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Coenzyme A (CoA, SHCoA, CoASH) is a coenzyme, notable for its role in the synthesis and oxidation of fatty acids, and the oxidation of pyruvate in the citric acid cycle.All genomes sequenced to date encode enzymes that use coenzyme A as a substrate, and around 4% of cellular enzymes use it (or a thioester) as a substrate.
Acetyl-CoA is a metabolic intermediate that is involved in many metabolic pathways in an organism. It is produced during the breakdown of glucose , fatty acids , and amino acids , and is used in the synthesis of many other biomolecules , including cholesterol , fatty acids , and ketone bodies .
Coenzyme A transferases (CoA-transferases) are transferase enzymes that catalyze the transfer of a coenzyme A group from an acyl-CoA donor to a carboxylic acid acceptor. [ 1 ] [ 2 ] Among other roles, they are responsible for transfer of CoA groups during fermentation and metabolism of ketone bodies .
General chemical structure of an acyl-CoA, where R is a carboxylic acid side chain. Acyl-CoA is a group of CoA-based coenzymes that metabolize carboxylic acids. Fatty acyl-CoA's are susceptible to beta oxidation, forming, ultimately, acetyl-CoA. The acetyl-CoA enters the citric acid cycle, eventually forming several equivalents of ATP. In this ...
The Wood–Ljungdahl pathway is a set of biochemical reactions used by some bacteria. It is also known as the reductive acetyl-coenzyme A pathway. [1] This pathway enables these organisms to use hydrogen (H 2) as an electron donor, and carbon dioxide (CO 2) as an electron acceptor and as a building block to generate acetate for biosynthesis.
β-Hydroxy β-methylglutaryl-CoA (HMG-CoA), also known as 3-hydroxy-3-methylglutaryl coenzyme A, is an intermediate in the mevalonate and ketogenesis pathways. It is formed from acetyl CoA and acetoacetyl CoA by HMG-CoA synthase. The research of Minor J. Coon and Bimal Kumar Bachhawat in the 1950s at University of Illinois led to its discovery.
The proposed metabolic pathway may explain the Warburg effect – that cancer cells produce energy through a suboptimal pathway – and hypoxia in cancer. The energy efficiency of this pathway is 3.76 times less than the normal β-oxidation Krebs cycle pathway, only producing 26 moles instead of 98 moles of ATP from 1 mole of palmitate. [13]
Also, copper ions deactivate acetyl Co-A synthetase by occupying the proximal site of the A-cluster active site, which prevents the enzyme from accepting a methyl group to participate in the Wood-Ljungdahl Pathway. [4] The presence of all the reactants in the proper concentration is also needed for proper functioning as in all enzymes.