Chembox Verifiedfields changed verifiedrevid 477863841 ImageFile Thymidine diphosphate glucose.png ImageSize 200px IUPACName nowiki nowiki 2 R ,3 S ,5 R 3 hydroxy 5 5 methyl 2,4 dioxopyrimidin 1 yl oxolan 2 yl methoxy oxidophosphoryl 2 R ,3 R ,4 S ,5 S ,6 R 3,4,5 trihydroxy 6 hydroxymethyl oxan 2 yl hydrogen phosphate OtherNames TDP glucose dTDP glucose Section1 Chembox Identifiers CASNo Ref cascite changed ?? CASNo 2196 62 5 ChEMBL Ref ebicite correct EBI ChEMBL 412989 PubChem 25202390 ChEBI Ref ebicite correct EBI ChEBI 15700 SMILES CC1 CN C O NC1 O C H 2C C H C H O2 COP O O OP O O O C H 3 C H C H C H C H O3 CO O O O O ChEMBL Ref ebicite correct EBI ChEMBL 412989 PubChem 443210 ChemSpiderID Ref chemspidercite correct chemspider ChemSpiderID 391476 ChEBI Ref ebicite correct EBI ChEBI 15700 SMILES O C1 C C N C O N1 C H 2O C H C H O C2 COP O O OP O O O C H 3O C H C H O C H O C H 3O CO C StdInChI Ref stdinchicite correct chemspider StdInChI 1S C16H26N2O16P2 c1 6 3 18 16 25 17 14 6 24 10 2 7 20 9 31 10 5 30 35 26,27 34 36 28,29 33 15 13 23 12 22 11 21 8 4 19 32 15 h3,7 13,15,19 23H,2,4 5H2,1H3, H,26,27 H,28,29 H,17,24,25 t7 ,8 ,9 ,10 ,11 ,12 ,13 ,15 m0 s1 StdInChIKey Ref stdinchicite correct chemspider StdInChIKey YSYKRGRSMLTJNL URARBOGNSA N Section2 Chembox Properties C 16 H 26 N 2 O 16 P 2 Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition Thymidine diphosphate glucose often abbreviated dTDP glucose or TDP glucose is a nucleotide linked sugar consisting of thymidine diphosphate deoxythymidine diphosphate linked to glucose . It is the starting compound for the syntheses of many deoxysugar s. ref name Liu cite journal doi 10.1146 annurev.biochem.71.110601.135339 author Xue M. He and Hung wen Liu title Formation of unusual sugars Mechanistic studies and biosynthetic applications journal Annu Rev Biochem volume 71 issue pages 701 754 year 2002 pmid 12045109 ref Biosynthesis DTDP glucose is produced by the enzyme glucose ... more details
enzyme Name nucleoside triphosphate adenylate kinase EC number 2.7.4.10 CAS number 9026 74 8 IUBMB EC number 2 7 4 10 GO code 0046899 image width caption Orphan date February 2009 In enzymology , a nucleoside triphosphate adenylate kinase EC number 2.7.4.10 is an enzyme that catalysis catalyzes the chemical reaction nucleoside triphosphate AMP math rightleftharpoons math nucleoside diphosphate ADP Thus, the two substrate biochemistry substrates of this enzyme are nucleoside triphosphate and adenosine monophosphate AMP , whereas its two product chemistry products are nucleoside diphosphate and adenosine diphosphate ADP . 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 nucleoside triphosphate AMP phosphotransferase . Other names in common use include guanosine triphosphate adenylate kinase , nucleoside triphosphate adenosine monophosphate transphosphorylase , GTP AMP phosphotransferase , and isozyme 3 of adenylate kinase . This enzyme participates in pyrimidine metabolism . 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 1ZD8 and PDB link 2AK3 . References reflist 1 cite journal author Albrecht GJ date 1970 title Purification and properties of nucleoside triphosphate adenosine monophosphate transphosphorylase from beef heart mitochondria journal Biochemistry. volume 9 pages 2462&ndash 70 pmid 5423264 doi 10.1021 bi00814a011 issue 12 cite journal author CHIGA M, ROGERS AE, PLAUT GW date 1961 title Nucleotide transphosphorylases from liver. II. Purification and properties of a 6 oxypurine nucleoside triphosphate adenosine monophosphate transphosphorylase from swine liver journal J. Biol. Chem. volume 236 pages 1800&ndash 5 pmid 13693071 enzyme stub Category EC 2.7.4 Category Enzymes of known ... more details
