chembox Verifiedfields changed verifiedrevid 418423836 Name small L small Tryptophan ImageFile L Tryptophan L Tryptophan.svg ImageName Skeletal formula of L isomer ImageFile1 L tryptophan 3D balls.png ImageName1 Ball and stick model of L isomer IUPACName Tryptophan or 2S 2 amino 3 1H indol 3 yl propanoic ... isbn 0 19 855338 2 oclc doi url ref Section3 Chembox Hazards MainHazards FlashPt Autoignition Tryptophan ... stereoisomer of tryptophan is used in Fibrous protein structural or enzyme proteins, but the D stereoisomer ... octapeptide containing D tryptophan comparison with protein loops journal Biochemistry volume 38 issue ... characteristic of tryptophan is that it contains an indole functional group. It is an essential amino ... of tryptophan was first reported by Frederick Hopkins in 1901 ref name pmid16992614 cite journal ... . From 600 gram s of crude casein one obtains 4 8 grams of tryptophan. ref name Cox 1943 OrgSyn ... Biosynthesis and industrial production Plants and microorganism s commonly synthesize tryptophan ... ER, Last RL title Tryptophan biosynthesis and metabolism biochemical and molecular genetics journal ... glycerinephosphate is produced, which in turn is transformed into indole . In the last step, tryptophan synthase catalyzes the formation of tryptophan from indole and the amino acid serine . Image Tryptophan biosynthesis en .svg 780px The industrial production of tryptophan is also biosynthetic and is based ... is catalyzed by the enzyme tryptophan synthase . ref name pmid12523387 cite journal author ... pages 1 35 year 2002 pmid 12523387 doi 10.1007 3 540 45989 8 1 ref Function Image Tryptophan metabolism.png thumb 365px Metabolism of L tryptophan into serotonin and melatonin left and niacin right ... including humans , tryptophan is an essential amino acid . This means that it cannot be synthesized by the organism and therefore must be part of its diet. Amino acids, including tryptophan, act as building blocks in protein biosynthesis . In addition, tryptophan functions as a biochemical Precursor ... more details
enzyme Name tryptophan dehydrogenase EC number 1.4.1.19 CAS number 94047 13 9 IUBMB EC number 1 4 1 19 GO code 0050363 image width caption In enzymology , a tryptophan dehydrogenase EC number 1.4.1.19 is an enzyme that catalysis catalyzes the chemical reaction L tryptophan NAD P H sub 2 sub O math rightleftharpoons math indol 3 yl pyruvate NH sub 3 sub NAD P H H sup sup The 4 substrate biochemistry substrates of this enzyme are L tryptophan , nicotinamide adenine dinucleotide NAD sup sup , nicotinamide adenine dinucleotide phosphate NADP sup sup , and water H sub 2 sub O , whereas its 5 product chemistry products are indol 3 yl pyruvate , ammonia NH sub 3 sub , nicotinamide adenine dinucleotide NADH , 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 NH2 group of donors with NAD or NADP as acceptor. The systematic name of this enzyme class is L tryptophan NAD P oxidoreductase deaminating . Other names in common use include NAD P L tryptophan dehydrogenase , L tryptophan dehydrogenase , L Trp dehydrogenase , and TDH . This enzyme has at least one effector biology effector , calcium . References reflist 1 cite journal author Vackova K, Mehta A and Kutacek M date 1985 title Tryptophan aminotransferase and tryptophan dehydrogenase activities in some cell compartments of spinach leaves the effect of calcium ions on tryptophan dehydrogenase journal Biol. Plant. volume 27 pages 154&ndash 158 doi 10.1007 BF02902153 issue 2 3 1.4 enzyme stub Category EC 1.4.1 Category NADPH dependent enzymes Category NADH dependent enzymes Category Enzymes of unknown structure it Triptofano deidrogenasi ja ... more details
enzyme Name tryptophan dimethylallyltransferase EC number 2.5.1.34 CAS number 55127 01 0 IUBMB EC number 2 5 1 34 GO code 0050364 image width caption In enzymology , a tryptophan dimethylallyltransferase EC number 2.5.1.34 is an enzyme that catalysis catalyzes the chemical reaction dimethylallyl diphosphate L tryptophan math rightleftharpoons math diphosphate 4 3 methylbut 2 enyl L tryptophan Thus, the two substrate biochemistry substrates of this enzyme are dimethylallyl diphosphate and L tryptophan , whereas its two product chemistry products are diphosphate and 4 3 methylbut 2 enyl L tryptophan . This enzyme belongs to the family of transferase s, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is dimethylallyl diphosphate L tryptophan dimethylallyltransferase . Other names in common use