Lower-intensity aerobic endurance sports
Nick Draper, Helen Marshall in Exercise Physiology, 2014
The cycle of reactions in β oxidation continues until the acyl CoA molecule has been fully oxidised to acetyl CoA molecules, each containing two carbons. In the case of palmitic acid, seven cycles of β oxidation would be required for the complete catabolism of the palmitic acyl CoA to create eight acetyl CoA molecules. In the first reaction, catalysed by acyl CoA dehydrogenase, two hydrogen atoms are removed and transferred to the electron transport chain by the co-enzyme carrier flavin adenine dinucleotide (FAD) (see Figure 12.7). In this reaction, therefore, FAD, a derivative of the B vitamin riboflavin and closely related to NAD+, is reduced to FADH2. The reduction of FAD is shown in Figure 12.7, forming FADH2 by the addition of two hydrogen atoms.
Organic acid disorders and disorders of fatty acid oxidation
Steve Hannigan in Inherited Metabolic Diseases: A Guide to 100 Conditions, 2018
Multiple acyl CoA dehydrogenase deiciency is a rare disorder that belongs to a group of conditions known as the organic acidaemias. It can be caused by a deiciency in either the electron transfer flavoprotein (ETF) enzyme or the ETF-ubiquinone oxidoreductase (ETF-QO) enzyme. This results in the accumulation of organic acids in the blood and urine. There are two forms of multiple acyl CoA dehydrogenase deiciency: a neonatal form in which the enzyme is completely absent, and that is often fatal during the newborn perioda late-onset form which is less severe and that can present at any age.
Introduction to disorders of fatty acid oxidation
William L. Nyhan, Georg F. Hoffmann, Aida I. Al-Aqeel, Bruce A. Barshop in Atlas of Inherited Metabolic Diseases, 2020
Specific acylCoA dehydrogenases (ACADs) with overlapping specificities for chain length include: short-chain acyl CoA dehydrogenase (SCAD) (Chapter 42), medium-chain acyl CoA dehydrogenase (MCAD) (Chapter 39), and very long-chain acyl CoA dehydrogenase (VLCAD) (Chapter 40). In addition, a tri-functional enzyme catalyzes 3-hydroxyacyl dehydrogenation, 2-enoyl-CoA hydration, and 3-oxoacylCoA thiolysis [7]. Long-chain hydroxyacyl CoA dehydrogenase (LCHAD) is now known to be one of these three enzymatic steps of the tri-functional protein (Chapter 41).
Anti-biofilm effect of a butenolide/polymer coating and metatranscriptomic analyses
Published in Biofouling, 2018
Wei Ding, Chunfeng Ma, Weipeng Zhang, Hoyin Chiang, Chunkit Tam, Ying Xu, Guangzhao Zhang, Pei-Yuan Qian
Firstly, comparing the DCOIT-treated biofilms and the control biofilms, genes involved in energy production, including enoyl-coenzyme A hydratase/carnithine racemase (COG1024) and acyl-coenzyme A dehydrogenases (COG1960) had lower abundance in the butenolide treated biofilms, suggesting inhibition of these genes by butenolide. In particular, acyl-coenzyme A dehydrogenase is an enzyme which generates energy by catalyzing the β-oxidation of long chain fatty acids (McAndrew et al. 2008). It has been demonstrated that butenolide binds to very long chain acyl-coenzyme A dehydrogenase, actin, and glutathione S-transferases in the barnacle Balanus (=Amphibalanus) amphitrite, and based on the result of in vitro molecular assay using purified proteins and compounds, butenolide binds to the succinyl-coenzyme A synthetase β subunit in the marine bacterium Vibrio sp. UST020129-010 to inhibit its growth (Zhang et al. 2012). These results imply that butenolide inhibits marine biofilm formation by altering the primary metabolism in microbes. It is worthwhile mentioning that some biocides also affect energy metabolism in bacteria. For example, tetrakis (hydroxymethyl) phosphonium sulfate has been shown to affect energy metabolic pathways in sulfate-reducing bacteria (Lee et al. 2010).
Administration timing and duration-dependent effects of sesamin isomers on lipid metabolism in rats
Published in Chronobiology International, 2020
Norifumi Tateishi, Satoshi Morita, Izumi Yamazaki, Hitoshi Okumura, Masaru Kominami, Sota Akazawa, Ayuta Funaki, Namino Tomimori, Tomohiro Rogi, Hiroshi Shibata, Shigenobu Shibata
With respect to triglyceride, SE tended to decrease liver triglycerides after administration at ZT23 (Figure 1c) or had no effect on serum triglycerides (Figure 1d). On the other hand, genes related to triglyceride metabolism in the liver were markedly affected by SE treatment. Gene expression of acyl-CoA dehydrogenase medium chain (Acadm, Figure 2d) and acyl-CoA oxidase 1 (Acox1, Figure 2e), which are members of enzymes involved in fatty acid beta-oxidation, were significantly higher in SE-treated liver when compared with that of CON. Fatty acid synthase (Fasn, Figure 2f), which contributes to fatty acid synthesis, was lower in SE-treated liver as compared with CON. There are no obvious differences between administration timings of SE. Although the influence of SE on the expression of these genes involved in triglyceride metabolism preferred to allow triglyceride parameters to be lower, we did not observe the effect under these test conditions.
A comprehensive proteomics analysis of the response of Pseudomonas aeruginosa to nanoceria cytotoxicity
Published in Nanotoxicology, 2023
Lidija Izrael Živković, Nico Hüttmann, Vanessa Susevski, Ana Medić, Vladimir Beškoski, Maxim V. Berezovski, Zoran Minić, Ljiljana Živković, Ivanka Karadžić
The upregulation of several enzymes involved in lipid catabolism through the β-oxidation of fatty acids were found: acetyl-CoA acetyltransferase, acyl-CoA dehydrogenase, acyl-CoA thiolase, and long-chain-fatty-acid-CoA ligase (Table 1), suggesting increased generation of acetyl-CoA, which enters the citric acid cycle, and NADH and FADH2 that are used for further oxidation and energy production. Interestingly, dihydrolipoyl dehydrogenase, which contains lipoamide as a cofactor, was downregulated, indicating reduced synthesis of lipid structures. Impaired structures and reduced biosynthesis of fatty acids and lipids in association with ROS that cause lipid peroxidation in P. aeruginosa produce a strong effect on maintaining bacterial cell integrity, primarily through the effects on membrane phospholipids, lipidated membrane proteins that are tightly connected to transport machinery, and lipopolysaccharides of the outer membrane, responsible for permeability. Notably, even the intact outer membrane of P. aeruginosa has low permeability to various compounds, not only toxic, but also nutritional substrates (Tamber, Ochs, and Hancock 2006).
Related Knowledge Centers
- Beta Oxidation
- Coenzyme A
- Enzyme
- Fatty Acid
- Flavin Adenine Dinucleotide
- Glutamic Acid
- Thioester
- Mitochondrion
- Cell
- Redox