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Flavin mononucleotide (FMN), or riboflavin-5′-phosphate, is a biomolecule produced from riboflavin (vitamin B 2) by the enzyme riboflavin kinase and functions as the prosthetic group of various oxidoreductases, including NADH dehydrogenase, as well as a cofactor in biological blue-light photo receptors. [1]
The 3 substrates of this enzyme are FMNH2, NAD +, and NADP +, whereas its 4 products are FMN, NADH, NADPH, and H +. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is FMNH2:NAD(P)+ oxidoreductase.
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5,6-dimethylbenzimidazole synthase (EC 1.14.99.40, BluB) is an enzyme with systematic name FMNH 2 oxidoreductase (5,6-dimethylbenzimidazole forming). [1] [2] [3] This enzyme catalyses the following chemical reaction
NAD + to NADH. FMN to FMNH 2. CoQ to CoQH 2.. Complex I is the first enzyme of the mitochondrial electron transport chain.There are three energy-transducing enzymes in the electron transport chain - NADH:ubiquinone oxidoreductase (complex I), Coenzyme Q – cytochrome c reductase (complex III), and cytochrome c oxidase (complex IV). [1]
Pyrimidine oxygenase (EC 1.14.99.46, RutA) is an enzyme with systematic name uracil,FMNH 2:oxygen oxidoreductase (uracil hydroxylating, ring-opening). [1] [2] This enzyme catalyses the following chemical reaction
In biochemistry, flavin adenine dinucleotide (FAD) is a redox-active coenzyme associated with various proteins, which is involved with several enzymatic reactions in metabolism.
Chorismate synthase requires the presence of a reduced flavin mononucleotide (FMNH2 or FADH2) for its activity. Chorismate synthase from various sources shows [2] [3] a high degree of sequence conservation. It is a protein of about 360 to 400 amino-acid residues.