Thiamine mono nitrate is a synthetic form of vitamin B1 . Allergic Reaction Health Concerns Liver Disease References University of Maryland Medical Center Vitamin B1 Journal of Nutrition Bioavailability for Rats of Thiamin in Whole Wheat and Thiamin Restored White Bread G. Ranhotra et al. May 1985 MedlinePlus Thiamine External link http www.livestrong.com article 313249 the side effects of thiamine mononitrate ixzz1iXetnLU1 Livestrong article Category Food additives ... more details
enzyme Name thiamin kinase EC number 2.7.1.89 CAS number 62213 38 1 IUBMB EC number 2 7 1 89 GO code 0019165 image width caption In enzymology , a thiamine kinase EC number 2.7.1.89 is an enzyme that catalysis catalyzes the chemical reaction ATP thiamine math rightleftharpoons math ADP thiamine phosphate Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and thiamine , whereas its two product chemistry products are adenosine diphosphate ADP and thiamine phosphate . 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 ATP thiamine phosphotransferase . Other names in common use include thiamin kinase phosphorylating , thiamin phosphokinase , ATP thiamin phosphotransferase , and thiamin kinase . This enzyme participates in thiamine metabolism . References reflist 1 cite journal author Iwashima A, Nishino H, Nose Y date 1972 title Conversion of thiamine to thiamine monophosphate by cell free extracts of Escherichia coli journal Biochim. Biophys. Acta. volume 258 pages 333&ndash 6 pmid 4550803 issue 1 enzyme stub Category EC 2.7.1 Category Enzymes of unknown structure ... more details
enzyme Name thiamin diphosphate kinase EC number 2.7.4.15 CAS number 9075 79 0 IUBMB EC number 2 7 4 15 GO code 0050331 image width caption In enzymology , a thiamine diphosphate kinase is an enzyme involved in thiamine metabolism . It catalysis catalyzes the chemical reaction thiamine diphosphate ATP math rightleftharpoons math thiamine triphosphate ADP Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and thiamine diphosphate , whereas its two product chemistry products are adenosine diphosphate ADP and thiamine triphosphate . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing groups phosphotransferase s with a phosphate group as acceptor. The systematic name of this enzyme class is ATP thiamine diphosphate phosphotransferase . Other names in common use include ATP thiamin diphosphate phosphotransferase , TDP kinase , thiamin diphosphate kinase , thiamin diphosphate phosphotransferase , thiamin pyrophosphate kinase , thiamine diphosphate kinase , and protein bound thiamin diphosphate ATP phosphoryltransferase . See also Thiamine triphosphatase References reflist 1 cite journal author Itokawa Y, Cooper JR date 1968 title The enzymatic synthesis of triphosphothiamin journal Biochim. Biophys. Acta. volume 158 pages 180&ndash 2 pmid 5661031 issue 1 cite journal author Kikuchi M and Ikawa T date Tokyo title Presence of an enzyme mediating transfer of phosphate from thiamine triphosphate to ADP in germinating maize journal Bot. volume Mag. pages 193&ndash 205 Kinases enzyme stub Category EC 2.7.4 Category Enzymes of unknown structure ... more details
enzyme Name thiamin diphosphokinase EC number 2.7.6.2 CAS number 9026 24 8 IUBMB EC number 2 7 6 2 GO code 0004788 image width caption In enzymology , a thiamine diphosphokinase EC number 2.7.6.2 is an enzyme that catalysis catalyzes the chemical reaction ATP thiamine math rightleftharpoons math AMP thiamine diphosphate Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and thiamine , whereas its two product chemistry products are adenosine monophosphate AMP and thiamine diphosphate . This enzyme belongs to the family of transferase s, specifically those transferring two phosphorus containing groups diphosphotransferase s . The systematic name of this enzyme class is ATP thiamine diphosphotransferase . Other names in common use include thiamin kinase , thiamine pyrophosphokinase , ATP thiamin pyrophosphotransferase , thiamin pyrophosphokinase , thiamin pyrophosphotransferase , thiaminokinase , thiamin ATP pyrophosphotransferase , and TPTase . This enzyme participates in thiamine metabolism . Structural studies As of late 2007, 6 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1IG0 , PDB link 1IG3 , PDB link 2F17 , PDB link 2G9Z , PDB link 2HH9 , and PDB link 2OMK . References reflist 1 cite journal author Leuthardt F and Nielsen H date 1952 title Phosphorylation biologique de la thiamine journal Helv. Chim. Acta volume 35 issue 4 pages 1196&ndash 1209 doi 10.1002 hlca.19520350415 cite journal author Shimazono N, Mano Y, Tanaka R and Kajiro Y date Tokyo title Mechanism of transpyrophosphorylation with thiamine pyrophosphokinase journal J. volume Biochem. pages 959&ndash 961 cite journal author Steyn Parve EP date 1952 title Partial purification and properties of thiaminokinase from yeast journal Biochim. Biophys. Acta volume 8 pages 310&ndash 324 doi 10.1016 0006 3002 52 90046 2 pmid 14934742 Kinases Metabolism of vitamins, coenzymes, and cofactors ... more details
enzyme Name thiamin phosphate kinase EC number 2.7.4.16 CAS number 9068 23 9 IUBMB EC number 2 7 4 16 GO code 0009030 image width caption In enzymology , a thiamine phosphate kinase EC number 2.7.4.16 is an enzyme that catalysis catalyzes the chemical reaction ATP thiamine phosphate math rightleftharpoons math ADP thiamine diphosphate Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and thiamine phosphate , whereas its two product chemistry products are adenosine diphosphate ADP and thiamine diphosphate . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing groups phosphotransferase s with a phosphate group as acceptor. The systematic name of this enzyme class is ATP thiamine phosphate phosphotransferase . Other names in common use include thiamin monophosphate kinase , thiamin monophosphatase , and thiamin monophosphokinase . This enzyme participates in thiamine metabolism . Structural studies As of late 2007, only one tertiary structure structure has been solved for this class of enzymes, with the Protein Data Bank PDB accession code PDB link 1VQV . References reflist 1 cite journal author Nishino H date Tokyo title Biogenesis of cocarboxylase in Escherichia coli. Partial purification and some properties of thiamine monophosphate kinase journal J. volume Biochem. pages 1093&ndash 100 pmid 4567662 issue 5 enzyme stub Category EC 2.7.4 Category Enzymes of known structure ... more details
enzyme Name 2 oxoglutarate decarboxylase EC number 4.1.1.71 CAS number 37205 42 8 IUBMB EC number 4 1 1 71 GO code 0008683 image width caption In enzymology , a 2 oxoglutarate decarboxylase EC number 4.1.1.71 is an enzyme that catalysis catalyzes the chemical reaction 2 oxoglutarate math rightleftharpoons math succinate semialdehyde CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , 2 oxoglutarate , and two product chemistry products , succinate semialdehyde and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of lyase s, specifically the carboxy lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is 2 oxoglutarate carboxy lyase succinate semialdehyde forming . Other names in common use include oxoglutarate decarboxylase , alpha ketoglutarate decarboxylase , alpha ketoglutaric decarboxylase , oxoglutarate decarboxylase , pre 2 oxoglutarate decarboxylase , and 2 oxoglutarate carboxy lyase . It employs one cofactor biochemistry cofactor , thiamin diphosphate . References reflist 1 cite journal author Shigeoka S, Onishi T, Maeda K, Nakano Y and Kitaoka S date 1986 title Occurrence of thiamin pyrophosphate dependent 2 oxoglutarate decarboxylase in mitochondria of Euglena gracilis journal FEBS Lett. volume 195 pages 43&ndash 47 doi 10.1016 0014 5793 86 80126 0 4.1 enzyme stub Category EC 4.1.1 Category Thiamine enzymes Category Enzymes of unknown structure ... more details
