Target type: molecularfunction
Binding to riboflavin. [GOC:TermGenie, PMID:12083520]
Riboflavin binding involves the specific interaction of a protein with the vitamin riboflavin (vitamin B2). This interaction is crucial for a variety of cellular processes, as riboflavin acts as a precursor for the coenzymes flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), which are essential for redox reactions catalyzed by various enzymes. The binding process typically involves the formation of non-covalent interactions between the protein and riboflavin, such as hydrogen bonds, van der Waals interactions, and hydrophobic interactions. These interactions are highly specific and ensure that riboflavin binds to the correct protein, allowing for the proper functioning of the enzyme. The binding site on the protein is often located in a deep pocket or groove, which provides a suitable environment for the interaction with riboflavin. The structure of the binding site and the interactions with riboflavin can vary between different proteins, depending on the specific function of the enzyme. For example, the binding site in some proteins may include aromatic amino acids that interact with the isoalloxazine ring of riboflavin, while other proteins may have charged residues that interact with the phosphate group. The process of riboflavin binding is essential for the proper function of a wide range of cellular processes, including energy metabolism, DNA replication, and the biosynthesis of various molecules.'
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| Protein | Definition | Taxonomy |
|---|---|---|
| Riboflavin-binding protein | A protein that is a translation product of the RTBDN gene in chicken. [PRO:DNx, UniProtKB:P02752] | Gallus gallus (chicken) |
| Compound | Definition | Classes | Roles |
|---|---|---|---|
| quinacrine | quinacrine : A member of the class of acridines that is acridine substituted by a chloro group at position 6, a methoxy group at position 2 and a [5-(diethylamino)pentan-2-yl]nitrilo group at position 9. Quinacrine: An acridine derivative formerly widely used as an antimalarial but superseded by chloroquine in recent years. It has also been used as an anthelmintic and in the treatment of giardiasis and malignant effusions. It is used in cell biological experiments as an inhibitor of phospholipase A2. | acridines; aromatic ether; organochlorine compound; tertiary amino compound | antimalarial; EC 1.8.1.12 (trypanothione-disulfide reductase) inhibitor |
| chloroquine | chloroquine : An aminoquinoline that is quinoline which is substituted at position 4 by a [5-(diethylamino)pentan-2-yl]amino group at at position 7 by chlorine. It is used for the treatment of malaria, hepatic amoebiasis, lupus erythematosus, light-sensitive skin eruptions, and rheumatoid arthritis. Chloroquine: The prototypical antimalarial agent with a mechanism that is not well understood. It has also been used to treat rheumatoid arthritis, systemic lupus erythematosus, and in the systemic therapy of amebic liver abscesses. | aminoquinoline; organochlorine compound; secondary amino compound; tertiary amino compound | anticoronaviral agent; antimalarial; antirheumatic drug; autophagy inhibitor; dermatologic drug |
| lumiflavin | lumiflavin : A compound showing yellow-green fluorescence, formed by a photolysis of riboflavin in alkaline solution. | flavin | |
| riboflavin | vitamin B2 : Any member of a group of vitamers that belong to the chemical structural class called flavins that exhibit biological activity against vitamin B2 deficiency. Symptoms associated with vitamin B2 deficiency include glossitis, seborrhea, angular stomaitis, cheilosis and photophobia. The vitamers include riboflavin and its phosphate derivatives (and includes their salt, ionised and hydrate forms). | flavin; vitamin B2 | anti-inflammatory agent; antioxidant; cofactor; Escherichia coli metabolite; food colouring; fundamental metabolite; human urinary metabolite; mouse metabolite; photosensitizing agent; plant metabolite |