| Identification | More | [Name]
RIBOFLAVIN-5'-PHOSPHATE SODIUM SALT DIHYDRATE | [CAS]
6184-17-4 | [Synonyms]
FLAVINE MONONUCLEOTIDE NA, DIHYDRATE
FLAVINE MONONUCLEOTIDE SODIUM SALT DIHYDRATE
FLAVINMONONUCLEOTIDE DIHYDRATE
FLAVIN MONONUCLEOTIDE MONOSODIUM SALT DIHYDRATE
FLAVIN MONONUCLEOTIDE SODIUM SALT DIHYDRATE
FMM-NA 2H2O
FMN
FMN, DIHYDRATE
FMN MONOSODIUM SALT DIHYDRATE
FMN-NA DIHYDRATE
FMN SODIUM SALT, DIHYDRATE
RIBOFLAVIN 5'-MONOPHOSPHATE SODIUM SALT DIHYDRATE
RIBOFLAVIN-5'-PHOSPHATE MONOSODIUM SALT DIHYDRATE
RIBOFLAVIN 5'-PHOSPHATE SODIUM, DIHYDRATE
RIBOFLAVIN-5'-PHOSPHATE SODIUM SALT DIHYDRATE
RIBOFLAVINE 5'-PHOSPHATE MONOSODIUM SALT DIHYDRATE
RIBOFLAVINE-5'-PHOSPHATE SODIUM SALT DIHYDRATE
RIBOFLAVINE PHOSPHATE SODIUM SALT DIHYDRATE
RIBOFLAVIN SODIUM PHOSPHATE
SODIUM RIBOFLAVINE PHOSPHATE DIHYDRATE | [EINECS(EC#)]
204-988-6 | [Molecular Formula]
C17H24N4NaO11P | [MDL Number]
MFCD00150993 | [Molecular Weight]
514.36 | [MOL File]
6184-17-4.mol |
| Chemical Properties | Back Directory | [Appearance]
Yellowish crystalline powder | [Melting point ]
>300°C | [storage temp. ]
2-8°C
| [solubility ]
H2O: 0.1 g/mL, clear, orange-yellow
| [form ]
powder
| [color ]
Orange to Dark Orange | [Stability:]
Stable. Incompatible with strong oxidizing agents. | [Water Solubility ]
Soluble in water at 50mg/ml | [Merck ]
14,8201 | [BRN ]
4106529 | [Major Application]
pharmaceutical (small molecule) | [InChIKey]
YDUBDYSQHQHEEE-GUYVJCBKNA-N | [SMILES]
C(N1C2=NC(=O)NC(=O)C2=NC2C=C(C)C(C)=CC1=2)[C@H](O)[C@H](O)[C@H](O)COP(O)(O)=O.[NaH].O |&1:19,21,23,r| | [CAS DataBase Reference]
6184-17-4(CAS DataBase Reference) |
| Safety Data | Back Directory | [Safety Statements ]
S22:Do not breathe dust .
S24/25:Avoid contact with skin and eyes . | [WGK Germany ]
3
| [F ]
8 | [TSCA ]
Yes | [HS Code ]
29362300 | [Storage Class]
11 - Combustible Solids |
| Hazard Information | Back Directory | [Description]
Riboflavin 5''-monophosphate (FMN) is a coenzyme that is tightly bound to enzymes catalyzing oxidation and reduction reactions in a variety of biosynthetic pathways.1,2 FMN also binds the FMN riboswitch (RFN element) on RNA to alter gene regulation.3,4 FMN is a substrate of FMN phosphohydrolases and is used to study their function.5 | [Chemical Properties]
Yellowish crystalline powder | [Uses]
Riboflavin 5′-monophosphate (FMN) is used as a prosthetic group by oxidoreductase (one and two electron transfer) enzymes such as NADH dehydrogenases, nitric oxide synthases, and nitrilotriacetate monooxygenases. Riboflavin 5′-monophosphate is used as a substrate to study the specificity and kinetics of FMN phosphohydrolases. FMN is used to study molecular sensing based gene regulation by riboswitches. | [Uses]
Riboflavin 5''-(Dihydrogen Phosphate) Monosodium Salt Dihydrate is a phosphated nutritional factor found in milk, eggs, malted barley, liver, kidney, heart, leafy vegetables. Richest natural source is yeast. Minute amounts present in all plant and animal cells. Vitamin (enzyme cofactor). | [General Description]
Riboflavin 5′-monophosphate (FMN) is highly soluble in water. Flavins are considered as blue-light absorbing dyes. | [Biochem/physiol Actions]
Riboflavin 5′-monophosphate (FMN) acts as a cofactor in flavoproteins and possess biological activity in enzymes?and photoreceptors. | [Synthesis]
Synthesis steps of Riboflavin-5'-phosphate sodium salt dihydrate: in 1000ml three-necked bottle add 20ml water, 250ml tetrahydrofuran and 48g riboflavin stirring to dissolve into a mixture, cooled to 5 ~ 10 ℃, slowly add 100ml of aqueous sodium metapho | [Purification Methods]
Purify FMN by paper chromatography using tert-butanol/water, cutting out the main spot and eluting it with water. It can also be purified by adsorption onto an apo-flavodoxin column, followed by elution and freeze drying. It crystallises from aqueous acidic solution. [Mayhew & Strating Eur J Biochem 59 539 1976, Beilstein 26 III/IV 2555.] | [References]
[1] WALSH C T, WENCEWICZ T A. Flavoenzymes: Versatile catalysts in biosynthetic pathways[J]. Natural Product Reports, 2012, 1: 175-200. DOI: 10.1039/c2np20069d
[2] CHANGJIAN FENG. Dissecting regulation mechanism of the FMN to heme interdomain electron transfer in nitric oxide synthases[J]. Journal of Inorganic Biochemistry, 2014, 130: Pages 130-140. DOI: 10.1016/j.jinorgbio.2013.09.005
[3] ALEXANDER SERGANOV Dinshaw J P Lili Huang. Coenzyme recognition and gene regulation by a flavin mononucleotide riboswitch[J]. Nature, 2009, 458 7235: 233-237. DOI: 10.1038/nature07642
[4] NORIHIKO TAKEMOTO Masayuki I Yuya Tanaka. Rho and RNase play a central role in FMN riboswitch regulation in Corynebacterium glutamicum.[J]. Nucleic Acids Research, 2015, 43 1: 520-529. DOI: 10.1093/nar/gku1281
[5] De Souza, F.I., Zumiotti, A.V., and Da Silva, C.F. Neuregulins 1-α and 1-β on the regeneration the peripheral nerves[J]. Acta Ortop Bras. |
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| Company Name: |
Alfa Aesar
|
| Telephone: |
400-6106006 |
| Website: |
http://chemicals.thermofisher.cn |
| Company Name: |
Energy Chemical
|
| Telephone: |
400-0056266 |
| Website: |
www.energy-chemical.com |
|