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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).
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.
Flavoproteins have either FMN (flavin mononucleotide) or FAD (flavin adenine dinucleotide) as a prosthetic group or as a cofactor. The flavin is generally tightly bound (as in adrenodoxin reductase, wherein the FAD is buried deeply). [1] About 5-10% of flavoproteins have a covalently linked FAD. [2]
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 ...
Flavin adenine dinucleotide (FAD) is a required co-factor in addition to the presence of an active site glutamate in order for the enzyme to function. The following reaction is the oxidation of the fatty acid by FAD to afford an α,β-unsaturated fatty acid thioester of coenzyme A:
Flavin Adenine Dinucleotide. 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.
Therefore, SDHA is a flavoprotein (Fp) due to the prosthetic group flavin adenine dinucleotide (FAD). Crystal structure suggests that FAD is covalently bound to a histidine residue (His99) and further coordinated by hydrogen bonds with number of other amino acid residues within the FAD-binding domain.
Note that the cofactor of E3 is a tightly bound flavin adenine dinucleotide (FAD) molecule. The electrons from dihydrolipoamide are transferred, via FAD, to NAD+, forming NADH. This is noteworthy since in the usual order of reduction potentials, the reduction of FAD by NADH would be the energetically favorable process.
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