italic title Taxobox name Mucor hiemalis regnum Fungi phylum Zygomycota classis Zygomycetes subclassis Incertae sedis ordo Mucorales familia Mucoraceae genus Mucor species M. hiemalis binomial Mucor hiemalis binomial authority Wehmer, 1903 Mucor hiemalis is a fungus fungal plant pathogen. Morphology and Cell biology cell structure M. hiemalis grows in expanding gray colonies. It grows branched sporangiophores that yielding yellow to dark brown sporangia which can mate to form black brown, spiny zygospore s. Physiology M. hiemalis is nitrate positive and requires thiamin to grow. External links http www.speciesfungorum.org Names Names.asp Index Fungorum http nt.ars grin.gov fungaldatabases USDA ARS Fungal Database Category Plant pathogens and diseases Category Zygomycota fungus stub plant disease stub ... more details
title Radical phosphate transfer mechanism for the thiamin diphosphate and FAD dependent pyruvate ... transfer to acetyl thiamin diphosphate via a transient FAD semiquinone hydroxyethyl ThDP radical ... 40 1.2 enzyme stub Category EC 1.2.3 Category Flavin enzymes Category Thiamin diphosphate enzymes ... 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
enzyme Name phenylglyoxylate dehydrogenase acylating EC number 1.2.1.58 CAS number 205510 78 7 IUBMB EC number 1 2 1 58 GO code 0047110 image width caption In enzymology , a phenylglyoxylate dehydrogenase acylating EC number 1.2.1.58 is an enzyme that catalysis catalyzes the chemical reaction phenylglyoxylate NAD sup sup CoA SH math rightleftharpoons math benzoyl S CoA CO sub 2 sub NADH The three substrate biochemistry substrates of this enzyme are phenylglyoxylate , nicotinamide adenine dinucleotide NAD sup sup , and CoA SH , whereas its 3 product chemistry products are benzoyl S CoA , carbon dioxide CO sub 2 sub , and nicotinamide adenine dinucleotide NADH . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the aldehyde or oxo group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is phenylglyoxylate NAD oxidoreductase . It has 3 cofactor biochemistry cofactors FAD , Thiamin diphosphate , and Iron sulfur . References reflist 1 cite journal author Hirsch W, Schagger H, Fuchs G date 1998 title Phenylglyoxylate NAD oxidoreductase CoA benzoylating , a new enzyme of anaerobic phenylalanine metabolism in the denitrifying bacterium Azoarcus evansii journal Eur. J. Biochem. volume 251 pages 907&ndash 15 pmid 9490067 doi 10.1046 j.1432 1327.1998.2510907.x issue 3 1.2 enzyme stub Category EC 1.2.1 Category NADH dependent enzymes Category Flavin enzymes Category Thiamin diphosphate enzymes Category Iron sulfur enzymes Category Enzymes of unknown structure it Fenilgliossilato deidrogenasi acilante ja ... more details
enzyme Name pyruvate dehydrogenase cytochrome EC number 1.2.2.2 CAS number 9079 84 9 IUBMB EC number 1 2 2 2 GO code 0008985 image width caption In enzymology , a pyruvate dehydrogenase cytochrome EC number 1.2.2.2 is an enzyme that catalysis catalyzes the chemical reaction pyruvate ferricytochrome b sub 1 sub H sub 2 sub O math rightleftharpoons math acetate CO sub 2 sub ferrocytochrome b sub 1 sub The 3 substrate biochemistry substrates of this enzyme are pyruvate , ferricytochrome b1 , and water H sub 2 sub O , whereas its 3 product chemistry products are acetate , carbon dioxide CO sub 2 sub , and ferrocytochrome b1 . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the aldehyde or oxo group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is pyruvate ferricytochrome b1 oxidoreductase . Other names in common use include pyruvate dehydrogenase , pyruvic dehydrogenase , pyruvic cytochrome b1 dehydrogenase , pyruvate ubiquinone 8 oxidoreductase , and pyruvate oxidase ambiguous . This enzyme participates in pyruvate metabolism . It has 2 cofactor biochemistry cofactors FAD , and Thiamin diphosphate . References reflist 1 cite journal author Williams FR and Hager LP date 1961 title A crystalline flavin pyruvate oxidase journal J. Biol. Chem. volume 236 pages PC36&ndash PC37 cite journal author Koland JG, Gennis RB date 1982 title Identification of an active site cysteine residue in Escherichia coli pyruvate oxidase journal J. Biol. Chem. volume 257 pages 6023&ndash 7 pmid 7042705 issue 11 1.2 enzyme stub Category EC 1.2.2 Category Flavin enzymes Category Thiamin diphosphate enzymes Category Enzymes of unknown structure it Piruvato deidrogenasi citocromo ... more details