enzyme Name guanosine triphosphate guanylyltransferase EC number 2.7.7.45 CAS number 54576 89 5 IUBMB EC number 2 7 7 45 GO code 0047351 image width caption In enzymology , a guanosine triphosphate guanylyltransferase EC number 2.7.7.45 is an enzyme that catalysis catalyzes the chemical reaction 2 GTP math rightleftharpoons math diphosphate P sub 1 sub ,P sub 4 sub bis 5 guanosyl tetraphosphate Hence, this enzyme has one substrate biochemistry substrate , guanosine triphosphate GTP , and two product chemistry products , diphosphate and P1,P4 bis 5 guanosyl tetraphosphate . 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 GTP GTP guanylyltransferase . Other names in common use include diguanosine tetraphosphate synthetase , GTP GTP guanylyltransferase , Gp4G synthetase , and guanosine triphosphate guanose triphosphate guanylyltransferase . References reflist 1 cite journal author Warner AH, Beers PC, Huang FL date 1974 title Biosynthesis of the diguanosine nucleotides. I. Purification and properties of an enzyme from yolk platelets of brine shrimp embryos journal Can. J. Biochem. volume 52 pages 231&ndash 40 pmid 4208243 issue 3 enzyme stub Category EC 2.7.7 Category Enzymes of unknown structure ... more details
enzyme Name nucleoside triphosphate diphosphatase EC number 3.6.1.19 CAS number 9075 54 1 IUBMB EC number 3 6 1 19 GO code 0047429 image width caption In enzymology , a nucleoside triphosphate diphosphatase EC number 3.6.1.19 is an enzyme that catalysis catalyzes the chemical reaction a nucleoside triphosphate H sub 2 sub O math rightleftharpoons math a nucleotide diphosphate Thus, the two substrate biochemistry substrates of this enzyme are nucleoside triphosphate and water H sub 2 sub O , whereas its two product chemistry products are nucleotide and diphosphate . This enzyme belongs to the family of hydrolase s, specifically those acting on acid anhydrides in phosphorus containing anhydrides. The systematic name of this enzyme class is nucleoside triphosphate diphosphohydrolase . This enzyme is also called nucleoside triphosphate pyrophosphatase . This enzyme participates in purine metabolism and pyrimidine metabolism . Structural studies As of late 2007, 5 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1V7R , PDB link 2CAR , PDB link 2E5X , PDB link 2I5D , and PDB link 2J4E . References reflist 1 cite journal author Chern CJ, MacDonald AB, Morris AJ date 1969 title Purification and properties of a nucleoside triphosphate pyrophosphohydrolase from red cells of the rabbit journal J. Biol. Chem. volume 244 pages 5489&ndash 95 pmid 4310599 issue 20 hydrolase stub Category EC 3.6.1 Category Enzymes of known structure ... more details
Multiple issues expert subject August 2008 cleanup August 2008 orphan February 2009 enzyme Name nucleoside triphosphate hexose 1 phosphate nucleotidyltransferase EC number 2.7.7.28 CAS number 37278 26 5 IUBMB EC number 2 7 7 28 GO code 0047339 image width caption In enzymology , a nucleoside triphosphate aldose 1 phosphate nucleotidyltransferase EC number 2.7.7.28 is an enzyme that catalysis catalyzes the chemical reaction nucleoside triphosphate alpha D aldose 1 phosphate math rightleftharpoons math diphosphate NDP hexose Thus, the two substrate biochemistry substrates of this enzyme are nucleoside triphosphate and alpha D aldose 1 phosphate , whereas its two product chemistry products are diphosphate and NDP hexose . 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 NTP alpha D aldose 1 phosphate nucleotidyltransferase . Other names in common use include NDP hexose pyrophosphorylase , hexose 1 phosphate nucleotidyltransferase , hexose nucleotidylating enzyme , nucleoside diphosphohexose pyrophosphorylase , hexose 1 phosphate guanylyltransferase , GTP alpha D hexose 1 phosphate guanylyltransferase , GDP hexose pyrophosphorylase , guanosine diphosphohexose pyrophosphorylase , nucleoside triphosphate hexose 1 phosphate nucleotidyltransferase , and NTP hexose 1 phosphate nucleotidyltransferase . References reflist 1 cite journal author Verachtert H, Rodriguez P, Bass ST, Hansen RG date 1966 title Purification and properties of guanosine diphosphate hexose pyrophosphorylase from mammalian tissues journal J. Biol. Chem. volume 241 pages 2007&ndash 13 pmid 5946626 issue 9 cite journal author Hansen RG, Verachtert H, Rodriguez P and Bass ST date 1966 title GDP hexose pyrophosphorylase from liver journal Methods Enzymol. volume 8 pages 269&ndash 271 doi 10.1016 0076 6879 66 08048 0 series Methods in Enzymology isbn 9780121818081 e ... more details
