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Acetyl—CoA synthetase - Wikipedia

In the latter case, conversion of acetyl-CoA to malonyl-CoA is the rate limiting step in fatty acid synthesis.

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Acyl-CoA synthetase | Sigma-Aldrich

Pantothenic acid is also known as vitamin B5. It is a component of coenzyme A (CoA), an essential coenzyme in a variety of reactions that sustain life. CoA is required for chemical reactions that generate energy from food (fat, carbohydrates, and proteins). The synthesis of essential fats, cholesterol, and steroid hormones requires CoA, as does the synthesis of the neurotransmitter, acetylcholine, and the hormone, melatonin. Heme, a component of hemoglobin, requires a CoA-containing compound for its synthesis. Metabolism of a number of drugs and toxins by the liver requires CoA.

Search results for Acyl-CoA synthetase at Sigma-Aldrich

Fatty acids synthesis uses acetyl-CoA as main substrate. However, since the process is quite endergonic acetyl-CoA must be activated, which happens through carboxylation. Like other carboxylases (e.g., those of or ), Acetyl-CoA carboxilase uses biotin as a prosthetic group.

02/09/2009 · Request (PDF) | Acyl-CoA synthesis,..

T1 - Acyl CoA and lipid synthesis from ketone bodies by the extramitochondrial fraction of hepatoma tissue

Succesive rouds of the cycle eventually lead to the total degradation of even-chain fatty acids in acetyl-CoA, which can be completely oxidized to CO2 through the : even-chain fatty acids cannot be used for net synthesis of oxaloacetate, and therefore are not a substrate for .

AB - BioF (8-amino-7-oxononanoate synthase) is a strictly conserved enzyme that catalyzes the first step in assembly of the fused heterocyclic rings of biotin. The BioF acyl chain donor has long been thought to be pimeloyl-CoA. Indeed, in vitro the Escherichia coli and Bacillus sphaericus enzymes have been shown to condense pimeloyl-CoA with L-alanine in a pyridoxal 5=-phosphate-dependent reaction with concomitant CoA release and decarboxylation of L-alanine. However, recent in vivo studies of E. coli and Bacillus subtilis suggested that the BioF proteins of the two bacteria could have different specificities for pimelate thioesters in that E. coli BioF may utilize either pimeloyl coenzyme A (CoA) or the pimelate thioester of the acyl carrier protein (ACP) of fatty acid synthesis. In contrast, B. subtilis BioF seemed likely to be specific for pimeloyl-CoA and unable to utilize pimeloyl-ACP. We now report genetic and in vitro data demonstrating that B. subtilis BioF specifically utilizes pimeloyl-CoA.

In fatty acid synthesis, acetyl‐CoA is ..

However, these acetyl-CoA's cannot leave the mitochondria, and are therefore not available for FA synthesis.

Much of the acetyl-CoA produced by fatty acid -oxidation in liver mitochodria is converted in acetoacetateand -hydroxybutyrate(also known as ketone bodies). These molecules can be used by heart and skeletal muscle to produce energy. Brain, which usually depends on glucose as sole energy source, can also use ketone bodies during a long fasting period (larger than two or three days). Ketogenesis (ketone bodies synthesis) begins with the condensation of two acetyl-CoA molecules to form acetoacetyl-CoA:

N2 - BioF (8-amino-7-oxononanoate synthase) is a strictly conserved enzyme that catalyzes the first step in assembly of the fused heterocyclic rings of biotin. The BioF acyl chain donor has long been thought to be pimeloyl-CoA. Indeed, in vitro the Escherichia coli and Bacillus sphaericus enzymes have been shown to condense pimeloyl-CoA with L-alanine in a pyridoxal 5=-phosphate-dependent reaction with concomitant CoA release and decarboxylation of L-alanine. However, recent in vivo studies of E. coli and Bacillus subtilis suggested that the BioF proteins of the two bacteria could have different specificities for pimelate thioesters in that E. coli BioF may utilize either pimeloyl coenzyme A (CoA) or the pimelate thioester of the acyl carrier protein (ACP) of fatty acid synthesis. In contrast, B. subtilis BioF seemed likely to be specific for pimeloyl-CoA and unable to utilize pimeloyl-ACP. We now report genetic and in vitro data demonstrating that B. subtilis BioF specifically utilizes pimeloyl-CoA.