enzyme Name tartronate semialdehyde synthase EC number 4.1.1.47 CAS number 9027 24 1 IUBMB EC number 4 1 1 47 GO code 0009028 image width caption In enzymology , a tartronate semialdehyde synthase EC number 4.1.1.47 is an enzyme that catalysis catalyzes the chemical reaction 2 glyoxylate math rightleftharpoons math tartronate semialdehyde CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , glyoxylate , and two product chemistry products , tartronate semialdehyde and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of lyase s, specifically the carboxy lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is glyoxylate carboxy lyase dimerizing tartronate semialdehyde forming . Other names in common use include tartronate semialdehyde carboxylase , glyoxylate carbo ligase , glyoxylic carbo ligase , hydroxymalonic semialdehyde carboxylase , tartronic semialdehyde carboxylase , glyoxalate carboligase , and glyoxylate carboxy lyase dimerizing . This enzyme participates in glyoxylate and dicarboxylate metabolism . It has 2 cofactor biochemistry cofactors FAD , and Thiamin diphosphate . References reflist 1 cite journal author GUPTA NK, VENNESLAND B date 1964 title GLYOXYLATE CARBOLIGASE OF ESCHERICHIA COLI A FLAVOPROTEIN journal J. Biol. Chem. volume 239 pages 3787&ndash 9 pmid 14257608 cite journal author BARKULIS SS, KRAKOW G date 1956 title Conversion of glyoxylate to hydroxypyruvate by extracts of Escherichia coli journal Biochim. Biophys. Acta. volume 21 pages 593&ndash 4 pmid 13363977 doi 10.1016 0006 3002 56 90208 6 issue 3 Category EC 4.1.1 Category Flavin enzymes Category Thiamin diphosphate enzymes Category Enzymes of unknown structure Category Article Feedback 5 4.1 enzyme stub ... more details
enzyme Name 1 deoxy D xylulose 5 phosphate synthase EC number 2.2.1.7 CAS number 202218 79 9 IUBMB EC number 2 2 1 7 GO code 0008661 image width caption In enzymology , a 1 deoxy D xylulose 5 phosphate synthase EC number 2.2.1.7 is an enzyme that catalysis catalyzes the chemical reaction pyruvate D glyceraldehyde 3 phosphate math rightleftharpoons math 1 deoxy D xylulose 5 phosphate CO sub 2 sub Thus, the two substrate biochemistry substrates of this enzyme are pyruvate and D glyceraldehyde 3 phosphate , whereas its two product chemistry products are 1 deoxy D xylulose 5 phosphate and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of transferase s, specifically those transferring aldehyde or ketone ketonic groups transaldolases and transketolases, respectively . The systematic name of this enzyme class is pyruvate D glyceraldehyde 3 phosphate acetaldehydetransferase decarboxylating . Other names in common use include 1 deoxy D xylulose 5 phosphate pyruvate lyase carboxylating , and DXP synthase . This enzyme participates in biosynthesis of steroids . Structural studies As of late 2007, two tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 2O1S and PDB link 2O1X . References reflist 1 cite journal author SV, Begley TP, Bringer Meyer S, Sahm H date 1997 title Identification of a thiamin dependent synthase in Escherichia coli required for the formation of the 1 deoxy D xylulose 5 phosphate precursor to isoprenoids, thiamin, and pyridoxol journal Proc. Natl. Acad. Sci. U.S.A. volume 94 pages 12857&ndash 62 pmid 9371765 doi 10.1073 pnas.94.24.12857 issue 24 pmc 24228 cite journal author Kuzuyama T, Takagi M, Takahashi S, Seto H date 2000 title Cloning and characterization of 1 deoxy D xylulose 5 phosphate synthase from Streptomyces sp. Strain CL190, which uses both the mevalonate and nonmevalonate pathways for isopentenyl diphosphate biosynthesis journal J. Bacteriol. volume 182 ... more details