include dimethylallylpyrophosphate L tryptophan dimethylallyltransferase , dimethylallyltryptophan synthetase , dimethylallylpyrophosphate tryptophan dimethylallyl transferase , DMAT synthetase , and 4 gamma,gamma dimethylallyl tryptophan synthase . References reflist 1 cite journal author Lee SL, Floss HG, Heinstein P date 1976 title Purification and properties of dimethylallylpyrophosphate tryptopharm dimethylallyl transferase, the first enzyme of ergot alkaloid biosynthesis in Claviceps. sp. SD 58 journal Arch. Biochem. Biophys. volume 177 pages 84&ndash 94 pmid 999297 doi 10.1016 0003 9861 76 90418 5 issue 1 transferase stub Category EC 2.5.1 Category Enzymes of unknown structure ... more details
enzyme Name tryptophan transaminase EC number 2.6.1.27 CAS number 9022 98 4 IUBMB EC number 2 6 1 27 GO code 0050362 image width caption In enzymology , a tryptophan transaminase EC number 2.6.1.27 is an enzyme that catalysis catalyzes the chemical reaction L tryptophan 2 oxoglutarate math rightleftharpoons math indol 3 yl pyruvate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are L tryptophan and 2 oxoglutarate , whereas its two product chemistry products are indol 3 yl pyruvate and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L tryptophan 2 oxoglutarate aminotransferase . Other names in common use include L phenylalanine 2 oxoglutarate aminotransferase , tryptophan aminotransferase , 5 hydroxytryptophan ketoglutaric transaminase , hydroxytryptophan aminotransferase , L tryptophan aminotransferase , and L tryptophan transaminase . This enzyme participates in tryptophan metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author George H, Gabay S year 1968 title Brain aromatic aminotransferase. I. Purification and some properties of pig brain L phenylalanine 2 oxoglutarate aminotransferase journal Biochim. Biophys. Acta. volume 167 pages 555&ndash 66 pmid 5722279 issue 3 cite journal author O Neil SR, DeMoss RD year 1968 title Tryptophan transaminase from Clostridium sporogenes journal Arch. Biochem. Biophys. volume 127 pages 361&ndash 9 pmid 5697992 doi 10.1016 0003 9861 68 90237 3 issue 1 cite journal author Tangen O, Fonnum F and Haavaldsen R year 1965 title Separation and purification of aromatic amino acid transaminases from rat brain journal Biochim. Biophys. Acta volume 96 pages 82&ndash 90 pmid 14285270 Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure transferase stub ... more details
enzyme Name tryptophan 2,3 dioxygenase EC number 1.13.11.11 CAS number 9014 51 1 IUBMB EC number 1 13 11 11 GO code 0004833 image width caption In enzymology , a tryptophan 2,3 dioxygenase EC number 1.13.11.11 is an enzyme that catalysis catalyzes the chemical reaction L tryptophan O sub 2 sub math rightleftharpoons math N formyl L kynurenine Thus, the two substrate biochemistry substrates of this enzyme are L tryptophan and oxygen O sub 2 sub , whereas its product chemistry product is N formyl L kynurenine . This enzyme belongs to the family of oxidoreductase s, specifically those acting on single donors with O sub 2 sub as oxidant and incorporation of two atoms of oxygen into the substrate oxygenases . The oxygen incorporated need not be derived from O sub 2 sub . The systematic name of this enzyme class is L tryptophan oxygen 2,3 oxidoreductase decyclizing . Other names in common use include tryptophan pyrrolase ambiguous , tryptophanase , tryptophan oxygenase , tryptamine 2,3 dioxygenase , tryptophan peroxidase , indoleamine 2,3 dioxygenase ambiguous , indolamine 2,3 dioxygenase ambiguous , L tryptophan pyrrolase , TDO , and L tryptophan 2,3 dioxygenase . This enzyme participates in tryptophan metabolism . It employs one cofactor biochemistry cofactor , heme . Structural studies As of mid 2008, several tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1YW0 , PDB link 2NOX , PDB link 2nw7 , PDB link ... Nozawa T, Hatano M date 1983 title Magnetic and natural circular dichroism of L tryptophan 2,3 dioxygenases ... E, Correia MA date 1996 title Expression of rat liver tryptophan 2,3 dioxygenase in Escherichia ... substrate reactivities for tryptophan 2,3 dioxygenase journal J. Biol. Chem. volume 268 pages 17781 ... effects of oxygen on indoleamine 2,3 dioxygenase and tryptophan 2,3 dioxygenase of the kynurenine ... Heme enzymes Category Enzymes of known structure de Tryptophan 2,3 Dioxygenase it Triptofano ... more details