enzyme Name diphosphate protein phosphotransferase EC number 2.7.99.1 CAS number 74092 32 3 IUBMB EC number 2 7 99 1 GO code 0047321 image width caption Orphan date February 2009 In enzymology , a triphosphate protein phosphotransferase EC number 2.7.99.1 is an enzyme that catalysis catalyzes the chemical reaction triphosphate microsomal membrane protein math rightleftharpoons math diphosphate phospho microsomal membrane protein Thus, the two substrate biochemistry substrates of this enzyme are triphosphate and microsomal membrane protein , whereas its two product chemistry products are diphosphate and phospho microsomal membrane protein . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing groups that are not covered by other phosphotransferase families. The systematic name of this enzyme class is triphosphate microsomal membrane protein phosphotransferase . Other names in common use include diphosphate microsomal membrane protein O phosphotransferase , erroneous , DiPPT erroneous , pyrophosphate protein phosphotransferase erroneous , diphosphate protein phosphotransferase erroneous , diphosphate microsomal membrane protein O phosphotransferase , and erroneous . References reflist 1 cite journal author Lam KS, Kasper CB date 1980 title Pyrophosphate protein phosphotransferase a membrane bound enzyme of endoplasmic reticulum journal Proc. Natl. Acad. Sci. U.S.A. volume 77 pages 1927&ndash 31 pmid 6246514 doi 10.1073 pnas.77.4.1927 issue 4 pmc 348622 cite journal author Tsutsui K date 1986 title Tripolyphosphate is an alternative phosphodonor of the selective protein phosphorylation of liver microsomal membrane journal J. Biol. Chem. volume 261 pages 2645&ndash 53 pmid 3949741 issue 6 enzyme stub Category EC 2.7.99 Category Enzymes of unknown structure ... more details
E. coli functional characterization of the enzyme synthesizing adenosine thiamine triphosphate journal ... v446 n7132 full 446112a.html cite journal author Jordan F title Adenosine triphosphate and thiamine ... more details
enzyme Name galactose 1 phosphate thymidylyltransferase EC number 2.7.7.32 CAS number 9023 25 0 IUBMB EC number 2 7 7 32 GO code 0047342 image width caption In enzymology , a galactose 1 phosphate thymidylyltransferase EC number 2.7.7.32 is an enzyme that catalysis catalyzes the chemical reaction dTTP alpha D galactose 1 phosphate math rightleftharpoons math diphosphate dTDP galactose Thus, the two substrate biochemistry substrates of this enzyme are dTTP and alpha D galactose 1 phosphate , whereas its two product chemistry products are diphosphate and dTDP galactose . 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 dTTP alpha D galactose 1 phosphate thymidylyltransferase . Other names in common use include dTDP galactose pyrophosphorylase , galactose 1 phosphate thymidylyl transferase , thymidine diphosphogalactose pyrophosphorylase , thymidine triphosphate alpha D galactose 1 phosphate , and thymidylyltransferase . This enzyme participates in nucleotide sugars metabolism . References reflist 1 cite journal author Pazur JH and Anderson JS year 1963 title Thymidine triphosphate alpha D galactose 1 phosphate thymidylyltransferase from Streptococcus faecalis grown on D galactose journal J. Biol. Chem. volume 238 pages 3155&ndash 3160 pmid 14085355 Category EC 2.7.7 Category Enzymes of unknown structure enzyme stub ... more details
