyl-CoA synthesis (Burrier et al., 1987) and their conversion to phospholipids (Bordewick et al., 1989). Studies using FABPs free of ACBP are needed to determine the role of I-FABP and L-FABP in fatty acyl-CoA metabolism. In this study, highly pure recombinant L-FABP and I-FABP were used first to establish binding to fatty acyl-CoAs and then to examine the effects of these FABPs on microsomal phosphatidic acid synthesis. The standard Lipidex-1000 binding assay using [14C]oleoyl-CoA and a new fluorescence binding assay using the fluorescent fatty acyl-CoA cis-parinaroyl-CoA were used to determine binding. The results of these assays indicate that L-FABP binds fatty acyl-CoAs at two sites with a high-affinity Kd = 3-14 microM. These binding assays showed that I-FABP has a much lower affinity for fatty acyl-CoAs than does L-FABP. Furthermore, in vitro only L-FABP significantly increases the rate of incorporation of oleoyl-CoA into lysophosphatidic acid and phosphatidic acid.
61 citations
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TL;DR: It is suggested that hepatic DGat2 deficiency successfully reduces diet‐induced HS and supports development of DGAT2 inhibitors as a therapeutic strategy for treating NAFLD and preventing downstream consequences.
61 citations
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TL;DR: Analysis of PHA production yields during growth on fatty acids with different chain lengths has revealed that the POX genotype significantly affects the PHA levels, but not the monomer composition of Pha, while three known models of β-oxidation are discussed and a 'leaky-hose pipe model' of the cycle can be applied to Y. lipolytica.
Abstract: The oleaginous yeast Yarrowia lipolytica possesses six acyl-CoA oxidase (Aox) isoenzymes encoded by genes POX1-POX6. The respective roles of these multiple Aox isoenzymes were studied in recombinant Y. lipolytica strains that express heterologous polyhydroxyalkanoate (PHA) synthase (phaC) of Pseudomonas aeruginosa in varying POX genetic backgrounds, thus allowing assessment of the impact of specific Aox enzymes on the routing of carbon flow to β-oxidation or to PHA biosynthesis. Analysis of PHA production yields during growth on fatty acids with different chain lengths has revealed that the POX genotype significantly affects the PHA levels, but not the monomer composition of PHA. Aox3p function was found to be responsible for 90% and 75% of the total PHA produced from either C9:0 or C13:0 fatty acid, respectively, whereas Aox5p encodes the main Aox involved in the biosynthesis of 70% of PHA from C9:0 fatty acid. Other Aoxs, such as Aox1p, Aox2p, Aox4p and Aox6p, were not found to play a significant role in PHA biosynthesis, independent of the chain length of the fatty acid used. Finally, three known models of β-oxidation are discussed and it is shown that a 'leaky-hose pipe model' of the cycle can be applied to Y. lipolytica.
60 citations