Flavin mononucleotide Riboflavin phosphate

Flavin mononucleotide (riboflavin-5 -phosphate) is synthesized from riboflavin with a purified enzyme from yeast according to the following equation ... 

Phosphate [146-17-8]. Rihoflavine 5 - dihydrogen phosphate), 9CL Flavin mononucleotide. Lactoflavin phosphate. Monophosphoribojiavin. Riboflavin monophosphate. Vitamin 82 phosphate. FMN The prosthetic group of various flavine enzymes. 

Riboflavin-5 -Phosphate. Riboflavin-5 -phosphate [146-17-8] (vitamin B2 phosphate, flavin mononucleotide, FMN, cytoflav), C2yH22N402P,... 

Riboflavin, or vitamin B2, is a constituent and precursor of both riboflavin 5 -phosphate, also known as flavin mononucleotide (FMN), and flavin adenine dinucleotide (FAD). The name riboflavin is a synthesis of the names for the molecule s component parts, ribitol and flavin. The structures of riboflavin. 

The varions flavin phosphates and their acetyl derivatives were identified by pH titration, electrophoresis, and H-NMR, which permit direct analysis of crude reaction prodncts as well as rapid purity check of commercial flavin mononucleotide or riboflavin 5 -monophosphate (FMN or 5 -FMN) [7]. Riboflavin 4 -monophosphate was determined as the main by-product of commercial FMN by preparative TLC on cellulose with n-butanol/acetic add/water (5 2 3, v/v) as a solvent [7]. 

HPLC with fluorescence detection was employed for the analysis of riboflavin (RF), flavin mononucleotide (FMN) and flavin-adenin dinucleotide (FAD) in beer, wine and other beverages. The investigation was motivated by the finding that these compounds are responsible for the so-called taste of light which develops in beverages exposed to light. Samples were filtered and injected in to the analytical column without any other pretreatment. Separations were carried out in an ODS column (200 X 2.1mm i.d. particle size 5 pm). Solvents A and B were 0.05 M phosphate buffer (pH 3) and ACN, respectively. The... 

The metal complexes of riboflavin-5 -phosphate (flavin mononucleotide, FMN) have been studied. Zn(FMN)-2H20 shows some perturbation of the IR bands of the phosphate group, suggesting that metal binding occurs at the phosphate group.579 Reviews are available.9-15 468c h 1470... 

FMN is the standard biochemical abbreviation for flavin mononucleotide (or riboflavin phosphate). The sodium salt (95-97% pure) of FMN is used. This grade 1s inexpensive and is available from Sigma Chemical Company. Its purpose is to effect recycling of the catalytic amount used of the much more costly NAD. A larger than stoichiometric amount of FMN is employed in order to ensure rapid recycling of the NAO. 

FMN Flavin mononucleotide as sodium salt Riboflavine 5 -(dihydrogen phosphate), monosodium salt (8,9) (130-40-5)... 

Flavin Mononucleotide, Sodium Salt Riboflavin 5 -Phosphate Ester Monosodium Salt Riboflavin 5 -Phosphate Ester Monosodium Salt, Dihydrate... 

Flavin mononucleotide (FMN)-adenosine and flavin adenine dinucleotide (FAD)-adenosine complexes show quenched triplet lifetimes compared to FMN alone, which is cited as evidence of intramolecular com-plexation between the flavins and adenosine by Shiga and Piette [142]. Adenosine phosphates also form complexes with FAD [143]. The com-plexation between a flavin and adenosine is identical to the intermolecular complexing of adenosine and flavin moieties, in the latter case enforced by hydrophobic bonding [144-146]. Rath and McCormick [147] have examined the riboflavin complexes of a series of purine ribose derivatives... 

The ribityl moiety is not linked to the isoalloxazine ring by a glycosidic linkage, and it is not strictly correct to caU FAD a dinucleotide. Nevertheless, this trivial name is accepted, as indeed is the even less correct term flavin mononucleotide for riboflavin phosphate. 

