Search results
Results From The WOW.Com Content Network
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 .
The Wood–Ljungdahl pathway is a set of biochemical reactions used by some bacteria. It is also known as the reductive acetyl-coenzyme A ( acetyl-CoA ) 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 ...
In enzymology, an acetate CoA-transferase (EC 2.8.3.8) is an enzyme that catalyzes the chemical reaction. acyl-CoA + acetate a fatty acid anion + acetyl-CoA. Thus, the two substrates of this enzyme are acyl-CoA and acetate, whereas its two products are long-chain carboxylate anion and acetyl-CoA.
The systematic name of this enzyme class is acetyl-CoA:acetoacetyl-CoA C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming).Other names in common use include (S)-3-hydroxy-3-methylglutaryl-CoA acetoacetyl-CoA-lyase, (CoA-acetylating), 3-hydroxy-3-methylglutaryl CoA synthetase, 3-hydroxy-3-methylglutaryl coenzyme A synthase, 3-hydroxy-3-methylglutaryl coenzyme A synthetase, 3 ...
The medium chain acyl-CoA dehydrogenase (MCAD) is the best known structure of all ACADs, and is the most commonly deficient enzyme within the class that leads to metabolic disorders in animals. [1] This protein is a homotetramer with each subunit containing roughly 400 amino acids and one equivalent of FAD per monomer.
In enzymology, a CoA-glutathione reductase (EC 1.8.1.10) is an enzyme that catalyzes the chemical reaction. CoA + glutathione + NADP + CoA-glutathione + NADPH + H +. The 3 substrates of this enzyme are CoA, glutathione, and NADP +, whereas its 3 products are CoA-glutathione, NADPH, and H +.