Relevant bibliographies by topics / Acyl-CoAs metabolome

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Academic literature on the topic 'Acyl-CoAs metabolome'

Author: Grafiati
Published: 27 July 2024
Last updated: 31 July 2025

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Journal articles on the topic "Acyl-CoAs metabolome"

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Tokarska-Schlattner, Malgorzata, Nour Zeaiter, Valérie Cunin, et al. "Multi-Method Quantification of Acetyl-Coenzyme A and Further Acyl-Coenzyme A Species in Normal and Ischemic Rat Liver." International Journal of Molecular Sciences 24, no. 19 (2023): 14957. http://dx.doi.org/10.3390/ijms241914957.

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Thioesters of coenzyme A (CoA) carrying different acyl chains (acyl-CoAs) are central intermediates of many metabolic pathways and donor molecules for protein lysine acylation. Acyl-CoA species largely differ in terms of cellular concentrations and physico-chemical properties, rendering their analysis challenging. Here, we compare several approaches to quantify cellular acyl-CoA concentrations in normal and ischemic rat liver, using HPLC and LC-MS/MS for multi-acyl-CoA analysis, as well as NMR, fluorimetric and spectrophotometric techniques for the quantification of acetyl-CoAs. In particular,
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Brejchova, J., K. Brejchova, and O. Kuda. "Metabolic Pathways of Acylcarnitine Synthesis." Physiological Research, Suppl 1 (August 31, 2024): S153—S163. http://dx.doi.org/10.33549/physiolres.935261.

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Acylcarnitines are important markers in metabolic studies of many diseases, including metabolic, cardiovascular, and neurological disorders. We reviewed analytical methods for analyzing acylcarnitines with respect to the available molecular structural information, the technical limitations of legacy methods, and the potential of new mass spectrometry-based techniques to provide new information on metabolite structure. We summarized the nomenclature of acylcarnitines based on historical common names and common abbreviations, and we propose the use of systematic abbreviations derived from the sh
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Han, Lijuan, Ling Zhao, Yong Zhou, et al. "Altered metabolome and microbiome features provide clues in understanding irritable bowel syndrome and depression comorbidity." ISME Journal 16, no. 4 (2021): 983–96. http://dx.doi.org/10.1038/s41396-021-01123-5.

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AbstractIrritable bowel syndrome (IBS) is one of the functional gastrointestinal disorders characterized by chronic and/or recurrent symptoms of abdominal pain and irregular defecation. Changed gut microbiota has been proposed to mediate IBS; however, contradictory results exist, and IBS-specific microbiota, metabolites, and their interactions remain poorly understood. To address this issue, we performed metabolomic and metagenomic profiling of stool and serum samples based on discovery (n = 330) and validation (n = 101) cohorts. Fecal metagenomic data showed moderate dysbiosis compared with o
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IGAL, R. Ariel, Ping WANG, and Rosalind A. COLEMAN. "Triacsin C blocks de novo synthesis of glycerolipids and cholesterol esters but not recycling of fatty acid into phospholipid: evidence for functionally separate pools of acyl-CoA." Biochemical Journal 324, no. 2 (1997): 529–34. http://dx.doi.org/10.1042/bj3240529.

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The trafficking of acyl-CoAs within cells is poorly understood. In order to determine whether newly synthesized acyl-CoAs are equally available for the synthesis of all glycerolipids and cholesterol esters, we incubated human fibroblasts with [14C]oleate, [3H]arachidonate or [3H]glycerol in the presence or absence of triacsin C, a fungal metabolite that is a competitive inhibitor of acyl-CoA synthetase. Triacsin C inhibited de novo synthesis from glycerol of triacylglycerol, diacylglycerol and cholesterol esters by more than 93%, and the synthesis of phospholipid by 83%. However, the incorpora
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Pons, Roser, and Darryl C. De Vivo. "Primary and Secondary Carnitine Deficiency Syndromes." Journal of Child Neurology 10, no. 2_suppl (1995): 2S8–2S24. http://dx.doi.org/10.1177/0883073895010002s03.

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The objective of this article is to review primary and secondary causes of carnitine deficiency, emphasizing recent advances in our knowledge of fatty acid oxidation. It is now understood that the cellular metabolism of fatty acids requires the cytosolic carnitine cycle and the mitochondrial β-oxidation cycle. Carnitine is central to the translocation of the long chain acyl-CoAs across the inner mitochondrial membrane. The mitochondrial β-oxidation cycle is composed of a newly described membrane-bound system and the classic matrix compartment system. Very long chain acyl-CoA dehydrogenase and
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Yu, Wenfeng, Xiquan Liang, Regina E. Ensenauer, Jerry Vockley, Lawrence Sweetman та Horst Schulz. "Leaky β-Oxidation of atrans-Fatty Acid". Journal of Biological Chemistry 279, № 50 (2004): 52160–67. http://dx.doi.org/10.1074/jbc.m409640200.

