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 is postulate that a very long chain fatty acyl CoA (VLCFA CoA) synthetase is required for the effective conversion of C 24:0 acid to C24:0 CoA, which appears to be absent from the mitochondrial membrane but present in the peroxisomal membrane.
25 citations
TL;DR: Gastrin inhibits the hydratase, dehydrogenase, and thiolase activities of the trifunctional protein and benzotript inhibited various monofunctional enzymes involved in fatty acid oxidation.
Abstract: The mitochondrial enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein (trifunctional protein) plays a major role in mitochondrial fatty acid oxidation. The enzyme complex consists of four molecules of alpha-subunit containing both hydratase and dehydrogenase domains and four molecules of beta-subunit containing the thiolase domain. The primary structure of a gastrin-binding protein (GBP) was highly homologous to that of the alpha-subunit of the trifunctional protein. Here, we report that gastrin inhibits the hydratase, dehydrogenase, and thiolase activities of the trifunctional protein. The gastrin/cholecystokinin receptor antagonist benzotript, which inhibited binding of gastrin to the GBP, also inhibited all three activities of the trifunctional protein. In addition, benzotript inhibits the activities of multifunctional enzymes having similar structures, such as the peroxisomal enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase bifunctional protein and the Pseudomonas fragi fatty acid oxidation enzyme complex. This reagent, however, hardly inhibited various monofunctional enzymes involved in fatty acid oxidation.
24 citations
TL;DR: The potent inhibition of AMP deaminase by fatty acyl-CoA (FA- CoA) is reported, and its physiological significance is discussed.
24 citations
TL;DR: Nuclear magnetic resonance studies show that the polysaccharide, a random coil in its free form, undergoes a major conformational transition upon enclosing long-chain acyl-CoA.
Abstract: MMP, a linear alpha 1 leads to 4 linked polymer of 3-O-methylmannose, regulates the fatty acid synthetase from Mycobacterium smegmatis by forming stoichiometric complexes with the long-chain acyl-CoA synthetase products. In agreement with previous proposals [Bloch, K. (1977) in Advances in Enzymology and Related Areas of Molecular Biology, ed. Meister, A. (Wiley, New York), Vol. 45, pp. 1-84], nuclear magnetic resonance studies show that the polysaccharide, a random coil in its free form, undergoes a major conformational transition upon enclosing long-chain acyl-CoA. The polysaccharide, probably in helical conformation in the complexed form, interacts with both the paraffinic chain and the CoA moieties of the included fatty acyl thioester.
24 citations
TL;DR: CoASH, Mg2+, ATP and (-)-carnitine were found to be essential for the production of palmitoyl CoA from palmitate by purified barley etio-chloroplasts and it was concluded that long-chain acyl CoA synthetase and carnitine long- chain acyl-transferase activity were present in the etio -chloroplast.
Abstract: CoASH, Mg2+, ATP and (-)-carnitine were found to be essential for the production of palmitoylcarnitine from palmitate by purified barley etio-chloroplasts. It was concluded that long-chain acyl CoA synthetase (palmitoyl CoA synthetase, EC 6.2.1.3) and carnitine long-chain acyl-transferase (carnitine palmitoyltransferase, EC 2.3.1.21) activity were present in the etio-chloroplasts. It is suggested that the long-chain acylcarnitine formed may move more easily through membrane barriers than the long-chain acyl CoA compound. Also or alternatively this enzyme may spare CoA by transferring long-chain acyl groups from long-chain acyl CoA to carnitine.
24 citations