Image HAT Selection.png thumb 300px right HAT selection depicted by a plasmacytoma thymidine kinase mutant fused with a mortal splenic B cell . Otheruses Hat disambiguation HAT Medium hypoxanthine aminopterin thymidine medium is a selection medium for mammalian cell culture, which relies on the combination of aminopterin, a drug that acts as a powerful folate metabolism inhibitor by inhibiting dihydrofolate reductase , with hypoxanthine a purine derivative and thymidine a deoxy nucleoside which are intermediates in DNA synthesis . The trick is that aminopterin blocks DNA De novo synthesis de novo synthesis , which is absolutely required for cell division to proceed, but hypoxanthine and thymidine provide cells with the raw material to evade the blockage the salvage pathway , provided that they have the right enzymes , which means having functioning copies of the genes that encode them. The enzyme dihydrofolate reductase , which produces tetrahydrofolate THF by the reduction of dihydrofolate, is specifically blocked by aminopterin. THF, acting in association with specific protein s, can receive single carbon units that are then transferred to specific targets. One of the important targets for cellular reproduction is thymidylate synthase , which creates thymidine monophosphate TMP from deoxyuridine monophosphate dUMP . By additional phosphorylation reactions, TMP can be used to make thymidinetriphosphate TTP , one of the four nucleotide precursors that are used by DNA polymerases to create DNA . Without the THF required to convert dUMP, there can be no TTP, and DNA synthesis cannot proceed, unless TMP can be produced from another source. The alternative source is that thymidine present in HAT medium can be absorbed by the cells and phosphorylated by thymidine kinase TK into TMP. The synthesis of IMP, precursor to GMP and GTP, and to AMP and ATP also requires THF, and also can be bypassed. In this case hypoxanthine guanine phosphoribosyltransferase HGPRT reacts hypoxanthine ... more details
wiktionary TTP may refer to Tehrik i Taliban Pakistan Students Movement of Pakistan , the main Taliban militant umbrella group in Pakistan Tenderness to palpation, a medical diagnostic such as in Trochleitis Tactics, techniques and procedures, the actions and methods used under certain combat situations Tarleton State University Traditions Ten Tarleton Peppers , a tradition of Tarleton State University Thrombotic thrombocytopenic purpura , a blood disorder Thymidine triphosphate , one of the four nucleoside triphosphates that make up DNA Time Triggered Protocol , a concept related to networking Titan Pharmaceuticals , a California company with the stock symbol TTP TOS Takes Parameters .TTP , a program type for Atari TOS that takes arguments from a dialog box Tractatus Theologico Politicus , one of Spinoza s works Tristetraprolin , a protein Trophically transmitted parasite Trusted third party , an entity facilitating interactions between two other parties disambig de TTP fr TTP ko TTP it TTP ja TTP pl TTP sr TTP ... more details
1970 title Purification and properties of thymidine monophosphate kinase from mouse hepatoma journal ..., Carter CE date 1969 title Purification and characterization of Thymidine 5 monophosphate kinase from ... more details
A salvage pathway is a Metabolic pathway pathway in which nucleotide s purine and pyrimidine are synthesized from intermediates in the degradative pathway for nucleotides. Salvage pathways are used to recover bases and nucleosides that are formed during biodegradation degradation of RNA and DNA . This is important in some organs because some tissues cannot undergo de novo synthesis . The salvaged bases and nucleosides can then be converted back into nucleotides. Substrates The salvage pathway requires distinct substrates Pyrimidines Uridine phosphorylase adds ribose 1 phosphate to the free base uracil, forming uridine monophosphate. Uridine kinase then phosphorylates this nucleoside into its diphosphate and triphosphate forms. Deoxythymidine phosphorylase adds deoxyribose 1 phosphate to thymine, forming deoxythymidine monophosphate. Thymidine kinase can then phosphorylate this compound to deoxythymidine diphosphate and triphosphate. Image Pyrimidine Ribonucleotide Salvage.png thumb none 400px The salvage of pyrimidine ribonucleotides. Purines Phosphoribosyltransferases add activated ribose 5 phosphate called phosphoribosyl pyrophosphate or PRPP to bases, creating nucleotide monophosphates. There are two types of