ImageFile Ref chemboximage correct ?? ImageName Kekul , skeletal formula of a minor riboflavin 10 2S,3S,4R 2,3,4 trihydroxypentyl tautomer ImageFileL1 Riboflavin 3d.png ImageFileL1 Ref chemboximage correct ?? ImageNameL1 Spacefill model of a minor riboflavin 10 2S,3S,4R 2,3,4 trihydroxypentyl tautomer ImageFileR1 Riboflavin powder.jpg ImageNameR1 Sample of microcrystaline riboflavin IUPACName 7,8 ... correct drugbank KEGG D00050 KEGG Ref keggcite changed kegg MeSHName Riboflavin ChEBI 17015 ... sup Appearance Orange crystals LogP 0.095 pKa 9.888 pKb 4.109 Image Riboflavin solution.jpg thumb right A solution of riboflavin. Riboflavin , also known as vitamin B sub 2 sub is an easily absorbed ... J. Drake title Riboflavin work Micronutrient Information Center publisher Linus Pauling Institute at Oregon State University year 2007 url http lpi.oregonstate.edu infocenter vitamins riboflavin ... destroys riboflavin. The name riboflavin comes from ribose the sugar whose reduction chemistry ... occurs in metabolism along with the oxidized form, is colorless. Riboflavin is best known visually ... diet. Image Riboflavinspectra.jpg thumb left Fluorescent spectra of riboflavin Further, they noted ... GSSG to its reduced form GSH is also FAD dependent Riboflavin in food occurrence, sources and stability Riboflavin is yellow or yellow orange in color and in addition to being used as a food ... George 2006. P168 175 Ball F.M. George, Riboflavin in Vitamins in Foods, Analysis, Bioavailability ... layers into the endosperm. Free riboflavin is naturally present in foods along with protein bound FMN and FAD. Bovine milk contains mainly free riboflavin, with a minor contribution from FMN and FAD .... Vitaminol., 37, 15, 1991 ref Egg white and egg yolk contain specialized riboflavin binding proteins, which are required for storage of free riboflavin in the egg for use by the developing embryo. It is difficult to incorporate riboflavin into many liquid products because it has poor solubility in water ... more details
enzyme Name riboflavin phosphotransferase EC number 2.7.1.42 CAS number 9026 26 0 IUBMB EC number 2 7 1 42 GO code 0050257 image width caption In enzymology , a riboflavin phosphotransferase EC number 2.7.1.42 is an enzyme that catalysis catalyzes the chemical reaction alpha D glucose 1 phosphate riboflavin math rightleftharpoons math D glucose FMN Thus, the two substrate biochemistry substrates of this enzyme are alpha D glucose 1 phosphate and riboflavin , whereas its two product chemistry products are D glucose and flavin mononucleotide FMN . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing groups phosphotransferase s with an alcohol group as acceptor. The systematic name of this enzyme class is alpha D glucose 1 phosphate riboflavin 5 phosphotransferase . Other names in common use include riboflavine phosphotransferase , glucose 1 phosphate phosphotransferase , G 1 P phosphotransferase , and D glucose 1 phosphate riboflavin 5 phosphotransferase . References reflist 1 cite journal author Katagiri H, Yamada H and Imai K date Tokyo title The transphosphorylation reactions catalyzed by glucose 1 phosphate phosphotransferases of Escherichia coli. I. Enzymic phosphorylation of riboflavine journal J. volume Biochem. pages 1119&ndash 1126 enzyme stub Category EC 2.7.1 Category Enzymes of unknown structure ... more details
