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  2. Cofactor (biochemistry) - Wikipedia

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

    Here, cofactors were defined as an additional substance apart from protein and substrate that is required for enzyme activity and a prosthetic group as a substance that undergoes its whole catalytic cycle attached to a single enzyme molecule. However, the author could not arrive at a single all-encompassing definition of a "coenzyme" and ...

  3. Flavin adenine dinucleotide - Wikipedia

    en.wikipedia.org/wiki/Flavin_adenine_dinucleotide

    Theorell confirmed the pigment to be riboflavin's phosphate ester, flavin mononucleotide (FMN) in 1937, which was the first direct evidence for enzyme cofactors. [5] Warburg and Christian then found FAD to be a cofactor of D-amino acid oxidase through similar experiments in 1938. [6]

  4. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Organic cofactors can be either coenzymes, which are released from the enzyme's active site during the reaction, or prosthetic groups, which are tightly bound to an enzyme. Organic prosthetic groups can be covalently bound (e.g., biotin in enzymes such as pyruvate carboxylase ).

  5. Thiamine pyrophosphate - Wikipedia

    en.wikipedia.org/wiki/Thiamine_pyrophosphate

    Thiamine pyrophosphate (TPP or ThPP), or thiamine diphosphate (ThDP), or cocarboxylase [1] is a thiamine (vitamin B 1) derivative which is produced by the enzyme thiamine diphosphokinase. Thiamine pyrophosphate is a cofactor that is present in all living systems, in which it catalyzes several biochemical reactions.

  6. Nitric oxide synthase - Wikipedia

    en.wikipedia.org/wiki/Nitric_oxide_synthase

    Zinc, though not a cofactor, also participates but as a structural element. [4] NOSs are unique in that they use five cofactors and are the only known enzyme that binds flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN), heme , tetrahydrobiopterin (BH 4 ) and calmodulin .

  7. Pyruvate dehydrogenase complex - Wikipedia

    en.wikipedia.org/wiki/Pyruvate_dehydrogenase_complex

    Pyruvate dehydrogenase deficiency (PDCD) can result from mutations in any of the enzymes or cofactors used to build the complex. Its primary clinical finding is lactic acidosis . [ 18 ] Such PDCD mutations, leading to subsequent deficiencies in NAD and FAD production, hinder oxidative phosphorylation processes that are key in aerobic respiration.

  8. Mitochondrial matrix - Wikipedia

    en.wikipedia.org/wiki/Mitochondrial_matrix

    The mitochondrial matrix contains the mitochondrial DNA, ribosomes, soluble enzymes, small organic molecules, nucleotide cofactors, and inorganic ions. [1] The enzymes in the matrix facilitate reactions responsible for the production of ATP , such as the citric acid cycle , oxidative phosphorylation , oxidation of pyruvate , and the beta ...

  9. Oxidoreductase - Wikipedia

    en.wikipedia.org/wiki/Oxidoreductase

    In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule, the reductant, also called the electron donor, to another, the oxidant, also called the electron acceptor. This group of enzymes usually utilizes NADP+ or NAD+ as cofactors.