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  2. Cofactor (biochemistry) - Wikipedia

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

    Cofactors typically differ from ligands in that they often derive their function by remaining bound. Cofactors can be classified into two types: inorganic ions and complex organic molecules called coenzymes. [1] Coenzymes are mostly derived from vitamins and other organic essential nutrients in small amounts. (Some scientists limit the use of ...

  3. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Coenzymes are usually continuously regenerated and their concentrations maintained at a steady level inside the cell. For example, NADPH is regenerated through the pentose phosphate pathway and S-adenosylmethionine by methionine adenosyltransferase. This continuous regeneration means that small amounts of coenzymes can be used very intensively.

  4. 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.

  5. Nicotinamide adenine dinucleotide - Wikipedia

    en.wikipedia.org/wiki/Nicotinamide_adenine_di...

    In 1936, the German scientist Otto Heinrich Warburg showed the function of the nucleotide coenzyme in hydride transfer and identified the nicotinamide portion as the site of redox reactions. [ 114 ] Vitamin precursors of NAD + were first identified in 1938, when Conrad Elvehjem showed that liver has an "anti-black tongue" activity in the form ...

  6. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    In biology and biochemistry, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction. The active site consists of amino acid residues that form temporary bonds with the substrate, the binding site , and residues that catalyse a reaction of that substrate, the catalytic site .

  7. Flavin adenine dinucleotide - Wikipedia

    en.wikipedia.org/wiki/Flavin_adenine_dinucleotide

    The 1930s launched the field of coenzyme research with the publication of many flavin and nicotinamide derivative structures and their obligate roles in redox catalysis. German scientists Otto Warburg and Walter Christian discovered a yeast derived yellow protein required for cellular respiration in 1932.

  8. Coenzyme Q10 - Wikipedia

    en.wikipedia.org/wiki/Coenzyme_Q10

    Coenzymes Q is a coenzyme family that is ubiquitous in animals and many Pseudomonadota, [10] a group of gram-negative bacteria. The fact that the coenzyme is ubiquitous gives the origin of its other name, ubiquinone. [1] [2] [11] In humans, the most common form of coenzymes Q is coenzyme Q 10, also called CoQ 10 (/ ˌ k oʊ k j uː ˈ t ɛ n ...

  9. Pyridoxal phosphate - Wikipedia

    en.wikipedia.org/wiki/Pyridoxal_phosphate

    Pyridoxal phosphate (PLP, pyridoxal 5'-phosphate, P5P), the active form of vitamin B 6, is a coenzyme in a variety of enzymatic reactions. The International Union of Biochemistry and Molecular Biology has catalogued more than 140 PLP-dependent activities, corresponding to ~4% of all classified activities. [5]