stack begin enzyme Name tryptophan 5 monooxygenase EC number 1.14.16.4 CAS number 9037 21 2 IUBMB EC number 1 14 16 4 GO code 0004510 image width caption protein Name TPH1 tryptophan hydroxylase 1 tryptophan ... 15.3 LocusSupplementaryData p14 protein Name TPH2 tryptophan hydroxylase 2 caption image width HGNCid ... Chromosome 12 Arm q Band 15 LocusSupplementaryData stack end Tryptophan hydroxylase TPH is an enzyme ... the following chemical reaction L tryptophan tetrahydrobiopterin O sub 2 sub math rightleftharpoons ... , iron . Function stack Enzymatic Reaction foward enzyme Tryptophan hydroxylase reverse enzyme substrate Tryptophan product 5 HTP reaction direction forward reversible reverse forward minor foward ... br BH sub 2 sub minor reverse substrate s minor reverse product s substrate image Tryptophan simple.png ... serotonin. It is also the first enzyme in the synthesis of melatonin. Tryptophan hydroxylase ... A title Conformation of the substrate and pterin cofactor bound to human tryptophan hydroxylase ... of tryptophan has an antidepressant effect Fact date November 2008 and inhibition of tryptophan hydroxylase ... of human tryptophan hydroxylase and its implications for the biosynthesis of the neurotransmitters ... pmid 12379098 doi 10.1021 bi026561f url ref The Enzyme activity activity of tryptophan hydroxylase i.e. the rate at which it converts L tryptophan into the serotonin precursor L 5 hydroxytryptophan ... tryptophan hydroxylase, thus increasing its activity. Isoforms In humans, as well as in other mammals ... cite journal author Walther DJ, Bader M title A unique central tryptophan hydroxylase isoform journal ... 2.png The pathway for the synthesis of serotonin from tryptophan Image Trp 5ht pathway.png Metabolic pathway from tryptophan to serotonin gallery References reflist Further reading refbegin 2 cite ... of tryptophan hydroxylase from rabbit hindbrain journal J. Biol. Chem. volume 247 pages 4165 ... 1979 title The role of intraneuronal 5 HT and of tryptophan hydroxylase activation in the control ... more details
enzyme Name tryptophan 2 monooxygenase EC number 1.13.12.3 CAS number 37256 65 8 IUBMB EC number 1 13 12 3 GO code 0050361 image width caption In enzymology , a tryptophan 2 monooxygenase EC number 1.13.12.3 is an enzyme that catalysis catalyzes the chemical reaction L tryptophan O sub 2 sub math rightleftharpoons math indol 3 yl acetamide CO sub 2 sub H sub 2 sub O Thus, the two substrate biochemistry substrates of this enzyme are L tryptophan and oxygen O sub 2 sub , whereas its 3 product chemistry products are indol 3 yl acetamide , carbon dioxide CO sub 2 sub , and water H sub 2 sub O . This enzyme belongs to the family of oxidoreductase s, specifically those acting on single donors with O sub 2 sub as oxidant and incorporation of two atoms of oxygen into the substrate oxygenases . The oxygen incorporated need not be derived from O with incorporation of one atom of oxygen internal monooxygenases o internal mixed function oxidases . The systematic name of this enzyme class is L tryptophan oxygen 2 oxidoreductase decarboxylating . This enzyme participates in tryptophan metabolism . References reflist 1 cite journal author Kosuge T, Heskett MG, Wilson EE date 1966 title Microbial synthesis and degradation of indole 3 acetic acid. I. The conversion of L tryptophan to indole 3 acetamide by an enzyme system from Pseudomonas savastanoi journal J. Biol. Chem. volume 241 pages 3738&ndash 44 pmid 5916389 issue 16 cite journal author Kuo, TT and Kosuge T date 1969 title Factors influencing the production and further metabolism of indole 3 acetic acid by Pseudomonas savastanoi journal J. Gen. Appl. Microbiol. volume 15 pages 51&ndash 63 doi 10.2323 jgam.15.51 1.13 enzyme stub Category EC 1.13.12 Category Enzymes of unknown structure it Triptofano 2 monoossigenasi ja 2 ... more details
chembox Watchedfields changed verifiedrevid 415829296 ImageFile tryptophan tryptophylquinone.png ImageSize 200px IUPACName 2 amino 3 2 2 amino 3 2 carboxyethyl 6,7 dioxo 1H indol 4 yl 1H indol 3 yl propanoic acid OtherNames Section1 Chembox Identifiers CASNo 134645 25 3 PubChem 5486829 SMILES C1 CC C2C C1 C C N2 C3 CC O C O C4 C3C C N4 N CCC O O CC C O O N MeSHName Tryptophan tryptophylquinone Section2 Chembox Properties Formula C sub 22 sub H sub 20 sub N sub 4 sub O sub 6 sub MolarMass 436.419 Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition Tryptophan tryptophylquinone is a molecule required for the functioning of amine dehydrogenase . See also Amicyanin protein primary structure Category Amino acid derivatives biochem stub ... more details