enzyme Name riboflavin kinase EC number 2.7.1.26 CAS number 9032 82 0 IUBMB EC number 2 7 1 26 GO code 0008531 image Riboflavkinase.png width caption Crystal structure of riboflavin kinase from Thermoplasma ..., Almo, S.C. year 2008 title Crystal structure of riboflavin kinase from Thermoplasma acidophilum ref Infobox protein family Symbol Flavokinase Name Riboflavin kinase image PDB 1s4m EBI.jpg width caption ... Symbol Riboflavin kinase Name Riboflavin kinase Pfam PF01687 InterPro IPR015865 PROSITE PDB PDB 1mrz PDB 1n05 PDB 1n06 PDB 1n07 PDB 1n08 PDB 1nb0 PDB 1nb9 PDB 1p4m PDB 1q9s PDB 1s4m In enzymology , a riboflavin ... riboflavin math rightleftharpoons math ADP FMN Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and riboflavin , whereas its two product chemistry products are adenosine diphosphate ADP and flavin mononucleotide FMN . Riboflavin is converted into catalytically active cofactors FAD and FMN by the actions of riboflavin kinase EC number 2.7.1.26 , which ... riboflavin kinase is orthologous to the Prokaryotic riboflavin biosynthesis protein bifunctional ... S title Ligand binding induced conformational changes in riboflavin kinase structural basis for the ordered .... The systematic name of this enzyme class is ATP riboflavin 5 phosphotransferase . This enzyme is also called flavokinase . This enzyme participates in riboflavin metabolism . However, CTP dependent riboflavin kinase archaeal riboflavin kinases EC number 2.7.1.161 are, in general, utilizing Cytidine triphosphate CTP rather than ATP as the donor nucleotide, catalyzing the reaction CTP riboflavin ... 2007 title A CTP Dependent Archaeal Riboflavin Kinase Forms a Bridge in the Evolution of Cradle ... url http www.uniprot.org uniprot Q9HJA6 ref Riboflavin kinase can also be isolated from ... Image hydrophob.gif thumb left alt A hydropathy plot for Riboflavin Kinase. Image ramachandran3CTA.jpg thumb none alt A hydropathy plot for Riboflavin Kinase. The complete enzyme arrangement can be observed ... more details
enzyme Name Riboflavin synthase EC number 2.5.1.9 CAS number 9075 82 5 IUBMB EC number 2 5 1 9 GO code ... E. coli br riboflavin synthase. ref name Liao PDB 1i8d Cite journal author Liao DI, Wawrzak Z, Calabrese JC, Viitanen PV, Jordan DB title Crystal structure of riboflavin synthase journal Structure volume ... Monomer With Ligands.jpg width caption Riboflavin synthase from Schizosaccharomyces pombe S. pombe ... Studies on the reaction mechanism of riboflavin synthase X ray crystal structure of a complex with 6 ... , PDB2 2c9b , PDB2 2c9d , PDB2 2f59 , PDB2 2i0f , PDB2 2o6h , PDB2 2obx , PDB2 2vi5 Riboflavin synthase is an enzyme that catalyzes the final reaction of riboflavin biosynthesis 2 6,7 dimethyl 8 ribityllumazine riboflavin 5 amino 6 ribitylamino 2,4 1H,3H pyrimidinedione 5 amino 6 ribitylamino 2,4 1 H ,3 H pyrimidinedione Structure The Riboflavin synthase monomer is 23kDa. Each monomer contains two ... B, Eisenreich W, Gerhardt S, Cushman M, Steinbacher S, Huber R, Bacher A title Riboflavin ... riboflavin formation at a time as the other two sites face outward and are exposed to solvent . ref ... and mechanism of riboflavin synthase journal Arch. Biochem. Biophys. volume 474 issue 2 pages ... No Cofactor biochemistry cofactors are needed for catalysis. Additionally, the formation of riboflavin from 6,7 dimethyl 8 ribityllumazine can occur in boiling aqueous solution in the absence riboflavin ... G title Biosynthesis of vitamin b2 riboflavin journal Annu. Rev. Nutr. volume 20 issue pages 153 67 ... YJ, Jordan DB, Liao DI title Examination of a reaction intermediate in the active site of riboflavin ... Production Scientists have hypothesized that enzymes involved in the riboflavin biosynthesis pathway, including riboflavin synthase, can be used to develop antibacterial drugs in order to treat infections ... negative bacteria, such as E. coli and S. typhimurium, to uptake riboflavin from the external environment ... of riboflavin synthase and lumazine synthase journal J. Org. Chem. volume 66 issue 25 pages ... more details
Unreferenced stub auto yes date December 2009 Orphan date November 2006 Riboflavin carrier proteins RFCPs together with human serum albumin transport flavin mononucleotide FMN in the Circulatory system blood circuit . RFCPs are important in pregnancy . DEFAULTSORT Riboflavin Carrier Protein Category Hematology Biochem stub ... more details