PBB geneid 27010 Thiamin pyrophosphokinase 1 is an enzyme that in humans is encoded by the TPK1 gene . ref name pmid11342111 cite journal author Nosaka K, Onozuka M, Kakazu N, Hibi S, Nishimura H, Nishino H, Abe T title Isolation and characterization of a human thiamine pyrophosphokinase cDNA journal Biochim Biophys Acta volume 1517 issue 2 pages 293 7 year 2001 month May pmid 11342111 pmc doi ref ref name entrez cite web title Entrez Gene TPK1 thiamin pyrophosphokinase 1 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 27010 accessdate ref The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text This gene encodes a protein, that exists as a homodimer, which catalyzes the conversion of thiamine to thiamine pyrophosphate. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. ref name entrez References reflist Further reading refbegin 2 PBB Further reading citations cite journal author Egi Y title Identification, purification and reconstitution of thiamin metabolizing enzymes in human red blood cells journal Biochim. Biophys. Acta volume 1160 issue 2 pages 171 8 year 1992 pmid 1332781 doi 10.1016 0167 4838 92 90004 W author separator , author2 Koyama S author3 Shioda T display authors 3 last4 Yamada first4 K last5 Kawasaki first5 T cite journal author Bohn H, Winckler W title Isolation and characterization ... metadata. cite journal author Nosaka K title Molecular cloning and expression of a mouse thiamin ... Zhao R, Gao F, Goldman ID title Molecular cloning of human thiamin pyrophosphokinase journal Biochim ... Onozuka M, Nosaka K title Steady state kinetics and mutational studies of recombinant human thiamin ... characterization of placental protein 20 PP20 human thiamin pyrophosphokinase hTPK journal Placenta ... region of the human thiamin pyrophosphokinase gene journal J. Nutr. Sci. Vitaminol. volume 51 issue ... more details
Image Raisin Wheats.jpg thumb Kellogg s Raisin Wheats Raisin Wheats formerly Raisin Splitz , Raisin Wheatleys are a Kellogg s breakfast cereal , made from shredded wholegrain wheat filled with raisin . It is in bite sized chunks of 3 4in x 1in, and are served in boxes weighing 0.5kg. Its ingredients, as published on the Kellogg s web site 24 May 2006, are Shredded Wholewheat, Raisins 23 , Glycerine, Niacin, Iron, Vitamin B sub 6 sub , Riboflavin B sub 2 sub , Thiamin B sub 1 sub , Folic Acid, Vitamin B sub 12 sub . The cereal has been subsequently manufactured by numerous other suppliers under a generic brand , often in supermarket s own brand range in the United Kingdom, Tesco, Sainsbury s and Waitrose have all produced their own versions of the cereal. External links http www.kelloggs.co.uk products product.asp?id 48 Kellogg s Category Kellogg Company cereals ... more details
ref improve date March 2012 enzyme Name thiamin oxidase EC number 1.1.3.23 CAS number 96779 44 1 IUBMB EC number 1 1 3 23 GO code 0050423 image width caption In enzymology , a thiamine oxidase EC number 1.1.3.23 is an enzyme that catalysis catalyzes the chemical reaction thiamine 2 O sub 2 sub H sub 2 sub O math rightleftharpoons math thiamine acetic acid 2 H sub 2 sub O sub 2 sub The 3 substrate biochemistry substrates of this enzyme are thiamine , oxygen O sub 2 sub , and water H sub 2 sub O , whereas its two product chemistry products are thiamine acetic acid and hydrogen peroxide H sub 2 sub O sub 2 sub . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is thiamine oxygen 5 oxidoreductase . Other names in common use include thiamin dehydrogenase , thiamine dehydrogenase , and thiamin oxygen 5 oxidoreductase . This enzyme participates in thiamine metabolism . It employs one cofactor biochemistry cofactor , FAD . References reflist 1 cite journal author Edmondson DE, Kenney WC, Singer TP date 1976 title Structural elucidation and properties of 8alpha N1 histidyl riboflavin the flavin component of thiamine dehydrogenase and beta cyclopiazonate oxidocyclase journal Biochemistry. volume 15 pages 2937&ndash 45 pmid 8076 doi 10.1021 bi00659a001 issue 14 cite journal author Gomez Moreno C, Edmondson DE date 1985 title Evidence for an aldehyde intermediate in the catalytic mechanism of thiamine oxidase journal Arch. Biochem. Biophys. volume 239 pages 46&ndash 52 pmid 2988447 doi 10.1016 0003 9861 85 90810 0 issue 1 cite journal author Neal RA date 1970 title Bacterial metabolism of thiamine. 