Enzyme Name Tryptophan Synthase EC number 4.2.1.20 CAS number 9014 52 2 IUBMB EC number 4 2 1 20 GO code 0004834 image Tryptophan Synthase Dimer 3.png width caption Subunits font color blue Alpha Subunit ... font Tryptophan synthase or tryptophan synthetase is an enzyme that catalyzes the final two steps in the biosynthesis of tryptophan . ref name Tryptophan synthase cite journal author Dunn MF, Niks D, Ngo H, Barends TRM, Schlichting I title Tryptophan synthase the workings of a channeling nanomachine ... cite journal author Jablonski P, Jablonski L, Pintado O, Sriranganathan N, Howde C title Tryptophan synthase Identification of Pasteurella multocida tryptophan synthase B subunit by antisera against ..., Lu P, Sangari R, Zhang A, Masurekar P, An Z title The tryptophan synthetase gene TRP1 of Nodulisporium ... RC, Ko SS, Tong CG, Yang RY, Chan MT title Overexpression of Arabidopsis thaliana tryptophan synthase ... SC, Kubler E, Hoffmann B, Braus GH title The tryptophan synthase encoding trpB gene of Aspergillus ... condensation of indole and serine to form tryptophan in a pyridoxal phosphate PLP dependent ... author Raboni S, Bettati S, Mozzarelli A title Tryptophan synthase a mine for enzymologists journal ... s00018 009 0028 0 url issn ref The active sites of tryptophan synthase are allosterically coupled. ref ... induced conformational changes of tryptophan synthase journal Biochemistry volume 48 issue 41 pages ... Subunits Tryptophan synthase typically exists as an complex. The and subunits have molecular ..., Liang PH, Anderson KS, Schlichting I title Loop closure and intersubunit communication in tryptophan ... 10.1146 annurev.biochem.70.1.149 url issn ref Image Tryptophan Synthase Mechanism 5.gif thumb left alt caption. Image 2 Proposed Mechanism of Tryptophan Synthase Enzyme Mechanism subunit reaction ... KS, Miles EW, Johnson KA title Serine modulates substrate channeling in tryptophan synthase. A novel ... the replacement reaction in which indole and serine condense to form tryptophan in a PLP dependent ... more details
A shows how binding tryptophan enhances DNA affinity journal Nature volume 327 issue 6123 pages 591 ... Arvidson DN, Arvidson CG, Lawson CL, Miner J, Adams C, Youderian P title The tryptophan repressor sequence ... , codes for the production of tryptophan itself. Another codes for the tryptophan repressor protein. These are forms of negative feedback feedback regulation . The tryptophan repressor is a 25 kD protein which regulates transcription genetics transcription of the tryptophan biosynthetic pathway ... operons. Mechanism When the amino acid tryptophan is in plentiful supply in the cell, trpR binds 2 molecules of tryptophan, which alters its structure and dynamics so that it becomes able to bind ... of the gene proteins which make more tryptophan. When the cellular levels of tryptophan decline, the tryptophan ... tryptophan is scarce. If there isn t enough tryptophan, the repressor protein breaks off from the operator ... for tryptophan is made. See also trp operon References reflist 2 Transcription Category Proteins protein ... more details
enzyme Name D tryptophan N acetyltransferase EC number 2.3.1.34 CAS number 37257 13 9 IUBMB EC number 2 3 1 34 GO code 0047835 image width caption In enzymology , a D tryptophan N acetyltransferase EC number 2.3.1.34 is an enzyme that catalysis catalyzes the chemical reaction acetyl CoA D tryptophan math rightleftharpoons math CoA N acetyl D tryptophan Thus, the two substrate biochemistry substrates of this enzyme are acetyl CoA and D tryptophan , whereas its two product chemistry products are coenzyme A CoA and N acetyl D tryptophan . This enzyme belongs to the family of transferase s, specifically those acyltransferase s transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl CoA D tryptophan N acetyltransferase . Other names in common use include D tryptophan acetyltransferase , and acetyl CoA D tryptophan alpha N acetyltransferase . References reflist 1 cite journal author Zenk MH and Schmitt J date 1964 title Enzymatische Acetylierung von D Tryptophan journal Naturwissenschaften volume 51 issue 21 pages 510&ndash 511 doi 10.1007 BF00632216 transferase stub Category EC 2.3.1 Category Enzymes of unknown structure it D triptofano N acetiltransferasi ... more details