Infobox protein family Symbol FAD syn Name FAD synthetase image PDB 1s4m EBI.jpg width caption crystal structure of flavin binding to fad synthetase from thermotoga maritina Pfam PF06574 Pfam clan CL0119 InterPro IPR015864 SMART PROSITE MEROPS SCOP 1n05 TCDB OPM family OPM protein CAZy CDD In molecular biology, the prokaryotic riboflavin biosynthesis protein is a bifunctional enzyme found in bacteria . Riboflavin is converted into catalyst catalytically active Cofactor biochemistry cofactors FAD and FMN by the actions of riboflavin kinase EC number 2.7.1.26 , which converts it into FMN, and FAD synthetase EC number 2.7.7.2 , which Adenylation adenylates FMN to FAD. Eukaryotes usually have two separate enzymes, while most prokaryotes have a single bifunctional protein that can carry out both catalyses, although exceptions occur in both cases. While eukaryotic monofunctional riboflavin kinase is orthologous to the bifunctional prokaryotic enzyme , the monofunctional FAD synthetase differs from its Prokaryote prokaryotic counterpart, and is instead related to the PAPS reductase family. ref name pmid14580199 cite journal author Karthikeyan S, Zhou Q, Osterman AL, Zhang H title Ligand binding induced conformational changes in riboflavin kinase structural basis for the ordered mechanism journal Biochemistry volume 42 issue 43 pages 12532 8 year 2003 month November pmid 14580199 doi 10.1021 bi035450t url ref ref name pmid17049878 cite journal author Galluccio M, Brizio C, Torchetti EM, Ferranti P, Gianazza E, Indiveri C, Barile M title Over expression in Escherichia coli, purification and characterization of isoform 2 of human FAD synthetase journal Protein Expr. Purif. volume 52 issue 1 pages 175 81 year 2007 month March pmid 17049878 doi 10.1016 j.pep.2006.09.002 url ref The bacteria l FAD synthetase that is part of the bifunctional enzyme has remote similarity to nucleotidyl transferase s and, hence, it may be involved in the adenylylation reaction of FAD synthetases. r ... more details
Pathogen reduction using riboflavin and UV light is a method by which infectious pathogen s in blood transfusion blood for transfusion are inactivated by adding riboflavin and irradiating with ultraviolet UV light . ref name Hardwick cite journal author Hardwick CC, Herivel TR, Hernandez SC, Ruane PH, Goodrich RP title Separation, identification and quantification of riboflavin and its photoproducts in blood products using high performance liquid chromatography with fluorescence detection a method to support pathogen reduction technology journal Photochem. Photobiol. volume 80 issue 3 pages 609 ... Falciparum in Plasma and Platelet Concentrations with Riboflavin and UV Light journal Vox Sanguinis ... Toxicity testing of a novel riboflavin based technology for pathogen reduction and white blood cell ... introduced. This technology uses riboflavin and light for the treatment of PLTs and plasma. Method This pathogen reduction process involves adding riboflavin vitamin B2 to the blood component, which ... to UV light activates riboflavin and when it is associated with nucleic acid s DNA and RNA , riboflavin ... M, Rold n V, Rivera J, Tsai HM, Vicente V, Roig R title The influence of riboflavin photochemistry ... inactivation of selected viruses and bacteria in platelet concentrates using riboflavin and light ... chapter Chapter 5 The Antiviral and Antibacterial Properties of Riboflavin and Light Applications ... doi 10.1111 j.1537 2995.2010.02984.x url issn ref UV Light Riboflavin Irreversible Inactivation This method using riboflavin and UV light renders pathogens harmless by using a non mutagenic, non toxic method. Riboflavin and its photoproducts are already present in the human body and do not need ... and platelet concentrates using riboflavin and ultraviolet light journal Transfus. Apher. Sci ... blood products, riboflavin and UV light treatment may be used as an alternative to gamma irradiation ... 2010 a serious blood transfusion related complication. Application The riboflavin and UV light method ... more details