3. Metabolism of thiamine to 3 2 methyl 4 amino 5 pyrimidylmethyl 4 methyl thiazole 5 acetic acid thiamine acetic acid by a flavoprotein isolated from a soil microorganism journal J. Biol. Chem. volume 245 pages 2599&ndash 604 pmid 4987737 issue 10 1.1 enzyme stub ... more details
Refimprove date May 2008 Disney Hunny B s Honey Graham was a breakfast cereal made by Kellogg Company Kellogg s & The Walt Disney Company Disney , described by the company as a naturally sweetened honey graham cracker graham cereal. The individual cereal pieces were in the shape of the letter B , with biscuits in the shapes of honey pots, Pooh s head and bees for a limited time, biscuits in the shape of Characters in Winne the Pooh Piglet s head were included It was only available in the 9 ounce oz 255 gram g size. It was classified as kosher dairy. Ingredients Corn meal , graham flour , brown sugar , sugar , salt , high fructose corn syrup , calcium carbonate , wheat starch , honey , baking soda , caramel color , Artificial flavor artificial cream flavor, iron , sodium ascorbate and ascorbic acid vitamin C , Nicotinamide niacinamide , red 40, yellow 5, zinc oxide , blue 1, pyridoxine hydrochloride vitamin B6 vitamin B sub 6 sub , yellow 6, riboflavin vitamin B2 vitamin B sub 2 sub , thiamin hydrochloride vitamin B1 vitamin B sub 1 sub , vitamin A palmitate, Butylated hydroxytoluene BHT preservative , folic acid , turmeric color, vitamin D , and vitamin B12 vitamin B sub 12 sub . Kellogg s food product stub Category Kellogg Company cereals Category Disney merchandise ... more details
Image Hershey s S mores wrapped.jpg right Hershey s S mores wrapper Image Hershey s S mores.jpg thumb 300px Hershey s S mores bar Image Hershey s S mores opened.jpg 300px thumb Hershey s S mores inside Hershey s S mores was a candy bar made by The Hershey Company and introduced in 2003. As the name indicates, the bar was based on s more s, a popular campfire treat. The bar consisted of a layer of graham cracker bits topped with marshmallow and coated with milk chocolate . The S mores bar has been discontinued by the manufacturer. Citation needed date February 2011 Ingredients Listed by weight milk chocolate sugar , milk , cocoa butter , chocolate , soy lecithin , vanillin , sugar , vegetable oil s shea oil, fractionated palm oil , corn syrup , enriched flour wheat flour , niacin , reduced iron , thiamin mononitrate , riboflavin , folic acid , high fructose corn syrup , graham flour , glycerin , maltodextrin , nonfat milk , partially hydrogenated vegetable oil s soybean oil, cottonseed oil , sorbitol , egg white s, brown sugar , natural and artificial flavouring flavors , Leavening agent leavening monocalcium phosphate , sodium bicarbonate , salt , cellulose gel, honey , molasses , malt syrup, annatto , carrageenan , soy lecithin , TBHQ preservative Hershey s confectionery products Category Candy bars Category The Hershey Company brands Category 2003 introductions confection stub ... more details
