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  2. Cofactor (biochemistry) - Wikipedia

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

    Cofactors can be divided into two major groups: organic cofactors, such as flavin or heme; and inorganic cofactors, such as the metal ions Mg 2+, Cu +, Mn 2+ and iron–sulfur clusters. Organic cofactors are sometimes further divided into coenzymes and prosthetic groups. The term coenzyme refers specifically to enzymes and, as such, to the ...

  3. Flavin adenine dinucleotide - Wikipedia

    en.wikipedia.org/wiki/Flavin_adenine_dinucleotide

    Theorell confirmed the pigment to be riboflavin's phosphate ester, flavin mononucleotide (FMN) in 1937, which was the first direct evidence for enzyme cofactors. [5] Warburg and Christian then found FAD to be a cofactor of D-amino acid oxidase through similar experiments in 1938. [6]

  4. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    [6]: 69 Coenzyme is a broad concept which includes metal ions, various vitamins and ATP. If an enzyme needs coenzyme to work itself, it is called an apoenzyme. In fact, it alone cannot catalyze reactions properly. Only when its cofactor comes in and binds to the active site to form holoenzyme does it work properly.

  5. Prosthetic group - Wikipedia

    en.wikipedia.org/wiki/Prosthetic_group

    A prosthetic group is the non-amino acid component that is part of the structure of the heteroproteins or conjugated proteins, being tightly linked to the apoprotein.. Not to be confused with the cosubstrate that binds to the enzyme apoenzyme (either a holoprotein or heteroprotein) by non-covalent binding a non-protein (non-amino acid)

  6. 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.

  7. Metalloprotein - Wikipedia

    en.wikipedia.org/wiki/Metalloprotein

    The differences between those cytochromes lies in the different side-chains. For instance cytochrome a has a heme a prosthetic group and cytochrome b has a heme b prosthetic group. These differences result in different Fe 2+ /Fe 3+ redox potentials such that various cytochromes are involved in the mitochondrial electron transport chain.

  8. Coenzyme Q10 - Wikipedia

    en.wikipedia.org/wiki/Coenzyme_Q10

    Coenzyme Q 10 (CoQ 10 / ˌ k oʊ k j uː ˈ t ɛ n /), also known as ubiquinone, is a naturally occurring biochemical cofactor (coenzyme) and an antioxidant produced by the human body. [ 1 ] [ 2 ] [ 3 ] It can also be obtained from dietary sources, such as meat, fish, seed oils, vegetables, and dietary supplements .

  9. Thiamine pyrophosphate - Wikipedia

    en.wikipedia.org/wiki/Thiamine_pyrophosphate

    Thiamine pyrophosphate is a cofactor that is present in all living systems, in which it catalyzes several biochemical reactions. Thiamine pyrophosphate is synthesized in the cytosol and is required in the cytosol for the activity of transketolase and in the mitochondria for the activity of pyruvate-, oxoglutarate- and branched chain keto acid ...

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