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  2. Cofactor (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Cofactor_(biochemistry)

    Other cofactors were identified throughout the early 20th century, with ATP being isolated in 1929 by Karl Lohmann, [78] and coenzyme A being discovered in 1945 by Fritz Albert Lipmann. [79] The functions of these molecules were at first mysterious, but, in 1936, Otto Heinrich Warburg identified the function of NAD + in hydride transfer. [80]

  3. Flavin adenine dinucleotide - Wikipedia

    en.wikipedia.org/wiki/Flavin_adenine_dinucleotide

    In biochemistry, flavin adenine dinucleotide (FAD) is a redox-active coenzyme associated with various proteins, which is involved with several enzymatic reactions in metabolism. A flavoprotein is a protein that contains a flavin group, which may be in the form of FAD or flavin mononucleotide (FMN).

  4. Vitamin B12 - Wikipedia

    en.wikipedia.org/wiki/Vitamin_B12

    "B12" and "Cbl" redirect here. For other uses of B12, see B12 (disambiguation). For the musical group, see Carbon Based Lifeforms. Pharmaceutical compound Vitamin B12 General skeletal formula of cobalamins Stick model of cyanocobalamin (R = CN) based on the crystal structure Clinical data Other names Vitamin B12, vitamin B-12, cobalamin AHFS / Drugs.com Monograph MedlinePlus a605007 License ...

  5. Thiamine pyrophosphate - Wikipedia

    en.wikipedia.org/wiki/Thiamine_pyrophosphate

    In several reactions, including that of pyruvate dehydrogenase, alpha-ketoglutarate dehydrogenase, and transketolase, TPP catalyses the reversible decarboxylation reaction (aka cleavage of a substrate compound at a carbon-carbon bond connecting a carbonyl group to an adjacent reactive group—usually a carboxylic acid or an alcohol).

  6. 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.

  7. Riboflavin - Wikipedia

    en.wikipedia.org/wiki/Riboflavin

    The flavin coenzymes support the function of roughly 70-80 flavoenzymes in humans (and hundreds more across all organisms, including those encoded by archeal, bacterial and fungal genomes) that are responsible for one- or two-electron redox reactions which capitalize on the ability of flavins to be converted between oxidized, half-reduced and ...

  8. Dihydrolipoyl transacetylase - Wikipedia

    en.wikipedia.org/wiki/Dihydrolipoyl_transacetylase

    Pyruvate dehydrogenase (EC 1.2.4.1) is responsible for the oxidation of pyruvate, dihydrolipoyl transacetylase (this enzyme; EC 2.3.1.12) transfers the acetyl group to coenzyme A (CoA), and dihydrolipoyl dehydrogenase (EC 1.8.1.4) regenerates the lipoamide. Because dihydrolipoyl transacetylase is the second of the three enzyme components ...

  9. Pantothenic acid - Wikipedia

    en.wikipedia.org/wiki/Pantothenic_acid

    Pantothenic acid (vitamin B 5) is a B vitamin and an essential nutrient. [6] All animals need pantothenic acid in order to synthesize coenzyme A (CoA), which is essential for cellular energy production and for the synthesis and degradation of proteins, carbohydrates, and fats.