Image All Bran Buds.jpg right thumb All Bran Buds is a variety of All Bran cereal manufactured by Kellogg Company Kellogg s . It is a wheat bran cereal that is a source of high dietary fiber fiber and psyllium . It is available in the United States and Canada . It used to be available in the United Kingdom during the 1970s. The cereal was available in Ireland until the mid 1980s. Nutrition A 1 3 cup serving 30g, 1.1 oz has 70 calories, 1 g of fat, 24 g of carbohydrates, and 2g of protein. It contains 13g of fiber 3 soluble, 10 insoluble . Ingredients Wheat bran , sugar glucose fructose , psyllium seed husks , corn bran, salt , baking soda , natural colour, vitamins thiamin hydrochloride, d calcium pantothenate, pyridoxine hydrochloride, folic acid , iron , Butylated hydroxytoluene BHT . All Bran Buds is both Kosher and Halal . External links http www.kelloggs.com brand allbran benefits2.shtml All Bran Buds USA http www.kelloggs.ca cgi bin klog canada product.pl?product 20&company 2 All Bran Buds Canada Kellogg s food product stub Category Kellogg Company cereals ... more details
moieties in bacteria . The THI element is an extension of a previously detected thiamin regulatory ... 2002 title Comparative genomics of thiamin biosynthesis in procaryotes. New genes and regulatory ... jbc.M208965200 ref Analysis of operon structures has identified a large number of new candidate thiamin ... is involved in regulation of thiamin biosynthetic gene expression in bacteria journal Proc Natl Acad ... more details
Red Cargo rice is a type of non glutinous long grain rice, similar to brown rice , in that it is unpolished rice, only the color of the bran is red, purple or maroon. Only the husks of the rice grains are removed during the milling process, retaining all the nutrients, vitamins and minerals intact in the bran layer and in the Cereal germ germ . Health and nutritional benefits Red rice is a good source of thiamin Vitamin B1 vitamin B sub 1 sub , riboflavin Vitamin B2 vitamin B sub 2 sub , fibre , iron and calcium . The flavor of cooked red cargo rice is generally more sweet and nutty, and the rice is more chewy than standard white polished rice. Red rice takes longer to cook than white rice, but not as long as brown rice. Soaking the rice in water for at least 30 minutes before cooking produces a softer texture. History The term cargo originates from the idea that this type of rice is exported transported by ship sea in bulk to the importers distributors who then package the rice in small 1 kg bags for the market, unlike white rice which is usually pre packed by exporters into 5, 10 or 25 kg bags. Varieties of rice ingredient stub Category Varieties of rice ... more details
enzyme Name 5 guanidino 2 oxopentanoate decarboxylase EC number 4.1.1.75 CAS number 56831 67 5 IUBMB EC number 4 1 1 75 GO code 0047435 image width caption In enzymology , a 5 guanidino 2 oxopentanoate decarboxylase EC number 4.1.1.75 is an enzyme that catalysis catalyzes the chemical reaction 5 guanidino 2 oxo pentanoate math rightleftharpoons math 4 guanidinobutanal CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , 5 guanidino 2 oxo pentanoate , and two product chemistry products , 4 guanidinobutanal and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of lyase s, specifically the carboxy lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is 5 guanidino 2 oxo pentanoate carboxy lyase 4 guanidinobutanal forming . Other names in common use include alpha ketoarginine decarboxylase , and 2 oxo 5 guanidinopentanoate carboxy lyase . It has 2 cofactor biochemistry cofactors thiamin diphosphate , and Divalent cation . References reflist 1 cite journal author Vanderbilt AS, Gaby NS, Rodwell VW date 1975 title Intermediates and enzymes between alpha ketoarginine and gamma guanidinobutyrate in the L arginine catabolic pathway of Pseudomonas putida journal J. Biol. Chem. volume 250 pages 5322&ndash 9 pmid 237915 issue 14 4.1 enzyme stub Category EC 4.1.1 Category Thiamine enzymes Category Divalent cation enzymes Category Enzymes of unknown structure ... more details
