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  2. Cofactor (biochemistry) - Wikipedia

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

    Evolution of enzymes without coenzymes. If enzymes require a co-enzyme, how does the coenzyme evolve? If enzymes require a co-enzyme, how does the coenzyme evolve? 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.

  3. 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.

  4. 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.

  5. Cofactor engineering - Wikipedia

    en.wikipedia.org/wiki/Cofactor_Engineering

    The coenzymes bind to the active site of an enzyme to promote catalysis. By engineering cofactors and coenzymes, a naturally occurring metabolic reaction can be manipulated to optimize the output of a metabolic network. [2] [3] [4] Common cofactor NADH, the first discovered.

  6. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Enzyme denaturation is normally linked to temperatures above a species' normal level; as a result, enzymes from bacteria living in volcanic environments such as hot springs are prized by industrial users for their ability to function at high temperatures, allowing enzyme-catalysed reactions to be operated at a very high rate.

  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. Transamination - Wikipedia

    en.wikipedia.org/wiki/Transamination

    The amino group is accommodated by conversion of this coenzyme to pyridoxamine-5'-phosphate (PMP). PLP is covalently attached to the enzyme via a Schiff Base linkage formed by the condensation of its aldehyde group with the ε-amino group of an enzymatic Lys residue. The Schiff base, which is conjugated to the enzyme's pyridinium ring, is the ...

  9. Acetyl-CoA synthetase - Wikipedia

    en.wikipedia.org/wiki/Acetyl-CoA_synthetase

    The role of the ACS enzyme is to combine acetate and Coenzyme A to form acetyl-CoA, however its significance is much larger. The most well known function of the product from this enzymatic reaction is the use of acetyl-CoA in the role of the TCA cycle as well as in the production of fatty acid.