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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 ...
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 ...
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
Coenzymes (1 C, 35 P) Pages in category "Cofactors" The following 32 pages are in this category, out of 32 total. This list may not reflect recent changes. ...
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.
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.
Enzymes often also incorporate non-protein components, such as metal ions or specialized organic molecules known as cofactor (e.g. adenosine triphosphate). Many cofactors are vitamins, and their role as vitamins is directly linked to their use in the catalysis of biological process within metabolism.
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. One example of the coenzyme is Flavin. It contains a distinct conjugated isoalloxazine ring system.