enzyme Name tryptophan 2 C methyltransferase EC number 2.1.1.106 CAS number 126626 83 3 IUBMB EC number 2 1 1 106 GO code 0030772 image width caption In enzymology , a tryptophan 2 C methyltransferase EC number 2.1.1.106 is an enzyme that catalysis catalyzes the chemical reaction S adenosyl L methionine L tryptophan math rightleftharpoons math S adenosyl L homocysteine L 2 methyltryptophan Thus, the two substrate biochemistry substrates of this enzyme are S Adenosyl methionine S adenosyl methionine and L tryptophan , whereas its two product chemistry products are S adenosylhomocysteine and L 2 methyltryptophan . This enzyme belongs to the family of transferase s, specifically those transferring one carbon group methyltransferases. The systematic name of this enzyme class is S adenosyl L methionine L tryptophan 2 C methyltransferase . Other names in common use include tryptophan 2 methyltransferase , and S adenosylmethionine tryptophan 2 methyltransferase . References reflist 1 cite journal author Frenzel T, Zhou P, Floss HG date 1990 title Formation of 2 methyltryptophan in the biosynthesis of thiostrepton isolation of S adenosylmethionine tryptophan 2 methyltransferase journal Arch. Biochem. Biophys. volume 278 pages 35&ndash 40 pmid 2321967 doi 10.1016 0003 9861 90 90227 P issue 1 transferase stub Category EC 2.1.1 Category Enzymes of unknown structure it Triptofano 2 C metiltransferasi ... more details
enzyme Name tryptophan phenylpyruvate transaminase EC number 2.6.1.28 CAS number 37277 87 5 IUBMB EC number 2 6 1 28 GO code 0047299 image width caption In enzymology , a tryptophan phenylpyruvate transaminase EC number 2.6.1.28 is an enzyme that catalysis catalyzes the chemical reaction L tryptophan phenylpyruvate math rightleftharpoons math indol 3 yl pyruvate L phenylalanine Thus, the two substrate biochemistry substrates of this enzyme are L tryptophan and phenylpyruvate , whereas its two product chemistry products are indol 3 yl pyruvate and L phenylalanine . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L tryptophan phenylpyruvate aminotransferase . This enzyme is also called L tryptophan alpha ketoisocaproate aminotransferase . References reflist 1 cite journal author Koide Y, Honma M and Shimomura T date 1980 title L Tryptophan alpha ketoisocaproate aminotransferase from Pseudomonas sp journal Agric. Biol. Chem. volume 44 pages 2013&ndash 2019 cite journal author Sukanya NK, Vaidyanathan CS date 1964 title Aminotransferases of Agrobacterium tumefaciens. Transamination between tryptophan and phenylpyruvate journal Biochem. J. volume 92 pages 594&ndash 8 pmid 5837443 issue 3 pmc 1206107 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
enzyme Name D tryptophan N malonyltransferase EC number 2.3.1.112 CAS number 94490 01 4 IUBMB EC number 2 3 1 112 GO code 0047836 image width caption In enzymology , a D tryptophan N malonyltransferase EC number 2.3.1.112 is an enzyme that catalysis catalyzes the chemical reaction malonyl CoA D tryptophan math rightleftharpoons math CoA N sub 2 sub malonyl D tryptophan Thus, the two substrate biochemistry substrates of this enzyme are malonyl CoA and D tryptophan , whereas its two product chemistry products are coenzyme A CoA and N2 malonyl D tryptophan . This enzyme belongs to the family of transferase s, specifically those acyltransferase s transferring groups other than aminoacyl groups. The systematic name of this enzyme class is malonyl CoA D tryptophan N malonyltransferase . References reflist 1 cite journal author Matern U, Feser C, Heller W date 1984 title N malonyltransferases from peanut journal Arch. Biochem. Biophys. volume 235 pages 218&ndash 27 pmid 6497391 doi 10.1016 0003 9861 84 90271 6 issue 1 transferase stub Category EC 2.3.1 Category Enzymes of unknown structure it D triptofano N maloniltransferasi ... more details
enzyme Name tryptophan 2 dioxygenase EC number 1.13.99.3 CAS number 64295 81 4 IUBMB EC number 1 13 99 3 GO code 0050360 image width caption In enzymology , a tryptophan 2 dioxygenase EC number 1.13.99.3 is an enzyme that catalysis catalyzes the chemical reaction L tryptophan O sub 2 sub math rightleftharpoons math indol 3 yl glycolaldehyde CO sub 2 sub NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are L tryptophan and oxygen O sub 2 sub , whereas its 3 product chemistry products are indol 3 yl glycolaldehyde , carbon dioxide CO sub 2 sub , and ammonia NH sub 3 sub . This enzyme belongs to the family of oxidoreductase s, specifically those acting on single donors with O sub 2 sub as oxidant and incorporation of two atoms of oxygen into the substrate oxygenases . The oxygen incorporated need not be derived from