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The prokaryotic riboflavin biosynthesis protein is a bifunctional enzyme found in bacteria that catalyzes the phosphorylation of riboflavin into flavin mononucleotide (FMN) and the adenylylation of FMN into flavin adenine dinucleotide (FAD). It consists of a C-terminal riboflavin kinase and an N-terminal FMN-adenylyltransferase. This bacterial ...
Riboflavin deficiency appears to impair the metabolism of the dietary mineral, iron, which is essential to the production of hemoglobin and red blood cells. Alleviating riboflavin deficiency in people who are deficient in both riboflavin and iron improves the effectiveness of iron supplementation for treating iron-deficiency anemia .
Riboflavin synthase is an enzyme that catalyzes the final reaction of riboflavin biosynthesis. It catalyzes the transfer of a four-carbon unit from one molecule of 6,7-dimethyl-8-ribityllumazine onto another, resulting in the synthesis of riboflavin and 5-amino-6-ribitylamino-2,4(1 H ,3 H )-pyrimidinedione :
Its active form is a coenzyme called thiamine pyrophosphate (TPP), which takes part in the conversion of pyruvate to acetyl coenzyme A in metabolism. [11] Vitamin B 2: Riboflavin: Riboflavin is involved in release of energy in the electron transport chain, the citric acid cycle, as well as the catabolism of fatty acids (beta oxidation). [12 ...
In Photobacterium leiognathi, the riboflavin synthesis genes ribB (DHBP synthase), ribE (riboflavin synthase), ribH (lumazine synthase) and ribA (GTP cyclohydrolase II) all reside in the lux operon. [2] RibB is sometimes found as a bifunctional enzyme with GTP cyclohydrolase II that catalyses the first committed step in the biosynthesis of
Biosynthesis, i.e., chemical synthesis occurring in biological contexts, is a term most often referring to multi-step, enzyme-catalyzed processes where chemical substances absorbed as nutrients (or previously converted through biosynthesis) serve as enzyme substrates, with conversion by the living organism either into simpler or more complex ...
This reaction is part of the biosynthesis of riboflavin (vitamin B2). Lumazine synthase is thus found in those organisms (plants, fungi and most microorganisms) which produce riboflavin. [2] Depending on the species, 5, 10 or 60 copies of the enzyme bind together to form homomers.
Epidermin biosynthesis protein, EpiD, which has been shown to be a flavoprotein that binds FMN. This enzyme catalyses the removal of two reducing equivalents from the cysteine residue of the C-terminal meso - lanthionine of epidermin to form a --C==C-- double bond [ 12 ]