enow.com Web Search

Search results

  1. Results from the WOW.Com Content Network
  2. Cofactor (biochemistry) - Wikipedia

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

    The most likely scenario is that enzymes can function initially without their coenzymes and later recruit the coenzyme, even if the catalyzed reaction may not be as efficient or as fast. Examples are Alcohol Dehydrogenase (coenzyme: NAD⁺), [73] Lactate Dehydrogenase (NAD⁺), [74] Glutathione Reductase . [75]

  3. Category:Coenzymes - Wikipedia

    en.wikipedia.org/wiki/Category:Coenzymes

    This page was last edited on 23 September 2022, at 20:28 (UTC).; Text is available under the Creative Commons Attribution-ShareAlike 4.0 License; additional terms may apply.

  4. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    For example, about 1000 enzymes are known to use the coenzyme NADH. [63] 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. 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 ...

  6. Oxidoreductase - Wikipedia

    en.wikipedia.org/wiki/Oxidoreductase

    For example, an enzyme that catalyzed this reaction would be an oxidoreductase: A – + B → A + B – In this example, A is the reductant (electron donor) and B is the oxidant (electron acceptor). In biochemical reactions, the redox reactions are sometimes more difficult to see, such as this reaction from glycolysis:

  7. 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.

  8. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    For example, the heme in cytochrome C is bound to the protein through thioester bond. 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 ...

  9. 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.