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  2. Flavin adenine dinucleotide - Wikipedia

    en.wikipedia.org/wiki/Flavin_adenine_dinucleotide

    FAD is the more complex and abundant form of flavin and is reported to bind to 75% of the total flavoproteome [16] and 84% of human encoded flavoproteins. [17] Cellular concentrations of free or non-covalently bound flavins in a variety of cultured mammalian cell lines were reported for FAD (2.2-17.0 amol/cell) and FMN (0.46-3.4 amol/cell). [18]

  3. Acyl-CoA dehydrogenase - Wikipedia

    en.wikipedia.org/wiki/Acyl-CoA_dehydrogenase

    The interface between the two monomers of a single dimer of an ACAD contains the FAD binding sites and has extensive bonding interactions. In contrast, the interface between the two dimers has fewer interactions. There are a total of 4 active sites within the tetramer, each of which contains a single FAD molecule and an acyl-CoA substrate ...

  4. Flavoprotein - Wikipedia

    en.wikipedia.org/wiki/Flavoprotein

    90 flavoproteins are encoded in the human genome; about 84% require FAD and around 16% require FMN, whereas 5 proteins require both. [4] Flavoproteins are mainly located in the mitochondria . [ 4 ] Of all flavoproteins, 90% perform redox reactions and the other 10% are transferases , lyases , isomerases , ligases .

  5. Nicotinamide adenine dinucleotide - Wikipedia

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

    NAD + in the cytosol is carried into the mitochondrion by a specific membrane transport protein, since the coenzyme cannot diffuse across membranes. [23] The intracellular half-life of NAD + was claimed to be between 1–2 hours by one review, [ 24 ] whereas another review gave varying estimates based on compartment: intracellular 1–4 hours ...

  6. 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 ...

  7. Flavin adenine dinucleotide synthetase 1 - Wikipedia

    en.wikipedia.org/wiki/Flavin_adenine_di...

    319945 Ensembl ENSG00000160688 ENSMUSG00000042642 UniProt Q8NFF5 Q8R123 RefSeq (mRNA) NM_001184891 NM_001184892 NM_025207 NM_201398 NM_177041 RefSeq (protein) NP_001171820 NP_001171821 NP_079483 NP_958800 NP_796015 NP_001349304 NP_001349305 Location (UCSC) Chr 1: 154.98 – 154.99 Mb Chr 3: 89.4 – 89.41 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Flavin adenine dinucleotide ...

  8. Acyl-CoA - Wikipedia

    en.wikipedia.org/wiki/Acyl-CoA

    During one cycle of beta oxidation, Acyl-CoA creates one molecule of Acetyl-CoA, FADH2, and NADH. [7] Acetyl-CoA is then used in the citric acid cycle while FADH2 and NADH are sent to the electron transport chain. [8] These intermediates all end up providing energy for the body as they are ultimately converted to ATP. [8]

  9. Electron transport chain - Wikipedia

    en.wikipedia.org/wiki/Electron_transport_chain

    An electron transport chain (ETC [1]) is a series of protein complexes and other molecules which transfer electrons from electron donors to electron acceptors via redox reactions (both reduction and oxidation occurring simultaneously) and couples this electron transfer with the transfer of protons (H + ions) across a membrane.