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  2. Coenzyme A - Wikipedia

    en.wikipedia.org/wiki/Coenzyme_A

    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.

  3. Acetyl-CoA - Wikipedia

    en.wikipedia.org/wiki/Acetyl-CoA

    Acetyl-CoA (acetyl coenzyme A) is a molecule that participates in many biochemical reactions in protein, carbohydrate and lipid metabolism. [2] Its main function is to deliver the acetyl group to the citric acid cycle (Krebs cycle) to be oxidized for energy production.

  4. Coenzyme A transferases - Wikipedia

    en.wikipedia.org/wiki/Coenzyme_A_transferases

    These reactions have different functions in cells. The reaction involving acetyl-CoA and butyrate (EC 2.8.3.8), for example, forms butyrate during fermentation. [3] The reaction involving acetyl-CoA and succinate (EC 2.8.3.18) is part of a modified TCA cycle [4] or forms acetate during fermentation. [5]

  5. Thioester - Wikipedia

    en.wikipedia.org/wiki/Thioester

    Structure of acetyl coenzyme A, a thioester that is a key intermediate in the biosynthesis of many biomolecules. Thioesters are common intermediates in many biosynthetic reactions, including the formation and degradation of fatty acids and mevalonate , precursor to steroids.

  6. Transferase - Wikipedia

    en.wikipedia.org/wiki/Transferase

    Transferases are involved in myriad reactions in the cell. Three examples of these reactions are the activity of coenzyme A (CoA) transferase, which transfers thiol esters, [3] the action of N-acetyltransferase, which is part of the pathway that metabolizes tryptophan, [4] and the regulation of pyruvate dehydrogenase (PDH), which converts ...

  7. Acyl-CoA dehydrogenase - Wikipedia

    en.wikipedia.org/wiki/Acyl-CoA_dehydrogenase

    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.

  8. Fatty acyl-CoA esters - Wikipedia

    en.wikipedia.org/wiki/Fatty_acyl-CoA_esters

    To participate in specific metabolic processes, fatty acids must first be activated by being joined in thioester linkage (R-CO-SCoA) to the -SH group of coenzyme A, where R is a fatty carbon chain. The thioester bond is a high energy bond. [1] The activation reaction normally occurs in the endoplasmic reticulum or the outer mitochondrial membrane.

  9. Succinyl coenzyme A synthetase - Wikipedia

    en.wikipedia.org/wiki/Succinyl_coenzyme_A_synthetase

    The reaction has a biochemical standard state free energy change of -3.4 kJ/mol. [4] The reaction takes place by a three-step mechanism [3] which is depicted in the image below. The first step involves displacement of CoA from succinyl CoA by a nucleophilic inorganic phosphate molecule to form succinyl phosphate.

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