O miscellaneous. The systematic name of this enzyme class is L tryptophan oxygen 2 oxidoreductase side chain cleaving . Other names in common use include indole 3 alkane alpha hydroxylase , tryptophan side chain alpha,beta oxidase , tryptophan side chain oxidase II , tryptophan side chain oxidase , TSO , indolyl 3 alkan alpha hydroxylase , tryptophan side chain oxidase type I , TSO I , TSO II , and tryptophan side chain oxidase . This enzyme participates in tryptophan metabolism . It employs one cofactor biochemistry cofactor , heme . References reflist 1 cite journal author Roberts J, Rosenfeld HJ year 1977 title Isolation, crystallization, and properties of indolyl 3 alkane alpha hydroxylase. A novel tryptophan metabolizing enzyme journal J. Biol. Chem. volume 252 pages 2640&ndash 7 pmid 15994 issue 8 cite journal author Takai K, Ushiro H, Noda Y, Narumiya S, Tokuyama T year 1977 title Crystalline hemoprotein from Pseudomonas that catalyzes oxidation of side chain of tryptophan and other indole derivatives journal J. Biol. Chem. volume 252 pages 2648&ndash 56 pmid 15995 issue 8 Category EC 1.13.99 Category Heme enzymes Category Enzymes ... more details
enzyme Name tryptophan alpha,beta oxidase EC number 1.3.3.10 CAS number 156859 19 7 IUBMB EC number 1 3 3 10 GO code 0050621 image width caption In enzymology , a tryptophan alpha,beta oxidase EC number 1.3.3.10 is an enzyme that catalysis catalyzes the chemical reaction L tryptophan O sub 2 sub math rightleftharpoons math alpha,beta didehydrotryptophan H sub 2 sub O sub 2 sub Thus, the two substrate biochemistry substrates of this enzyme are L tryptophan and oxygen O sub 2 sub , whereas its two product chemistry products are alpha,beta didehydrotryptophan 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 CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is L tryptophan oxygen alpha,beta oxidoreductase . Other names in common use include L tryptophan 2 ,3 oxidase , and L tryptophan alpha,beta dehydrogenase . It employs one cofactor biochemistry cofactor , heme . References reflist 1 cite journal author Genet R, Denoyelle C, Menez A year 1994 title Purification and partial characterization of an amino acid alpha,beta dehydrogenase, L tryptophan 2 ,3 oxidase from Chromobacterium violaceum journal J. Biol. Chem. volume 269 pages 18177&ndash 84 pmid 8027079 issue 27 cite journal author Genet R, Benetti PH, Hammadi A, Menez A year 1995 title L tryptophan 2 ,3 oxidase from Chromobacterium violaceum. Substrate specificity and mechanistic implications journal J. Biol. Chem. volume 270 pages 23540&ndash 5 pmid 7559518 issue 40 doi 10.1074 jbc.270.40.23540 Category EC 1.3.3 Category Heme enzymes Category Enzymes of unknown structure 1.3 enzyme stub it Triptofano alfa,beta ossidasi ja , ... more details
enzyme Name peptide tryptophan 2,3 dioxygenase EC number 1.13.11.26 CAS number 37256 64 7 IUBMB EC number 1 13 11 26 GO code 0050169 image width caption In enzymology , a peptide tryptophan 2,3 dioxygenase EC number 1.13.11.26 is an enzyme that catalysis catalyzes the chemical reaction peptide tryptophan O sub 2 sub math rightleftharpoons math peptide formylkynurenine Thus, the two substrate biochemistry substrates of this enzyme are peptide tryptophan and oxygen O sub 2 sub , whereas its product chemistry product is peptide formylkynurenine . This enzyme belongs to the family of oxidoreductase s, specifically those acting on single donors with O sub 2 sub as oxidant and incorporation of two atoms of oxygen into the substrate oxygenases . The oxygen incorporated need not be derived from O sub 2 sub . The systematic name of this enzyme class is peptide tryptophan oxygen 2,3 oxidoreductase decyclizing . Other names in common use include pyrrolooxygenase , peptidyltryptophan 2,3 dioxygenase , and tryptophan pyrrolooxygenase . References reflist 1 cite journal author Frydman RB, Tomaro ML, Frydman B date 1972 title Pyrrolooxygenase its action on tryptophan containing enzymes and peptides journal Biochim. Biophys. Acta. volume 284 pages 80&ndash 9 pmid 4403729 issue 1 1.13 enzyme stub Category EC 1.13.11 Category Enzymes of unknown structure it Peptide triptofano 2,3 diossigenasi ja 2,3 ... more details