phosphoribosyltransferases adenine phosphoribosyltransferase APRT and hypoxanthine guanine phosphoribosyltransferase HGPRT . Lesch Nyhan syndrome is associated with a deficiency of HGPRT. class wikitable Nucleoside Enzyme Nucleotide hypoxanthine hypoxanthine guanine phosphoribosyl transferase HGPRT Inosine monophosphate IMP guanine hypoxanthine guanine phosphoribosyl transferase HGPRT Guanosine monophosphate GMP adenine adenine phosphoribosyltransferase APRT Adenosine monophosphate AMP External links http www.chem.brandeis.edu pochapsky research.html Enzymes in the methionine salvage pathway structure and function at Brandeis University Category Genetics genetics stub Protein metabolism Nucleotide metabolism ca Salvament de nucle tids de Salvage Pathway ja ... more details
may be attributed to two factors. First, cellular thymidine kinases phosphorylate the parent form significantly less rapidly than does the viral thymidine kinase, so the active triphosphate is present ... Penciclovir is inactive in its initial form. Within a virally infected cell a viral thymidine ... penciclovir triphosphate. This activated form inhibits viral DNA polymerase , thus impairing ... widely used aciclovir . A difference between aciclovir and penciclovir is that the active triphosphate ... more details
, guanosine , thymidine and inosine . Biological function Nucleosides can be phosphorylation phosphorylated ... s such as the thymidine monophosphate into nucleosides such as thymidine and phosphate. The nucleosides ... nucleotides See also Adenosine triphosphate ATP Nucleotide Nucleobase Synthesis of nucleosides Nucleobases ... more details
unreferenced date March 2012 File D glucopyranosyloxymethyluracil.svg thumb Anomer of Glucopyranosyloxymethyluracil File Synthesis of D glucopyranosyloxymethyluracil.svg thumb Biosynthesis of the base J D glucopyranosyloxymethyluracil with A Thymidine hydroxylase B beta glucosyltranferase 1 dT desoxy thymidine 2 HOCH3dU 3 dJ Glucopyranosyloxymethyluracil or Base J is a hypermodified base found in the DNA of kinetoplastids including the human pathogenic Trypanosomes . Base J is formed by the initial hydroxylation of thymidine and the subsequent glucosylation by an as yet unidentified glycosyltransferase . Category DNA de Glucopyranosyloxymethyluracil ... more details
for the similarly spelled B vitamin Thiamine chembox Verifiedfields changed Watchedfields changed verifiedrevid 458956008 ImageFile1 Thymine skeletal.svg ImageSize1 120px ImageFileL2 Thymine 3D balls.png ImageSizeL2 120px ImageFileR2 Thymine 3D vdW.png ImageSizeR2 120px IUPACName 5 Methylpyrimidine 2,4 1 H ,3 H dione OtherNames 5 methyluracil Section1 Chembox Identifiers CASNo 65 71 4 CASNo Ref cascite correct CAS ChEMBL Ref ebicite changed EBI ChEMBL 993 UNII Ref fdacite correct FDA UNII QR26YLT7LT PubChem 1135 ChemSpiderID Ref chemspidercite changed chemspider ChemSpiderID 1103 SMILES Cc1c nH c O nH c1 O InChI 1 C5H6N2O2 c1 3 2 6 5 9 7 4 3 8 h2H,1H3, H2,6,7,8,9 InChIKey RWQNBRDOKXIBIV UHFFFAOYAL StdInChI Ref stdinchicite changed chemspider StdInChI 1S C5H6N2O2 c1 3 2 6 5 9 7 4 3 8 h2H,1H3, H2,6,7,8,9 StdInChIKey Ref stdinchicite changed chemspider StdInChIKey RWQNBRDOKXIBIV UHFFFAOYSA N MeSHName Thymine Section2 Chembox Properties C 5 H 6 N 2 O 2 Appearance Density 1.23 g cm sup 3 sup calculated MeltingPtCL 316 MeltingPtCH 317 BoilingPtC 335 Boiling notes decomposes Section3 Chembox Hazards Solubility MainHazards FlashPt Autoignition Thymine T , Thy is one of the four nucleobase s in the nucleic acid of DNA that are represented by the letters G C A T. The others are adenine , guanine , and cytosine . Thymine is also known as 5 methyluracil, a pyrimidine nucleobase. As the name suggests, thymine may be derived by methylation of uracil at the 5th carbon. In RNA , thymine is replaced with uracil in most cases. In DNA, thymine T binds to adenine A via two hydrogen bonds, thus stabilizing the nucleic acid structures. Thymine combined with deoxyribose creates the nucleoside deoxythymidine , which is synonymous with the term thymidine . Thymidine can be phosphorylated with one, two, or three phosphoric acid groups, creating, respectively, TMP, TDP, or TTP thymidine mono , di , or triphosphate . One of the common mutations of DNA involves two adjacent thymines or cytosine ... more details
