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For example, ligands such as hormones that bind to and activate receptor proteins are termed cofactors or coactivators, whereas molecules that inhibit receptor proteins are termed corepressors. One such example is the G protein-coupled receptor family of receptors, which are frequently found in sensory neurons.
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 ...
Prosthetic groups are a subset of cofactors. Loosely bound metal ions and coenzymes are still cofactors, but are generally not called prosthetic groups. [2] [3] [4] In enzymes, prosthetic groups are involved in the catalytic mechanism and required for activity. Other prosthetic groups have structural properties.
The iron–molybdenum cofactor of nitrogenases contains an Fe 6 C unit and is an example of an interstitial carbide found in biology. [9] [10] The first example of a naturally-occurring arylmetal species, a pincer complex containing a nickel–aryl bond, has been reported to form the active site of lactate racemase. [11]
The structure of hemoglobin.The heme cofactor, containing the metal iron, shown in green.. Metalloprotein is a generic term for a protein that contains a metal ion cofactor. [1] [2] A large proportion of all proteins are part of this category.
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An example of an enzyme that contains a cofactor is carbonic anhydrase, which has a zinc cofactor bound as part of its active site. [4] These tightly bound ions or molecules are usually found in the active site and are involved in catalysis. [5]: 8.1.1 For example, flavin and heme cofactors are often involved in redox reactions. [5]: 17
Cofactors can be either inorganic (e.g., metal ions and iron-sulfur clusters) or organic compounds, (e.g., [Flavin group|flavin] and heme). Organic cofactors can be either prosthetic groups, which are tightly bound to an enzyme, or coenzymes, which are released from the enzyme's active site during the reaction.