In higher mammals, riboflavin is absorbed readily from the intestines and distributed to all tis.sues. It is the precursor in the biosynthesis of the cocnzyme.s flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD). The metabolic functions of this vitamin involve these Iwocoenzymes. which participate in numerous vital oxidation-reduction proces.ses. FMN (riboflavin 5 -phosphate) is produced from the vitamin and ATP by flavokinasc catalysis. This step con be inhibited by phcnothiazincs and the tricyclic antidepressants. FAD originates from an FMN and ATP reaction that involves reversible dinucicotide formation catalyzed by flavin nucleotide pyrophosphorylase. The.se coenzymes function in combination with several enzymes as coenzyme-en-zyme complexes, often characterized as, flavoproteins. 

Other Coenzymes and Cofactors.— The chemical synthesis of riboflavin phosphates and their acetyl derivatives has been reinvestigated. Riboflavin 4 -monophosphate (10) is an important contaminant of commercial flavin mononucleotide (FMN), and... 

Flavin mononucleotide (FMN) (also called riboflavin phosphate)... 

Bi) is converted to thiamine pyrophosphate simply by the addition of pyrophosphate. It is involved in aldehyde group transfer. Niacin (nicotinic acid) is esterified to adenine dinucleotide and its two phosphates to form nicotinamide adenine dinucleotide. Pyridoxine (vitamin B ) is converted to either pyridoxal phosphate or pyridoxamine phosphate before complexing with enzymes. Riboflavin becomes flavin mononucleotide by obtaining one phosphate (riboflavin 5 -phosphate). If it complexes with adenine dinucleotide via a pyrophosphate ester linkage, it becomes flavin adenine dinucleotide. 

Flavin mononucleotide (Na, 2H2O salt, riboflavin-5 -phosphate [Na salt, 2H2O], FMN)... 

It is still unknown how the pyrimidine intermediate 5 is dephosphorylated (reaction VI). However, it is well established that the dephosphorylation product 6 is condensed with 3,4-dihydroxy-2-butanone 4-phosphate (8) by the catalytic action of lumazine synthase (reaction VIII). The carbohydrate substrate 8 is in turn obtained from ribulose phosphate (7) by a complex reaction sequence that is catalyzed by a single enzyme, 3,4-dihydroxy-2-butanone 4-phosphate synthase (reaction VII). As mentioned above, the lumazine 9 is converted to riboflavin (10) by the catalytic action of riboflavin synthase (reaction IX). Ultimately, riboflavin is converted to the coenzymes, riboflavin 5 -phosphate (flavin mononucleotide (FMN), 11) and flavin adenine dinucleotide (FAD, 12) by the catalytic action of riboflavin kinase (reaction X) and FAD synthase (reaction XI). These reaction steps are required in all organisms, irrespective of their acquisition of riboflavin from nutritional sources or by endogenous biosynthesis. 

Fig. 19.10. Reduction of FAD. FAD accepts two electrons as two hydrogen atoms and is reduced. The reduced coenzyme is denoted in this text as FAD(2H) because it often accepts a total of two electrons one at a time, never going to the fully reduced form, FADH2. FMN (flavin mononucleotide) consists of riboflavin with one phosphate group attached.

Ann O Rexia has been malnourished for some time, and has developed subclinical deficiencies of many vitamins, including riboflavin. The coenzymes FAD (flavin adenine dinucleotide) and FMN (flavin mononucleotide) are synthesized from the vitamin riboflavin. Riboflavin is actively transported into cells, where the enzyme flavokinase adds a phosphate to form FMN. FAD synthetase then adds AMP to form FAD. FAD is the major coenzyme in tissues and is generally found tightly bound to proteins, with about 10% being covalently bound. Its turnover in the body is very slow, and people can live for long periods on low intakes without displaying any signs of a riboflavin deficiency. 

In riboflavin (7,8-dimethyl-10-(/ )-ribityl isoalloxazine), the polyol ribitol is connected via an amino bond to the chromophore. Riboflavin is not an iV-gly-coside. Accordingly, flavin mononucleotide (FMN, riboflavin S -phosphate) and flavin adenine dinucleotide (FAD riboflavin 5 -adenosine diphosphate) are hydrolyzable only in the nucleotide part (Scheme 7.2.22). 

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