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  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. 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. 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.

  6. Nicotinamide adenine dinucleotide - Wikipedia

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

    This difference in the ultraviolet absorption spectra between the oxidized and reduced forms of the coenzymes at higher wavelengths makes it simple to measure the conversion of one to another in enzyme assays – by measuring the amount of UV absorption at 340 nm using a spectrophotometer. [10] NAD + and NADH also differ in their fluorescence.

  7. 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 ...

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

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

    Enzymes are critical to our survival, but human enzymes have different properties than enzymes found in the things we eat, including all plant-based and animal foods. And while enzymes are ...

  9. Flavin adenine dinucleotide - Wikipedia

    en.wikipedia.org/wiki/Flavin_adenine_dinucleotide

    Riboflavin is formed by a carbon-nitrogen (C-N) bond between the isoalloxazine and the ribitol. The phosphate group is then bound to the terminal ribose carbon, forming a FMN. Because the bond between the isoalloxazine and the ribitol is not considered to be a glycosidic bond, the flavin mononucleotide is not truly a nucleotide. [7]

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