enow.com Web Search

Search results

  1. Results from the WOW.Com Content Network
  2. Flavin adenine dinucleotide - Wikipedia

    en.wikipedia.org/wiki/Flavin_adenine_dinucleotide

    In biochemistry, flavin adenine dinucleotide (FAD) is a redox-active coenzyme associated with various proteins, which is involved with several enzymatic reactions in metabolism. A flavoprotein is a protein that contains a flavin group , which may be in the form of FAD or flavin mononucleotide (FMN).

  3. Flavoprotein - Wikipedia

    en.wikipedia.org/wiki/Flavoprotein

    This led to the discovery that the protein studied required not riboflavin but flavin mononucleotide to be catalytically active. [6] [7] Similar experiments with D-amino acid oxidase [8] led to the identification of flavin adenine dinucleotide (FAD) as a second form of flavin utilised by enzymes. [9]

  4. Acyl-CoA dehydrogenase - Wikipedia

    en.wikipedia.org/wiki/Acyl-CoA_dehydrogenase

    This gives a total of four FAD molecules and four acyl-CoA substrate binding sites per enzyme. FAD is bound between the three domains of the monomer, where only the nucleotide portion is accessible. FAD binding contributes significantly to overall enzyme stability. The acyl-CoA substrate is bound completely within each monomer of the enzyme ...

  5. Dehydrogenase - Wikipedia

    en.wikipedia.org/wiki/Dehydrogenase

    FAD, or flavin adenine dinucleotide, is a prosthetic group (a non-polypeptide unit bound to a protein that is required for function) that consists of an adenine nucleotide and a flavin mononucleotide. [10] FAD is a unique electron acceptor.

  6. Flavin group - Wikipedia

    en.wikipedia.org/wiki/Flavin_group

    The flavin moiety is often attached with an adenosine diphosphate to form flavin adenine dinucleotide (FAD), and, in other circumstances, is found as flavin mononucleotide (or FMN), a phosphorylated form of riboflavin. It is in one or the other of these forms that flavin is present as a prosthetic group in flavoproteins.

  7. Branched-chain alpha-keto acid dehydrogenase complex

    en.wikipedia.org/wiki/Branched-chain_alpha-keto...

    The E 3 component is a flavoprotein, and it re-oxidizes the reduced lipoyl sulfur residues of E 2 using FAD (a catalytic cofactor) as the oxidant. FAD then transfers these protons and electrons to NAD+ (a stoichiometric cofactor) to complete the reaction cycle.

  8. Adrenodoxin reductase - Wikipedia

    en.wikipedia.org/wiki/Adrenodoxin_reductase

    Adrenodoxin reductase is a flavoprotein as it carries a FAD type coenzyme. The enzyme functions as the first electron transfer protein of mitochondrial P450 systems such as P450scc. [6] The FAD coenzyme receives two electrons from NADPH and transfers them one at a time to the electron transfer protein adrenodoxin. [13]

  9. Adenine - Wikipedia

    en.wikipedia.org/wiki/Adenine

    Adenine derivatives have various roles in biochemistry including cellular respiration, in the form of both the energy-rich adenosine triphosphate (ATP) and the cofactors nicotinamide adenine dinucleotide (NAD), flavin adenine dinucleotide (FAD) and Coenzyme A. It also has functions in protein synthesis and as a chemical component of DNA and RNA ...