Infobox disease Name Ariboflavinosis Image Riboflavin.svg Caption riboflavin DiseasesDB ICD10 ICD10 E 53 e 50 ICD9 ICD9 266.0 ICDO OMIM MedlinePlus eMedicineSubj eMedicineTopic MeshID Ariboflavinosis pronounced AY rybo flayvin OH sis is the medical condition caused by deficiency of riboflavin vitamin B sub 2 sub . Ariboflavinosis is most often seen in association with protein energy malnutrition , and also ... Recommended Daily Allowance RDA for riboflavin ranges from 1.1 to 1.3 milligrams per day for healthy adults to as high as 1.6 mg day for pregnant or nursing women. Causes The most common cause of riboflavin ... limited quantities of riboflavin containing foods such as meat s, egg food egg s, milk , cheese , yogurt , leafy green vegetable s and whole grain s. Riboflavin deficiency can also occur in those with impaired liver function, which prevents proper use of the vitamin. Borderline riboflavin deficiency ... acidosis . An animal model of riboflavin kinase deficiency has been identified. ref name pmid19641494 cite journal author Yazdanpanah B title Riboflavin kinase couples TNF receptor 1 to NADPH oxidase ... of riboflavin deficiency typically include sore throat with redness and swelling of the mouth and throat ... red blood cell count with normal cell size and hemoglobin content normochromic normocytic anemia . Riboflavin ... of riboflavin, leading to deficiency if not monitored closely. Persons with chronic alcoholism can have impaired absorption of riboflavin and other vitamins such as thiamine see Wernicke s encephalopathy ... incidence of esophageal cancer , have shown some relationship between chronic riboflavin deficiency and the onset of esophageal malignancies. One study of pregnant women has found that riboflavin deficient ..., Fr hauf J, Schulz M, Chiwora FM, Volz J, Becker K title Riboflavin deficiency and preeclampsia journal ... which includes an adequate amount of riboflavin. In cases related to weakened liver function, intravenous ... infocenter vitamins riboflavinRiboflavin at the Linus Pauling Institute Nutritional pathology Category ... more details
wiktionary E101 E101 may refer to Riboflavin , food additive which has been assigned E number Flavin mononucleotide , biomolecule produced from riboflavin European route E101 , autoroad of International E road network between Kiev and Moscow E101 , a form for stating applicable legislation within the EEA and Switzerland Letter NumberCombDisambig de E101 it E101 nl E101 pl E101 ujednoznacznienie ru E101 sv E101 ... more details
enzyme Name flavin reductase EC number 1.5.1.30 CAS number 56626 29 0 IUBMB EC number 1 5 1 30 GO code 0042602 image width caption In enzymology , a flavin reductase EC number 1.5.1.30 is an enzyme that catalysis catalyzes the chemical reaction reduced riboflavin NADP sup sup math rightleftharpoons math riboflavin NADPH H sup sup Thus, the two substrate biochemistry substrates of this enzyme are reduced riboflavin and nicotinamide adenine dinucleotide phosphate NADP sup sup , whereas its 3 product chemistry products are riboflavin , nicotinamide adenine dinucleotide phosphate NADPH , and hydrogen ion H sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH NH group of donors with NAD sup sup or NADP sup sup as acceptor. The systematic name of this enzyme class is reduced riboflavin NADP oxidoreductase . Other names in common use include NADPH flavin oxidoreductase , riboflavin mononucleotide reduced nicotinamide adenine dinucleotide , phosphate reductase , flavin mononucleotide reductase , flavine mononucleotide reductase , FMN reductase NADPH , NADPH dependent FMN reductase , NADPH flavin reductase , NADPH FMN reductase , NADPH specific FMN reductase , riboflavin mononucleotide reductase , riboflavine mononucleotide reductase , NADPH2 dehydrogenase flavin , and NADPH2 riboflavin oxidoreductase . References reflist 1 cite journal author Lo H, Reeves RE date 1980 title Purification and properties of NADPH flavin oxidoreductase from Entamoeba histolytica journal Mol. Biochem. Parasitol. volume 2 pages 23&ndash 30 pmid 6258069 doi 10.1016 0166 6851 80 90045 6 issue 1 cite journal author Yubisui T, Tamura M, Takeshita M date 1987 title Characterization of a second form of NADPH flavin reductase purified from human erythrocytes journal Biochem. Int. volume 15 pages 1&ndash 8 pmid 3453680 issue 1 1.5 enzyme stub Category EC 1.5.1 Category NADPH dependent enzymes Category Enzymes of unknown structure it Flavina reduttasi ja ... more details
enzyme Name riboflavinase EC number 3.5.99.1 CAS number 9024 79 7 IUBMB EC number 3 5 99 1 GO code 0050258 image width caption In enzymology , a riboflavinase EC number 3.5.99.1 is an enzyme that catalysis catalyzes the chemical reaction riboflavin H sub 2 sub O math rightleftharpoons math ribitol lumichrome Thus, the two substrate biochemistry substrates of this enzyme are riboflavin and water H sub 2 sub O , whereas its two product chemistry products are ribitol and lumichrome . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is riboflavin hydrolase . This enzyme participates in riboflavin metabolism . References reflist 1 cite journal author Yanagita T and Foster JW year 1956 title A bacterial riboflavin hydrolase journal J. Biol. Chem. volume 221 pages 593&ndash 607 pmid 13357454 issue 2 Carbon nitrogen non peptide hydrolases Category EC 3.5.99 Category Enzymes of unknown structure hydrolase stub ... more details
Orphan date September 2011 Infobox protein family Symbol DHBP synthase Name DHBP synthase image PDB 1g58 EBI.jpg width caption crystal structure of 3,4 dihydroxy 2 butanone 4 phosphate synthase gold derivative Pfam PF00926 Pfam clan InterPro IPR000422 SMART PROSITE MEROPS SCOP 1iez TCDB OPM family OPM protein CAZy CDD In molecular biology, 3,4 dihydroxy 2 butanone 4 phosphate synthase DHBP synthase RibB EC number 4.1.99.12 is an enzyme which catalysis catalyses the conversion of ribulose 5 phosphate D ribulose 5 phosphate to formate and 3,4 dihydroxy 2 butanone 4 phosphate , the latter serving as the biosynthetic precursor for the xylene ring of riboflavin . ref name pmid9211332 cite journal author Richter G, Krieger C, Volk R, Kis K, Ritz H, Gotze E, Bacher A title Biosynthesis of riboflavin 3,4 dihydroxy 2 butanone 4 phosphate synthase journal Meth. Enzymol. volume 280 issue pages 374 82 year 1997 pmid 9211332 doi 10.1016 S0076 6879 97 80128 0 url ref In Photobacterium leiognathi , the riboflavin synthesis genes ribB DHBP synthase , ribE riboflavin synthase , ribH lumazone synthase and ribA GTP cyclohydrolase II all reside in the lux operon . ref name pmid11396941 cite journal author Lin JW, Chao YF, Weng SF title Riboflavin synthesis genes ribE, ribB, ribH, ribA reside in the lux operon of Photobacterium leiognathi journal Biochem. Biophys. Res. Commun. volume 284 issue 3 pages 587 95 year 2001 month June pmid 11396941 doi 10.1006 bbrc.2001.5013 url ref RibB is sometimes found as a bifunctional enzyme with GTP cyclohydrolase II that catalyses the first committed step in the biosynthesis of riboflavin. No sequence biology sequence s with significant homology to DHBP synthase are found in the metazoa . References reflist InterPro content IPR000422 Category Protein families ... more details
RIBO can stand for Radioactive Ion Beam Optimization Rotamah Island Bird Observatory Ribo is the nickname of football player Rivaldo ribo is a combining form referring to the sugar ribose or some compound with a ribose component, including ribonucleic acid RNA riboflavin vitamin B sub 2 sub disambig ... more details
