Search results
Results from the WOW.Com Content Network
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).
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.
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 ...
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 ...
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.
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.
In order to work as a catalyst, GOx requires a coenzyme, flavin adenine dinucleotide (FAD). FAD is a common component in biological oxidation-reduction reactions. Redox reactions involve a gain or loss of electrons from a molecule. In the GOx-catalyzed redox reaction, FAD works as the initial electron acceptor and is reduced to FADH −. [12]
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]