T1 - Rat long chain acyl-CoA synthetase 5 increases fatty acid uptake and partitioning to cellular triacylglycerol in McArdle-RH7777 cells
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  • Synthesis of acyl-CoA thioesters - ResearchGate

    Synthesis of Acetyl CoA

  • The Acyl-CoA Synthetase Encoded by LACS2 Is Essential …

    While acetyl CoA can be synthesized via pyruvate or amino acids, it can also be formed by the breakdown of acyl-CoA

  • Engineered short branched-chain acyl-CoA synthesis in …

    Acyl-CoA_synthetase-WikiOmni

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Fatty-acyl-CoA synthase - Wikipedia

When acetyl-CoA is abundant, liver and adipose tissue synthesize fatty acids. The syntheis pathway is quite similar to the reverse of -oxidation, but presents several imporatant differences:

Fatty acids are first converted to acyl-CoA

Fatty acid synthesis happens in the cytoplasm, but acetyl-CoA is produced in the mitochondrion. Therefore acetyl-CoA must cross the inner mitochondrial membrane before it can be used in fatty acid synthesis. This is performed by the citrate shuttle: citrate is formed in the mitochondrion by and diffuses through the membrane into the cytoplasm, where it gets cleaved by citrate-lyase into acetyl-CoA and oxaloacetate, whic, upon reduction to malate, can return to the mitochondrial matrix. Malate can also be used to produce part of the NADPH needed for fatty acid synthesis, through the action of the . The remainder of the NADPH needed for fatty acid synthesis must be produced by the .

Acyl-CoAs, insulin resistance, and lipotoxicity

BioF (8-amino-7-oxononanoate synthase) is a strictly conserved enzyme that catalyzes the first step in assembly of the fused heterocyclic rings of biotin. The BioF acyl chain donor has long been thought to be pimeloyl-CoA. Indeed, in vitro the Escherichia coli and Bacillus sphaericus enzymes have been shown to condense pimeloyl-CoA with L-alanine in a pyridoxal 5=-phosphate-dependent reaction with concomitant CoA release and decarboxylation of L-alanine. However, recent in vivo studies of E. coli and Bacillus subtilis suggested that the BioF proteins of the two bacteria could have different specificities for pimelate thioesters in that E. coli BioF may utilize either pimeloyl coenzyme A (CoA) or the pimelate thioester of the acyl carrier protein (ACP) of fatty acid synthesis. In contrast, B. subtilis BioF seemed likely to be specific for pimeloyl-CoA and unable to utilize pimeloyl-ACP. We now report genetic and in vitro data demonstrating that B. subtilis BioF specifically utilizes pimeloyl-CoA.

ATP-independent Fatty Acyl-Coenzyme A Synthesis …

Note that acetate carbons come into play twice, once as the source of acetyl-CoA to enter the malonyl-CoA pathway and once as the source of malonyl-CoA that adds the two carbons to each cycle of the fatty acid synthetase.

ATP-independent fatty acyl-coenzyme A synthesis …

Although the underlying causes of insulin resistance have not been completely delineated, in most analyses, a recurring theme is dysfunctional metabolism of fatty acids. Because the conversion of fatty acids to activated acyl-CoAs is the first and essential step in the metabolism of long-chain fatty acid metabolism, interest has grown in the synthesis of acyl-CoAs, their contribution to the formation of signaling molecules like ceramide and diacylglycerol, and their direct effects on cell function. In this review, we cover the evidence for the involvement of acyl-CoAs in what has been termed lipotoxicity, the regulation of the acyl-CoA synthetases, and the emerging functional roles of acyl-CoAs in the major tissues that contribute to insulin resistance and lipotoxicity, adipose, liver, heart and pancreas.

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