enzyme Name FAD AMP lyase cyclizing EC number 4.6.1.15 CAS number 208349 48 8 IUBMB EC number 4 6 1 15 GO code image width caption In enzymology , a FAD AMP lyase cyclizing EC number 4.6.1.15 is an enzyme that catalysis catalyzes the chemical reaction FAD math rightleftharpoons math AMP riboflavin cyclic 4 ,5 phosphate Hence, this enzyme has one substrate biochemistry substrate , FAD , and two product chemistry products , adenosine monophosphate AMP and riboflavin cyclic 4 ,5 phosphate . This enzyme belongs to the family of lyase s, specifically the class of phosphorus oxygen lyases. The systematic name of this enzyme class is FAD AMP lyase riboflavin cyclic 4 ,5 phosphate forming . Other names in common use include FMN cyclase , and FAD AMP lyase cyclic FMN forming . References reflist 1 cite journal author Cameselle JC date 1998 title Enzymic formation of riboflavin 4 ,5 cyclic phosphate from FAD evidence for a specific low Km FMN cyclase in rat liver1 journal Biochem. J. volume 330 pages 881&ndash 8 pmid 9480905 last2 Pinto first2 RM last3 Costas first3 MJ last4 Aavalos first4 M last5 Canales first5 J last6 Cabezas first6 A last7 Cameselle first7 JC pmc 1219220 issue Pt 2 cite journal author Cameselle JC date 2001 title Purification, characterization, and substrate and inhibitor structure activity studies of rat liver FAD AMP lyase cyclizing preference for FAD and specificity for splitting ribonucleoside diphosphate X into ribonucleotide and a five atom cyclic phosphodiester of X, either a monocyclic compound or a cis bicyclic phosphodiester pyranose fusion journal Biochemistry. volume 40 pages 13710&ndash 22 pmid 11695920 doi 10.1021 bi0157159 last2 Pinto first2 RM last3 Fraiz first3 F last4 Canales first4 J last5 Gonz lez Santiago first5 S last6 Cameselle first6 JC issue 45 enzyme stub Phosphorus oxygen lyases Category EC 4.6.1 Category Enzymes of unknown structure ... more details
enzyme Name FMN adenylyltransferase EC number 2.7.7.2 CAS number 9026 37 3 IUBMB EC number 2 7 7 2 GO code 0003919 image width caption In enzymology , a FMN adenylyltransferase EC number 2.7.7.2 is an enzyme that catalysis catalyzes the chemical reaction ATP FMN math rightleftharpoons math diphosphate FAD Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and flavin mononucleotide FMN , whereas its two product chemistry products are diphosphate and FAD . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ATP FMN adenylyltransferase . This enzyme participates in riboflavin metabolism . Other names Other names in common use include FAD pyrophosphorylase riboflavin mononucleotide adenylyltransferase adenosine triphosphate riboflavin mononucleotide transadenylase adenosine triphosphate riboflavine mononucleotide transadenylase FAD synthetase riboflavin adenine dinucleotide pyrophosphorylase riboflavine References reflist 1 cite journal author GIRI KV, RAO NA, CAMA HR, KUMAR SA year 1960 title Studies on flavinadenine dinucleotide synthesizing enzyme in plants journal Biochem. J. volume 75 pages 381&ndash 6 pmid 13828163 pmc 1204435 cite journal author Schrecker AW and Kornberg A year 1950 title Reversible enzymatic synthesis of flavin adenine dinucleotide journal J. Biol. Chem. volume 182 pages 795&ndash 803 pmid 19994476 issue 2 Category EC 2.7.7 Category Enzymes of unknown structure enzyme stub de FAD Synthetase ... more details
Lumazine synthase LS or more specifically 6,7 dimethyl 8 ribityllumazine synthase is a protein enzyme also known as riboflavin synthase which catalysis catalyses the penultimate step in the Biosynthesis synthesis of riboflavin . This protein is found in bacteria , archaea , plants and fungi , with a number of different quaternary structure s. However each of these proteins is homology biology homologous , sharing a common tertiary structure subunit fold . Icosahedral 60 subunit assemblies are found in spinach , Bacillus subtilis , and Aquifex aeolicus while pentamer ic 5 subunit assemblies are found in Brucella abortus , Saccharomyces cerevisiae and certain fungi. References cite journal author Fornasari MS, Laplagne DA, Frankel N, Cauerhff AA, Goldbaum FA, Echave J title Sequence determinants of quaternary structure in lumazine synthase journal Mol. Biol. Evol. volume 21 issue 1 pages 97 107 year 2004 pmid 14523158 doi 10.1093 molbev msg244 url http mbe.oxfordjournals.org cgi content abstract 21 1 97 br Category Enzymes enzyme stub ... more details