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The degradation of elaidic acid (9-trans-octadecenoic acid), oleic acid, and stearic acid by rat mitochondria was studied to determine whether the presence of atransdouble bond in place of acisdouble bond or no double bond affects β-oxidation. Rat mitochondria from liver or heart effectively degraded the coenzyme A derivatives of all three fatty acids. However, with elaidoyl-CoA as a substrate, a major metabolite accumulated in the mitochondrial matrix. This metabolite was isolated and identified as 5-trans-tetradecenoyl-CoA. In contrast, little or none of the corresponding metabolites were de
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Varner, Erika L., Sophie Trefely, David Bartee, et al. "Quantification of lactoyl-CoA (lactyl-CoA) by liquid chromatography mass spectrometry in mammalian cells and tissues." Open Biology 10, no. 9 (2020): 200187. http://dx.doi.org/10.1098/rsob.200187.

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Lysine lactoylation is a recently described protein post-translational modification (PTM). However, the biochemical pathways responsible for this acylation remain unclear. Two metabolite-dependent mechanisms have been proposed: enzymatic histone lysine lactoylation derived from lactoyl-coenzyme A (lactoyl-CoA, also termed lactyl-CoA), and non-enzymatic lysine lactoylation resulting from acyl-transfer via lactoyl-glutathione. While the former has precedent in the form of enzyme-catalysed lysine acylation, the lactoyl-CoA metabolite has not been previously quantified in mammalian systems. Here,
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Xia, Chuanwu, Zhuji Fu, Kevin P. Battaile та Jung-Ja P. Kim. "Crystal structure of human mitochondrial trifunctional protein, a fatty acid β-oxidation metabolon". Proceedings of the National Academy of Sciences 116, № 13 (2019): 6069–74. http://dx.doi.org/10.1073/pnas.1816317116.

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Membrane-bound mitochondrial trifunctional protein (TFP) catalyzes β-oxidation of long chain fatty acyl-CoAs, employing 2-enoyl-CoA hydratase (ECH), 3-hydroxyl-CoA dehydrogenase (HAD), and 3-ketothiolase (KT) activities consecutively. Inherited deficiency of TFP is a recessive genetic disease, manifesting in hypoketotic hypoglycemia, cardiomyopathy, and sudden death. We have determined the crystal structure of human TFP at 3.6-Å resolution. The biological unit of the protein is α2β2. The overall structure of the heterotetramer is the same as that observed by cryo-EM methods. The two β-subunits
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Lone, Museer A., Andreas J. Hülsmeier, Essa M. Saied, et al. "Subunit composition of the mammalian serine-palmitoyltransferase defines the spectrum of straight and methyl-branched long-chain bases." Proceedings of the National Academy of Sciences 117, no. 27 (2020): 15591–98. http://dx.doi.org/10.1073/pnas.2002391117.

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Sphingolipids (SLs) are chemically diverse lipids that have important structural and signaling functions within mammalian cells. SLs are commonly defined by the presence of a long-chain base (LCB) that is normally formed by the conjugation ofl-serine and palmitoyl-CoA. This pyridoxal 5-phosphate (PLP)-dependent reaction is mediated by the enzyme serine-palmitoyltransferase (SPT). However, SPT can also metabolize other acyl-CoAs, in the range of C14to C18, forming a variety of LCBs that differ by structure and function. Mammalian SPT consists of three core subunits: SPTLC1, SPTLC2, and SPTLC3.
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Carrer, Alessandro, Joshua L. D. Parris, Sophie Trefely, et al. "Impact of a High-fat Diet on Tissue Acyl-CoA and Histone Acetylation Levels." Journal of Biological Chemistry 292, no. 8 (2017): 3312–22. http://dx.doi.org/10.1074/jbc.m116.750620.

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Cellular metabolism dynamically regulates the epigenome via availability of the metabolite substrates of chromatin-modifying enzymes. The impact of diet on the metabolism-epigenome axis is poorly understood but could alter gene expression and influence metabolic health. ATP citrate-lyase produces acetyl-CoA in the nucleus and cytosol and regulates histone acetylation levels in many cell types. Consumption of a high-fat diet (HFD) results in suppression of ATP citrate-lyase levels in tissues such as adipose and liver, but the impact of diet on acetyl-CoA and histone acetylation in these tissues
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Dissertations / Theses on the topic "Acyl-CoAs metabolome"

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Zeaiter, Nour. "Les effets des changements métaboliques sur le métabolome des acyl-CoAs et l'acylation d'histone épigénétique." Electronic Thesis or Diss., Université Grenoble Alpes, 2024. http://www.theses.fr/2024GRALV013.

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Des preuves de plus en plus nombreuses suggèrent que le métabolisme peut affecter les modifications épigénétiques post-traductionnelles des histones, établissant ainsi un lien potentiel entre la disponibilité des nutriments ou les conditions environnementales, d'une part, et l'expression des gènes et la physiopathologie humaine, d'autre part. Cependant, on manque encore d'informations plus détaillées sur cette relation. Nous étudions ici le rôle des acyl-CoAs à chaîne courte (sc), générés dans diverses voies métaboliques, en tant que substrats pour l'acylation des histones. L'analyse des acyl-
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Knoll, Anja. "Etude du métabolisme des acides gras à très longues chaînes dans le cerveau du rat : activités enzymatiques d'élongation des acyl-CoAs, expression des gènes de la béta-oxydation peroxysomale." Bordeaux 2, 2000. http://www.theses.fr/2000BOR28756.

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