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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. 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. 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 ...

  5. Pyruvate dehydrogenase complex - Wikipedia

    en.wikipedia.org/wiki/Pyruvate_dehydrogenase_complex

    Pyruvate dehydrogenase deficiency (PDCD) can result from mutations in any of the enzymes or cofactors used to build the complex. Its primary clinical finding is lactic acidosis . [ 18 ] Such PDCD mutations, leading to subsequent deficiencies in NAD and FAD production, hinder oxidative phosphorylation processes that are key in aerobic respiration.

  6. Cofactor engineering - Wikipedia

    en.wikipedia.org/wiki/Cofactor_Engineering

    Cofactors can be both organic and inorganic compounds. Some examples of inorganic cofactors are iron or magnesium, and some examples of organic cofactors include ATP or coenzyme A. Organic cofactors are more specifically known as coenzymes, and many enzymes require the addition of coenzymes to assume normal catalytic function in a metabolic ...

  7. 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.

  8. Oxidoreductase - Wikipedia

    en.wikipedia.org/wiki/Oxidoreductase

    In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule, the reductant, also called the electron donor, to another, the oxidant, also called the electron acceptor.

  9. 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.