Infobox rfam Name Tryptophan operon leader image RF00513.jpg width caption Predicted secondary structure and sequence conservation of Trp leader Symbol Trp leader AltSymbols Rfam RF00513 miRBase miRBase family RNA type Cis regulatory element Cis reg leader Tax domain Bacteria GO SO SO 0000233 CAS number EntrezGene HGNCid OMIM PDB RefSeq Chromosome Arm Band LocusSupplementaryData The Tryptophan operon leader is an cis regulatory element RNA element found at the 5 of some bacterial Trp operon tryptophan operons . The leader sequence can assume two different secondary structures known as the terminator and the anti terminator structure. The leader also codes for very short peptide sequence that is rich in Tryptophan. The terminator structure is recognised as a termination signal for RNA polymerase and the operon is not transcribed. This structure forms when the cell has an excess of tryptophan and ribosome movement over the leader transcript is not impeded. ref cite journal last Kolter first R coauthors Yanofsky C year 1982 title Attenuation in amino acid biosynthetic operons journal Annu Rev Genet volume 16 pages 113 134 pmid 6186194 doi 10.1146 annurev.ge.16.120182.000553 ref When there is a deficiency of the charged tryptophanyl tRNA the ribosome translating the leader peptide stalls and the antiterminator structure can form. This allows RNA polymerase to transcribe the operon. At least 6 different amino acid operons are known to be regulated by this attenuation. References Reflist External links Rfam id RF00513 name Tryptophan operon leader Category Cis regulatory RNA elements molecular cell biology stub ... more details
enzyme Name tryptophan tRNA ligase EC number 6.1.1.2 CAS number 9023 44 3 IUBMB EC number 6 1 1 2 GO code 0004830 image width caption In enzymology , a tryptophan tRNA ligase EC number 6.1.1.2 is an enzyme that catalysis catalyzes the chemical reaction ATP L tryptophan tRNATrp math rightleftharpoons math AMP diphosphate L tryptophyl tRNATrp The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L tryptophan , and tRNA Trp , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L tryptophyl tRNATrp . This enzyme belongs to the family of ligase s, to be specific those forming carbon oxygen bonds in aminoacyl tRNA and related compounds. The systematic name of this enzyme class is L tryptophan tRNATrp ligase AMP forming . Other names in common use include tryptophanyl tRNA synthetase , L tryptophan tRNATrp ligase AMP forming , tryptophanyl transfer ribonucleate synthetase , tryptophanyl transfer ribonucleic acid synthetase , tryptophanyl transfer RNA synthetase , tryptophanyl ribonucleic synthetase , tryptophanyl transfer ribonucleic synthetase , tryptophanyl tRNA synthase , tryptophan translase , and TrpRS . This enzyme participates in tryptophan metabolism and aminoacyl trna biosynthesis . Structural studies As of late 2007, 21 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1D2R , PDB link 1I6K , PDB link 1I6L , PDB link 1I6M , PDB link 1M83 , PDB link 1MAU , PDB link 1MAW , PDB link 1MB2 , PDB link 1O5T , PDB link 1R6T , PDB link 1R6U , PDB link 1ULH , PDB link 1YIA , PDB link 1YID , PDB link 2A4M , PDB link 2AKE , PDB link 2AZX , PDB link 2DR2 , PDB link 2G36 , PDB link 2IP1 , and PDB link 2OV4 . References reflist 1 cite journal author DAVIE EW, KONINGSBERGER VV, LIPMANN F date 1956 title The isolation of a tryptophan activating enzyme from pancreas journal Arch. Biochem. Biophys. volume 65 pages 21&ndash 38 pmid 13373404 ... more details
Histidine tryptophan ketoglutarate , or Custodiol HTK solution is a high flow, low potassium preservation solution used for organ transplantation . HTK solution is intended for perfusion and flushing of donor liver kidney, heart, lung and pancreas prior to removal from the donor and for preserving these organs during hypothermic storage and transport to the recipient. HTK solution is based on the principle of inactivating organ function by withdrawal of extracellular sodium and calcium , together with intensive buffering of the extracellular space by means of histidine histidine hydrochloride, so as to prolong the period during which the organs will tolerate interruption of oxygenated blood . The composition of HTK is similar to that of extracellular fluid . All of the components of HTK occur naturally in the body. class wikitable Component HTK Sodium mmol L 15 Potassium mmol L 10 Magnesium mmol L 4 Calcium mmol L 0.015 Ketoglutarate glutamic acid mmol L 1 Histidine mmol L 198 Mannitol mmol L 30 Tryptophan mmol L 2 Osmolarity mOsm L 310 Custodiol HTK is the registered trademark of Dr. Franz K hler Chemie GmbH, Germany . References No footnotes date April 2009 1. 