enzyme Name benzoin aldolase EC number 4.1.2.38 CAS number 122097 01 2 IUBMB EC number 4 1 2 38 GO code 0047695 image width caption In enzymology , a benzoin aldolase EC number 4.1.2.38 is an enzyme that catalysis catalyzes the chemical reaction 2 hydroxy 1,2 diphenylethanone math rightleftharpoons math 2 benzaldehyde Hence, this enzyme has one substrate biochemistry substrate , 2 hydroxy 1,2 diphenylethanone , and one product chemistry product , benzaldehyde . This enzyme belongs to the family of lyase s, specifically the aldehyde lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is 2 hydroxy 1,2 diphenylethanone benzaldehyde lyase benzaldehyde forming . Other names in common use include benzaldehyde lyase , and 2 hydroxy 1,2 diphenylethanone benzaldehyde lyase . It employs one cofactor biochemistry cofactor , thiamin diphosphate . Structural studies As of late 2007, 3 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 2AG0 , PDB link 2AG1 , and PDB link 2UZ1 . References reflist 1 cite journal author Gonzalez B, Vicuna R date 1989 title Benzaldehyde lyase, a novel thiamine PPi requiring enzyme, from Pseudomonas fluorescens biovar I journal J. Bacteriol. volume 171 pages 2401&ndash 5 pmid 2496105 issue 5 pmc 209914 4.1 enzyme stub Category EC 4.1.2 Category Thiamine enzymes Category Enzymes of known structure ... more details
enzyme Name thiamin triphosphatase EC number 3.6.1.28 CAS number 9068 47 7 IUBMB EC number 3 6 1 28 GO code 0050333 image width caption protein Name thiamine triphosphatase caption image width HGNCid 18987 Symbol THTPA AltSymbols EntrezGene 79178 OMIM RefSeq NM 024328 UniProt Q9BU02 PDB ECnumber 3.6.1.28 Chromosome 14 Arm q Band 11.2 LocusSupplementaryData Thiamine triphosphatase is an enzyme involved in thiamine metabolism . It catalysis catalyzes the chemical reaction thiamine triphosphate H sub 2 sub O math rightleftharpoons math thiamine diphosphate phosphate This enzyme belongs to the family of acid anhydride hydrolase s, specifically those acting on phosphorus containing anhydrides. Its systematic name is thiamine triphosphate phosphohydrolase. Structural studies As of late 2007, only one tertiary structure structure has been solved for this class of enzymes, with the Protein Data Bank PDB accession code PDB link 2JMU . See also Thiamine diphosphate kinase References reflist 1 cite journal author Hashitani Y, Cooper JR date 1972 title The partial purification of thiamine triphosphatase from rat brain journal J. Biol. Chem. volume 247 pages 2117&ndash 9 pmid 4335862 issue 7 Acid anhydride hydrolases hydrolase stub Category EC 3.6.1 Category Enzymes of known structure ... more details
enzyme Name acetoin ribose 5 phosphate transaldolase EC number 2.2.1.4 CAS number 87843 76 3 IUBMB EC number 2 2 1 4 GO code 0047156 image width caption In enzymology , an acetoin ribose 5 phosphate transaldolase EC number 2.2.1.4 is an enzyme that catalysis catalyzes the chemical reaction 3 hydroxybutan 2 one D ribose 5 phosphate math rightleftharpoons math acetaldehyde 1 deoxy D altro heptulose 7 phosphate Thus, the two substrate biochemistry substrates of this enzyme are 3 hydroxybutan 2 one and D ribose 5 phosphate , whereas its two product chemistry products are acetaldehyde and 1 deoxy D altro heptulose 7 phosphate . This enzyme belongs to the family of transferase s, specifically those transferring aldehyde or ketone ketonic groups transaldolases and transketolases, respectively . The systematic name of this enzyme class is 3 hydroxybutan 2 one D ribose 5 phosphate aldehydetransferase . Other names in common use include 1 deoxy D altro heptulose 7 phosphate synthetase , 1 deoxy D altro heptulose 7 phosphate synthase , 3 hydroxybutan 2 one D ribose 5 phosphate aldehydetransferase wrong , and substrate name . It employs one cofactor biochemistry cofactor , thiamin diphosphate . References reflist 1 cite journal author Yokota A and Sasajima K date 1983 title Enzymatic formation of a new monosaccharide, 1 deoxy D altro heptulose phosphate, from DL acetoin and D ribose 5 phosphate by a transketolase mutant of Bacillus pumilus journal Agric. Biol. Chem. volume 47 pages 1545&ndash 1553 transferase stub Category EC 2.2.1 Category Thiamine enzymes Category Enzymes of unknown structure it Acetoina ribosio 5 fosfato transaldolasi ... more details
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