Flavoprotein
Protein family / From Wikipedia, the free encyclopedia
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Flavoproteins are proteins that contain a nucleic acid derivative of riboflavin. These proteins are involved in a wide array of biological processes, including removal of radicals contributing to oxidative stress, photosynthesis, and DNA repair. The flavoproteins are some of the most-studied families of enzymes.
Flavoprotein | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
Symbol | Flavoprotein | ||||||||
Pfam | PF02441 | ||||||||
InterPro | IPR003382 | ||||||||
SCOP2 | 1e20 / SCOPe / SUPFAM | ||||||||
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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] Based on the available structural data, FAD-binding sites can be divided into more than 200 different types.[3]
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]