Riboflavin 5-phosphate sodium - CAS 130-40-5
Catalog number: B0084-056970
Category: Inhibitor
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Riboflavin 5-phosphate sodium, a riboflavin derivative, is a commonly existed nutritional factor and could improve the biomechanical stiffness of corneal.
Vitamin supplement in health care products.
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B0084-056970 250 g $199 In stock
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Flavin Mononucleotide; Riboflavin sodium phosphate
Ingredient of health care products.
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1.WrpA Is an Atypical Flavodoxin Family Protein under Regulatory Control of the Brucella abortus General Stress Response System.
Herrou J1, Czyż DM1, Willett JW1, Kim HS1, Chhor G2, Babnigg G2, Kim Y2, Crosson S3. J Bacteriol. 2016 Mar 31;198(8):1281-93. doi: 10.1128/JB.00982-15. Print 2016 Apr 15.
The general stress response (GSR) system of the intracellular pathogenBrucella abortuscontrols the transcription of approximately 100 genes in response to a range of stress cues. The core genetic regulatory components of the GSR are required forB. abortussurvival under nonoptimal growth conditionsin vitroand for maintenance of chronic infection in anin vivomouse model. The functions of the majority of the genes in the GSR transcriptional regulon remain undefined.bab1_1070is among the most highly regulated genes in this regulon: its transcription is activated 20- to 30-fold by the GSR system under oxidative conditionsin vitro We have solved crystal structures of Bab1_1070 and demonstrate that it forms a homotetrameric complex that resembles those of WrbA-type NADH:quinone oxidoreductases, which are members of the flavodoxin protein family. However,B. abortusWrbA-relatedprotein (WrpA) does not bind flavin cofactors with a high affinity and does not function as an NADH:quinone oxidoreductasein vitro Soaking crystals with flavin mononucleotide (FMN) revealed a likely low-affinity binding site adjacent to the canonical WrbA flavin binding site.
2.Degradation of Reactive Black 5 dye by a newly isolated bacterium Pseudomonas entomophila BS1.
Khan S1,2, Malik A2,2. Can J Microbiol. 2016 Mar;62(3):220-32. doi: 10.1139/cjm-2015-0552. Epub 2015 Nov 23.
The textile and dye industries are considered as one of the major sources of environmental pollution. The present study was conducted to investigate the degradation of the azo dye Reactive Black 5 (RB 5) using a bacterium isolated from soil samples collected around a textile industry. The bacterial strain BS1 capable of degrading RB 5 was isolated and identified as Pseudomonas entomophila on the basis of 16S rDNA sequencing. The effects of different parameters on the degradation of RB 5 were studied to find out the optimal conditions required for maximum degradation, which was 93% after 120 h of incubation. Static conditions with pH in the range of 5-9 and a temperature of 37 °C were found to be optimum for degrading RB 5. Enzyme assays demonstrated that P. entomophila possessed azoreductase, which played an important role in degradation. The enzyme was dependent on flavin mononucleotide and NADH for its activity. Furthermore, a possible degradation pathway of the dye was proposed through gas chromatography - mass spectrometry analysis, which revealed that the metabolic products were naphthalene-1,2-diamine and 4-(methylsulfonyl) aniline.
3.Kinetic and Binding Studies of Streptococcus pneumoniae Type 2 Isopentenyl Diphosphate:Dimethylallyl Diphosphate Isomerase.
Janczak MW1, Poulter CD1. Biochemistry. 2016 Apr 5. [Epub ahead of print]
Type 2 isopentenyl diphosphate:dimethylallyl diphosphate isomerase (IDI-2) converts isopentenyl diphosphate (IPP) to dimethylallyl diphosphate (DMAPP), the two fundamental building blocks of isoprenoid molecules. IDI-2 is found in many species of bacteria and is a potential antibacterial target since this isoform is non-homologous to the type 1 enzyme in Homo sapiens. IDI-2 requires a reduced flavin mononucleotide to form the catalytically active ternary complex, IDI-2·FMNH2·IPP. For IDI-2 from the pathogenic bacterium Streptococcus pneumoniae, the flavin can be treated kinetically as a dissociable cosubstrate in incubations with IPP and excess NADH. Under these conditions, the enzyme follows a modified sequential ordered mechanism where FMN adds before IPP. Interestingly, the enzyme shows sigmoidal behavior when incubated with IPP and NADH with varied concentrations of FMN in aerobic conditions. In contrast, sigmoidal behavior is not seen in incubations under anaerobic conditions where FMN is reduced to FMNH2 before the reaction is initiated by addition of IPP.
4.Engineering nitric oxide synthase chimeras to function as NO dioxygenases.
Wang ZQ1, Haque MM2, Binder K2, Sharma M2, Wei CC3, Stuehr DJ4. J Inorg Biochem. 2016 Mar 15. pii: S0162-0134(16)30066-6. doi: 10.1016/j.jinorgbio.2016.03.002. [Epub ahead of print]
Nitric oxide synthases (NOSs) catalyze a two-step oxidation of l-arginine to form nitric oxide (NO) and l-citrulline. NOS contains a N-terminal oxygenase domain (NOSoxy) that is the site of NO synthesis, and a C-terminal reductase domain (NOSred) that binds nicotinamide adenine dinucleotide phosphate (NADPH), flavin adenine dinucleotide (FAD), and flavin mononucleotide (FMN) and provides electrons to the NOSoxy heme during catalysis. The three NOS isoforms in mammals inducible NOS (iNOS), neuronal NOS (nNOS), and endothelial NOS (eNOS) share high structural similarity but differ in NO release rates and catalytic properties due to differences in enzyme kinetic parameters. These parameters must be balanced for NOS enzymes to release NO, rather than consume it in a competing, inherent NO dioxygenase reaction. To improve understanding, we drew on a global catalytic model and previous findings to design three NOS chimeras that may predominantly function as NO dioxygenases: iNOSoxy/nNOSred (Wild type (WT) chimera), V346I iNOSoxy/nNOSred (V346I chimera) and iNOSoxy/S1412D nNOSred (S1412D chimera).
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CAS 130-40-5 Riboflavin 5-phosphate sodium

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