is an analogue of the nucleoside thymidine . The drug works because it is able to be incorporated .... The active compound is the 5 triphosphate of BVDU, which is formed in subsequent phosphorylations by viral thymidine kinase and presumably by nucleoside diphosphate kinase. The drug s name Brivudine ... more details
Stavudine is an analog chemistry analog of thymidine . It is phosphorylated by cellular kinase s into active triphosphate. Stavudine triphosphate inhibits the HIV reverse transcriptase by competing with natural substrate, thymidinetriphosphate. It also causes termination of DNA synthesis by incorporating ... more details
T7 DNA helicase is a hexameric motor protein that uses energy from Thymidinetriphosphate dTTP hydrolysis to process unidirectionally along single stranded DNA , separating the two strands as it progresses. Crystal structure The crystal structure was solved to 3.0 resolution in 2000, ref cite journal doi 10.1016 S0092 8674 00 80871 5 author Singleton MR, Sawaya MR, Ellenberger T, Wigley DB title Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides journal Cell volume 101 issue 6 pages 589 600 year 2000 month June pmid 10892646 url http linkinghub.elsevier.com retrieve pii S0092 8674 00 80871 5 ref as shown in the figure. In A , notice that the separate subunits appear to be anchored through interactions between an alpha helix and an adjacent subunit. In B , there are six sets of three loops. The red loop, known as loop II, contains three lysine residues and is thought to be involved in binding the ssDNA that is fed through the center of the enzyme. Mechanism of sequential dTTP hydrolysis Crampton et al. have proposed a mechanism for the ssDNA dependent hydrolysis of dTTP by T7 DNA helicase as shown in the figure below. ref cite journal author Crampton DJ, Mukherjee S, Richardson CC title DNA induced switch from independent to sequential dTTP hydrolysis in the bacteriophage T7 DNA helicase journal Mol. Cell volume 21 issue 2 pages 165 74 year 2006 month January pmid 16427007 doi 10.1016 j.molcel.2005.11.027 url http linkinghub.elsevier.com retrieve pii S1097 2765 05 01815 0 ref In their model, protein loops located on each hexameric subunit, each of which contain three lysine residues, sequentially interact with the negatively charged phosphate backbone of ssDNA. This interaction presumably causes a conformational change in the actively bound subunit, providing for the efficient release of dTDP from its dTTP binding site. In the process of dTDP release, the ssDNA is transferred to the neighboring subunit, which ... more details
Thymineless death is the phenomenon by which bacteria, yeasts and mammalian cells undergo irreversible cell death when they are starved of thymidine triphosphate dTTP , an essential precursor for DNA replication . ref name Ahmad cite journal last Ahmad first S. I. coauthors Kirk, S. H. Eisenstark, A. title Thymine Metabolism and Thymineless Death in Prokaryotes and Eukaryotes journal Annual Review of Microbiology year 1998 month October volume 52 pages 591 625 doi 10.1146 annurev.micro.52.1.591 pmid 9891809 url http www.annualreviews.org doi full 10.1146 annurev.micro.52.1.591 accessdate 3 October 2011 ref This phenomenon underlies the mechanism of action of several antibacterial , antimalarial and anticancer agents, such as Trimethoprim , Sulfamethoxazole , Methotrexate and Fluorouracil . ref name Ahmad ref ref Cite pmid 12724731 ref ref Cite pmid 373913 ref History The phenomenon was first reported in 1954 by Hazel D. Barner and Seymour S. Cohen in Escherichia coli when thymine requiring mutants of the bacterium lost viability when grown in a medium lacking thymine but containing other essential nutrients. ref Cite pmid 13183905 ref ref