Pfam box Symbol Folate rec Name Folate receptor family image width caption Pfam PF03024 InterPro IPR004269 SMART Prosite SCOP TCDB OPM family OPM protein PDB Folate receptors bind folate and reduced folic acid derivatives and mediates delivery of tetrahydrofolate to the interior of cells. It is then converted from monoglutamate to polyglutamate forms such as 5 methyltetrahydrofolate as only monoglutamate forms can be transported across cell membranes. Polyglutamate forms are biologically active enzymatic cofactors required for many folate dependent processes such as folate dependent one carbon metabolism. These proteins are attached to the membrane by a GPI anchor . A riboflavin binding protein required for the transport of riboflavin to the developing oocyte in chicken also belong to this family. Human proteins from this family include FOLR1 Folate receptor 1 adult , FOLR2 Folate receptor 2 fetal , FOLR3 and RTBDN . InterPro content IPR004269 Category Protein families Category Membrane proteins ... more details
form in which riboflavin is found in cell biology cell s and biological tissue tissues . It requires more energy to produce, but is more soluble than riboflavin. Food additive Flavin mononucleotide ... related food dye, is riboflavin 5 phosphate sodium salt, which consists mainly of the monosodium salt of the 5 monophosphate ester of riboflavin. It is rapidly turned to free riboflavin after ingestion ... lt Riboflavin 5 fosfatas hu Riboflavin 5 foszf t nl Riboflavine 5 fosfaat ja oc Flavina ... more details
Image Pyrimidin.svg thumb right Pyrimidine Pyrimidinediones are a class of chemical compounds characterized by a pyrimidine ring substituted with two carbonyl groups. Examples include naturally occurring metabolite s class wikitable Trivial name IUPAC name Structure Pathway Uracil Pyrimidine 2,4 1 H ,3 H dione Image Uracil.svg Pyrimidine biosynthesis Thymine 5 Methylpyrimidine 2,4 1 H ,3 H dione File Thymine chemical structure.png 150px Pyrimidine biosynthesis 5,6 Diaminopyrimidine 2,4 1 H ,3 H dione Riboflavin biosynthesis and drugs Image Primidone.png thumb right Primidone Fluorouracil Idoxuridine Primidone Trifluridine References http www.biam2.org www Cla20291.html Classe PYRIMIDINEDIONE heterocyclic stub Category Pyrimidinediones fr Pyrimidinedione ja sr Pirimidindion zh ... more details
cleanup date June 2011 Lipoflavonoid or Lipo flavonoid is a Property proprietary , Over the counter substance over the counter , nutrient formula created in 1961, by DSE Healthcare Solutions, intended to help combat tinnitus sounds in the ears . It has not been approved by the Food and Drug Administration for this purpose. Composition and effects Lipoflavonoid is sold as a dietary supplement . It is composed of eriodictyol glycoside a bioflavonoid found naturally in the peel of lemons and the following vitamins vitamin B6 and vitamin B12 B12 B complex , vitamin C , niacin , riboflavin , thiamine , choline , inositol , and pantothenic acid . cn date June 2011 . References reflist Category Dietary supplements ... more details
Infobox protein family Symbol FAD oxidase C Name FAD linked oxidases, C terminal domain image PDB 1wve EBI.jpg width caption p cresol methylhydroxylase alteration of the structure of the flavoprotein subunit upon its binding to the cytochrome subunit Pfam PF02913 Pfam clan CL0277 InterPro IPR004113 SMART PROSITE MEROPS SCOP 1ahu TCDB OPM family OPM protein CAZy CDD In molecular biology FAD oxidases are a family of FAD dependent oxidoreductases . They are flavoprotein s that contain a covalently bound FAD group which is attached to a histidine via an 8 alpha N3 histidyl riboflavin linkage. The region around the histidine that binds the FAD group is conserved sequence conserved in these enzyme s. ref name pmid9141139 Cite pmid 9141139 ref References reflist InterPro content IPR004113 Category Protein domains ... more details
