enow.com Web Search

Search results

  1. Results from the WOW.Com Content Network
  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. 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. 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.

  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. Acyl-CoA dehydrogenase - Wikipedia

    en.wikipedia.org/wiki/Acyl-CoA_dehydrogenase

    Acyl-CoA dehydrogenases (ACADs) are a class of enzymes that function to catalyze the initial step in each cycle of fatty acid β-oxidation in the mitochondria of cells.Their action results in the introduction of a trans double-bond between C2 (α) and C3 (β) of the acyl-CoA thioester substrate. [1]

  7. Pyruvate dehydrogenase complex - Wikipedia

    en.wikipedia.org/wiki/Pyruvate_dehydrogenase_complex

    Pymol-generated image of E1 subunit of pyruvate dehydrogenase complex in E. Coli. The E1 subunit, called the pyruvate dehydrogenase subunit, is either a homodimer (comprising two “α” chains, e.g. in Escherichia coli) or a heterotetramer of two different chains (two “α” and two “β” chains).

  8. Biosynthesis - Wikipedia

    en.wikipedia.org/wiki/Biosynthesis

    Uridine monophosphate biosynthesis involves an enzyme that is located in the mitochondrial inner membrane and multifunctional enzymes that are located in the cytosol. [ 19 ] The first step involves the enzyme carbamoyl phosphate synthase combining glutamine with CO 2 in an ATP dependent reaction to form carbamoyl phosphate .

  9. Dihydrolipoyl transacetylase - Wikipedia

    en.wikipedia.org/wiki/Dihydrolipoyl_transacetylase

    There are three different enzyme components in the pyruvate dehydrogenase complex. Pyruvate dehydrogenase (EC 1.2.4.1) is responsible for the oxidation of pyruvate, dihydrolipoyl transacetylase (this enzyme; EC 2.3.1.12) transfers the acetyl group to coenzyme A (CoA), and dihydrolipoyl dehydrogenase (EC 1.8.1.4) regenerates the lipoamide ...