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  2. Cofactor (biochemistry) - Wikipedia

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

    The succinate dehydrogenase complex showing several cofactors, including flavin, iron–sulfur centers, and heme.. A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst (a catalyst is a substance that increases the rate of a chemical reaction).

  3. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    In some occasions, coenzymes can leave enzymes after the reaction is finished. Otherwise, they permanently bind to the enzyme. [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.

  4. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    For example, about 1000 enzymes are known to use the coenzyme NADH. [62] 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 ...

  5. What are enzymes, and what do they have to do with ... - AOL

    www.aol.com/enzymes-digestion-090536230.html

    Enzymes also help with nerve function, respiration, digestion, muscle growth and much more. "The list is very long," says Farina. "The list is very long," says Farina.

  6. 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.

  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. Dehydrogenase - Wikipedia

    en.wikipedia.org/wiki/Dehydrogenase

    Oxidoreductases, enzymes that catalyze oxidation-reduction reactions, constitute Class EC 1 of the IUBMB classification of enzyme-catalyzed reactions. [2] Any of these may be called dehydrogenases, especially those in which NAD + is the electron acceptor (oxidant), but reductase is also used when the physiological emphasis on reduction of the substrate, and oxidase is used only when O 2 is the ...

  9. Nicotinamide adenine dinucleotide phosphate - Wikipedia

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

    Nicotinamide adenine dinucleotide phosphate, abbreviated NADP [1] [2] or, in older notation, TPN (triphosphopyridine nucleotide), is a cofactor used in anabolic reactions, such as the Calvin cycle and lipid and nucleic acid syntheses, which require NADPH as a reducing agent ('hydrogen source').