saved book title subtitle cover image cover color Vitamins All about Vitamins 1 General Information Vitamin 2 Vitamin A Vitamin A Hypervitaminosis A 3 B Vitamins General Information B vitamins 3.a Vitamin B1 Thiamine Beriberi Wernicke Korsakoff syndrome 3.b Vitamin B2 Riboflavin Ariboflavinosis 3.c Vitamin B3 Niacin Pellagra 3.d Vitamin B5 Pantothenic acid 3.e Vitamin B6 Vitamin B6 3.f Vitamin B7 Biotin 3.g Vitamin B9 Folic acid 3.h Vitamin B12 Vitamin B12 4 Vitamin C Vitamin C 5 Vitamin D Vitamin D 6 Vitamin E Vitamin E 7 Vitamin K Vitamin K ... more details
Vecon is a concentrated vegetable Stock food stock , used for flavouring dishes. It is popular amongst vegetarians, as it can be used to replace other stock in soups, stews, etc. It is fortified with a number of vitamins that are rarer in vegetarian or vegan diets, such as iron and vitamin B12 vitamin B sub 12 sub . It s also often used sparingly as a spread much like marmite is on toast. Ingredients Hydrolysed vegetable soya and maize , protein, water, dehydrated vegetable powder onion, celery, tomato, parsley, spinach, garlic yeast extract, red pepper extract 1 , carrot extract 1 , kelp,ferrous sulphate, vitamin C, niacin, beta carotene ground black pepper, riboflavin, thiamin, vitamin B12. ref name GoodnessDirect cite web title Vecon Concentrated Vegetable Stock 225g url http www.goodnessdirect.co.uk cgi local frameset detail 600381 Vecon Concentrated Vegetable Stock 225g.html work Goodness Direct.co.uk accessdate 27 September 2011 ref ref name VeggieStuff cite web title Vecon Concentrated Vegetable Stock 225g url http www.veggiestuff.com acatalog vecon concentrated vegetable stock.html aMOD030 work VeggieStuff.com accessdate 27 September 2011 ref Nutritional Information Nutritional Information per 100g Energy 531kJ 125kcal, Protein 16.6g, Carbohydrate 13.9g as sugars 2.9g, Fat 1.3g, as saturates 0.0g, Fibre 3.4g, Sodium 16.5g, Vitamin A 833.00ug, Vitamin C 100.00mg, Thiamin Vit B 5.00mg, Riboflavin Vit B2 6.00mg, Niacin 50.00mg , Vitamin B12 13.00ug, Iron 70.00mg ref name GoodnessDirect ref name VeggieStuff Distribution Australia Kintra Foods ref cite web title Kintra Foods Home Page url http www.kintrafoods.com.au work KintraFoods.com.au accessdate 27 September 2011 ref References Reflist Category Vegetarian cuisine Category Food ingredients Ingredient stub he ... more details
chembox verifiedrevid 443355767 ImageFile 6,7 dimethyl 8 ribityllumazine.svg ImageSize IUPACName OtherNames Section1 Chembox Identifiers ChemSpiderID Ref chemspidercite correct chemspider ChemSpiderID 147805 InChI 1 C13H18N4O6 c1 5 6 2 17 3 7 19 10 21 8 20 4 18 11 9 14 5 12 22 16 13 23 15 11 h7 8,10,18 21H,3 4H2,1 2H3, H,16,22,23 t7 ,8 ,10 m0 s1 InChIKey SXDXRJZUAJBNFL XKSSXDPKBB StdInChI Ref stdinchicite correct chemspider StdInChI 1S C13H18N4O6 c1 5 6 2 17 3 7 19 10 21 8 20 4 18 11 9 14 5 12 22 16 13 23 15 11 h7 8,10,18 21H,3 4H2,1 2H3, H,16,22,23 t7 ,8 ,10 m0 s1 StdInChIKey Ref stdinchicite correct chemspider StdInChIKey SXDXRJZUAJBNFL XKSSXDPKSA N CASNo 5118 16 1 PubChem 168989 ChEBI Ref ebicite correct EBI ChEBI 17601 SMILES O C2 N C 1 N C C N C 1C O N2 C C C C H O C H O C H O CO MeSHName 6,7 dimethyl 8 ribityllumazine Section2 Chembox Properties Formula C sub 13 sub H sub 18 sub N sub 4 sub O sub 6 sub MolarMass 326.305 g mol Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition 6,7 Dimethyl 8 ribityllumazine is a precursor for riboflavin . It is acted upon by riboflavin synthase . DEFAULTSORT Dimethyl 8 ribityllumazine, 6,7 biochem stub Category Pteridines Category Imides fa ja 6,7 8 ... more details
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