510 k Summary. Custodiol HTK Solution Common Classification Name Isolated Kidney Perfusion and Transport System and Accessories, 21 CFR 876.5880 Franz Kohler. Prepared December 14, 2004. http www.fda.gov cdrh pdf4 K043461.pdf http www.fda.gov cdrh pdf4 K043461.pdf 2. Ringe B.,et al. Safety and efficacy of living donor liver preservation with HTK solution. Transplant Proc. 2005 37 316 319. 3. Agarawal A., et al. Follow up experience using histidine tryptophan ketoglutarate solution in clinical pancreas transplantation Transplant Proc. 2005 37 3523 3526. 4. Pokorny H., et al. Histidine tryptophan ketoglutarate solution for organ preservation in human liver transplantation a prospective multi centre observation study ..., 1999. 7. Hatano E., et al. Hepatic preservation with histidine tryptophan ketoglutarate solution ... more details
OrganicBox complete wiki name Tryptophan name S 2 Amino 3 1H indol 3 yl propanoic acid GENERAL INFORMATION C 11 H 12 N 2 O 2 mass 204.23 abbreviation W, Trp image Image L tryptophan skeletal.png 150px Image L tryptophan 3D sticks.png 140px synonyms DATABASES SMILES C N C O O CC1c2ccccc2NC 1 InChI 1 C11H12N2O2 c12 9 11 14 15 5 7 6 13 10 4 2 1 3 8 7 10 h1 4,6,9,13H,5,12H2, H,14,15 t9 m1 s1 f h14H 1 C3H7NO2 c1 2 4 3 5 6 h2H,4H2,1H3, H,5,6 f h5H CAS 73 22 3 DrugBank EINECS br 200 795 6 ref 1 a PubChem 9060 D ref 2 a , 6305 L ref 3 a PHYSICAL PROPERTIES Structure index of refraction abbe number dielectric constant magnetic susceptibility dipole moment U V data lambda max extinction coefficient Infrared data absorption bands NMR data proton NMR carbon NMR other NMR Spectrometry data mass spectrometry Phase behaviour delta fus H o delta fus S o delta vap H o delta vap S o triple point K triple point C triple point Pa criticle point K criticle point C criticle point Pa Solid properties delta f H o solid S o solid heat capacity solid density solid 1.34 melting point C 228 melting point F melting point K Liquid properties delta f H o liquid S o liquid heat capacity liquid density liquid viscosity liquid boiling point C boiling point F boiling point K Gas properties delta f H o gas S o gas heat capacity gas viscosity gas HAZARD PROPERTIES MSDS main hazards nfpa health nfpa flammability nfpa reactivity nfpa special flash point r phrases s phrases RTECS number CHEMICAL PROPERTIES XLogP 1.3 isoelectric point 5.89 disociation constant 2.38, 9.34 tautomers H bond donor 3 H bond acceptor 4 PHARMACOLOGICAL PROPERTIES References refbegin note 1 a EINECS 73 22 3 EINECS for Tryptophan note 2 a PubChem 9060 note 3 a PubChem 6305 refend AminoAcids Category Chemical data pages ar ... more details
Copy to Wikimedia Commons By Richard Wheeler Zephyris 2006. For the Wikipedia Wikiproject Metabolic Pathways metabolic pathways wikiproject. Licensing GFDL self with disclaimers migration relicense Category Unclassified Chemical Structures ... more details
TDO is an acronym that may refer to TDO connector , the telephone plug used in Austria. The Delicious One , the Wienerschnitzel s mascot. Tryptophan 2,3 dioxygenase , an enzyme in the metabolism of tryptophan Territorial Defence Organization of Yugoslavia Test Data Output disambig de TDO it TDO ... more details
HTK may refer to HTK software , a hidden Markov model software tool Histidine tryptophan ketoglutarate , a preservative for donor organs Kaman HTK , a helicopter disambig de HTK ... more details
Image L phenylalanine skeletal.png thumb phenylalanine Image L tryptophan skeletal.png thumb tryptophan Image L tyrosine skeletal.png thumb tyrosine Image Histidin Histidine.svg thumb histidine Image Thyroxine 2D skeletal.png thumb thyroxine Aromatic amino acids are amino acids that include an Aromaticity aromatic ring. Examples include Among 20 standard amino acids phenylalanine , tryptophan , histidine and tyrosine Others thyroxine See also Aromatic L amino acid decarboxylase Phenylalanine , histidine , and tryptophan are essential amino acids. Since they are not synthesized in the human body, they must be derived from the diet. Tyrosine is semi essential it can be synthesized, but only from phenylalanine. A lack of the enzyme phenylalanine hydroxylase used in tyrosine synthesis causes phenylketonuria . Many plants and microorganisms synthesize aromatic amino acids. Many herbicides inhibit aromatic acid synthesis, which is why they can be toxic to pets and humans. Clarify date July 2010 External links MeshName Aromatic Amino Acids MetabolismMap Category Amino acids Category Aromatic amino acids biochemistry stub zh ... more details
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