name scientist http www.the scientist.com news display 54259 50 years ago in cell biology A virologist recalls his work on cell growth inhibition ref Subsequently, this discovery led to the development of or explained the mechanism of action of several pyrimidine analogs that targeted thymine metabolism in bacteria and tumor cells. ref name scientist ref Cite pmid 16590300 ref The phenomenon was commonly attributed to unbalanced growth wherein cells continued fundamental processes of RNA transcription , protein synthesis and metabolism in the absence of DNA replication. ref Cite pmid 16589586 ref However, nutrient starvation generally do not kill cells to the extent as observed in cells that lack thymine. The molecular mechanism of thymineless death remains unknown ref name Ahmad ref DNA breaks were observed during thymineless deat ... more details
enzyme Name dTDP 4 amino 4,6 dideoxy D glucose transaminase EC number 2.6.1.33 CAS number 9023 19 2 IUBMB EC number 2 6 1 33 GO code 0019179 image width caption lowercase In enzymology , a dTDP 4 amino 4,6 dideoxy D glucose transaminase EC number 2.6.1.33 is an enzyme that catalysis catalyzes the chemical reaction dTDP 4 amino 4,6 dideoxy D glucose 2 oxoglutarate math rightleftharpoons math dTDP 4 dehydro 6 deoxy D glucose L glutamate Thus, the two substrate biochemistry substrates of this enzyme are dTDP 4 amino 4,6 dideoxy D glucose and 2 oxoglutarate , whereas its two product chemistry products are dTDP 4 dehydro 6 deoxy D glucose 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 dTDP 4 amino 4,6 dideoxy D glucose 2 oxoglutarate aminotransferase . Other names in common use include thymidine diphospho 4 amino 4,6 dideoxyglucose aminotransferase , thymidine diphospho 4 amino 6 deoxyglucose aminotransferase , thymidine diphospho 4 keto 6 deoxy D glucose transaminase , thymidine diphospho 4 keto 6 deoxy D glucose glutamic transaminase , and TDP 4 keto 6 deoxy D glucose transaminase . This enzyme participates in nucleotide sugars metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Matsuhashi M, Strominger JL date 1966 title Thymidine diphosphate 4 acetamido 2,6 dideoxyhexoses. 3 Purification and properties of thymidine diphosphate 4 keto 6 deoxy D glucose transaminase from Escherichia coli strain B journal J. Biol. Chem. volume 241 pages 4738&ndash 44 pmid 5332731 issue 20 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
Pfam box Symbol Thymidylate kin Name Thymidylate kinase Pfam PF02223 InterPro IPR000062 PROSITE PDOC01034 PDB PDB 1e2d PDB 1e2e PDB 1e2f PDB 1e2g PDB 1e2q PDB 1e98 PDB 1e99 PDB 1e9a PDB 1e9b PDB 1e9c Thymidylate kinase EC number 2.7.4.9 dTMP kinase catalyzes the phosphorylation of Thymidine monophosphate thymidine 5 monophosphate dTMP to form thymidine 5 diphosphate dTDP in the presence of ATP and magnesium ATP thymidine 5 phosphate math rightleftharpoons math ADP thymidine 5 diphosphate Thymidylate kinase is a ubiquitous enzyme of about 25 Kd and is important in the dTTP synthesis pathway for DNA synthesis. The function of dTMP kinase in eukaryotes comes from the study of a cell cycle mutant, cdc8, in Saccharomyces cerevisiae Saccharomyces cerevisiae . Structural and functional analyses suggest that the cDNA codes for authentic human dTMP kinase. The mRNA levels and enzyme activities corresponded to cell cycle progression and cell growth stages. ref name PUB00016913 cite journal author Li C, Huang SH, Tang A, Drisco B, Zhang SQ, Seeger R, Jong A title Human dTMP kinase gene expression and enzymatic activity coinciding with cell cycle progression and cell growth journal DNA Cell Biol. volume 13 issue 5 pages 461 471 year 1994 pmid 8024690 doi 10.1089 dna.1994.13.461 ref Subfamilies Predicted thymidylate kinase, TKRP1 InterPro IPR014505 Human proteins containing this domain DTYMK See also Thymidine kinase Thymidylate synthase References reflist InterPro content IPR000062 DEFAULTSORT Thymidylate Kinase Category Protein families protein stub ... more details
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