2.0 2012-05-31 09:55:42 -0600 2015-09-13 12:56:05 -0600 ECMDB00034 M2MDB000010 Adenine Adenine is a purine base. Adenine is found in both DNA and RNA. Adenine is a fundamental component of adenine nucleotides. Adenine forms adenosine, a nucleoside, when attached to ribose, and deoxyadenosine when attached to deoxyribose; it forms adenosine triphosphate (ATP), a nucleotide, when three phosphate groups are added to adenosine. Adenosine triphosphate is used in cellular metabolism as one of the basic methods of transferring chemical energy between chemical reactions. 1,6-Dihydro-6-iminopurine 1H-Purin-6-amine 1H-Purine-6-amine 3,6-Dihydro-6-iminopurine 6-Amino-1H-purine 6-Amino-3H-purine 6-Amino-7H-purine 6-Amino-9H-purine 6-Amino-Purine 6-Aminopurine 9H-Purin-6-amine 9H-Purin-6-yl-amin 9H-Purin-6-ylamine 9H-Purine-6-amine Ade Adenin Adenine Adeninimine Vitamin B4 C5H5N5 135.1267 135.054495185 7H-purin-6-amine vitamin B4 73-24-5 NC1=C2NC=NC2=NC=N1 InChI=1S/C5H5N5/c6-4-3-5(9-1-7-3)10-2-8-4/h1-2H,(H3,6,7,8,9,10) GFFGJBXGBJISGV-UHFFFAOYSA-N Solid Cytosol Extra-organism Periplasm logp -0.38 ALOGPS logs -1.07 ALOGPS solubility 1.15e+01 g/l ALOGPS melting_point 360 oC logp -0.57 ChemAxon pka_strongest_acidic 10.29 ChemAxon pka_strongest_basic 3.64 ChemAxon iupac 7H-purin-6-amine ChemAxon average_mass 135.1267 ChemAxon mono_mass 135.054495185 ChemAxon smiles NC1=C2NC=NC2=NC=N1 ChemAxon formula C5H5N5 ChemAxon inchi InChI=1S/C5H5N5/c6-4-3-5(9-1-7-3)10-2-8-4/h1-2H,(H3,6,7,8,9,10) ChemAxon inchikey GFFGJBXGBJISGV-UHFFFAOYSA-N ChemAxon polar_surface_area 80.48 ChemAxon refractivity 38.22 ChemAxon polarizability 12.29 ChemAxon rotatable_bond_count 0 ChemAxon acceptor_count 4 ChemAxon donor_count 2 ChemAxon physiological_charge 0 ChemAxon formal_charge 0 ChemAxon Purine metabolism ec00230 Cysteine and methionine metabolism ec00270 Pantothenate and CoA biosynthesis The CoA biosynthesis requires compounds from two other pathways: aspartate metabolism and valine biosynthesis. It requires a Beta-Alanine and R-pantoate. The compound (R)-pantoate is generated in two reactions, as shown by the interaction of alpha-ketoisovaleric acid, 5,10 methylene-THF and water through a 3-methyl-2-oxobutanoate hydroxymethyltransferase resulting in a tetrahydrofolic acid and a 2-dehydropantoate. This compound interacts with hydrogen through a NADPH driven acetohydroxy acid isomeroreductase resulting in the release of NADP and R-pantoate. On the other hand L-aspartic acid interacts with a hydrogen ion and gets decarboxylated through an Aspartate 1- decarboxylase resulting in a carbon dioxide and a Beta-alanine. Beta-alanine and R-pantoate interact with an ATP driven pantothenate synthetase resulting in pyrophosphate, AMP, hydrogen ion and pantothenic acid. Pantothenic acid is phosphorylated through a ATP-driven pantothenate kinase resulting in a ADP, a hydrogen ion and D-4'-Phosphopantothenate. This compound interacts with a CTP and a L-cysteine resulting in a fused 4'-phosphopantothenoylcysteine decarboxylase and phosphopantothenoylcysteine synthetase resulting in a hydrogen ion, a pyrophosphate, a CMP and 4-phosphopantothenoylcysteine. The latter compound interacts with a hydrogen ion through a fused 4'-phosphopantothenoylcysteine decarboxylase and phosphopantothenoylcysteine synthetase resulting in a carbon dioxide release and a 4-phosphopantetheine. This compound interacts with an ATP, hydrogen ion and an phosphopantetheine adenylyltransferase resulting in a release of pyrophosphate, and dephospho-CoA. Dephospho-CoA reacts with an ATP driven dephospho-CoA kinase resulting in a ADP , a hydrogen ion and a Coenzyme A. . The latter is converted into (R)-4'-phosphopantothenate is two steps, involving a β-alanine ligase and a kinase. In most organsims the ligase acts before the kinase (EC 6.3.2.1, pantoate—β-alanine ligase (AMP-forming) followed by EC 2.7.1.33, pantothenate kinase, as described in phosphopantothenate biosynthesis I and phosphopantothenate biosynthesis II. However, in archaea the order is reversed, and EC 2.7.1.169, pantoate kinase acts before EC 6.3.2.36, 4-phosphopantoate—β-alanine ligase, as described in phosphopantothenate biosynthesis III. The kinases are feedback inhibited by CoA itself, accounting for the primary regulatory mechanism of CoA biosynthesis. The addition of L-cysteine to (R)-4'-phosphopantothenate, resulting in the formation of R-4'-phosphopantothenoyl-L-cysteine (PPC), is followed by decarboxylation of PPC to 4'-phosphopantetheine. The ultimate reaction is catalyzed by EC 2.7.1.24, dephospho-CoA kinase, which converts 4'-phosphopantetheine to CoA. All enzymes of this pathway are essential for growth. The reactions in the biosynthetic route towards CoA are identical in most organisms, although there are differences in the functionality of the involved enzymes. In plants every step is catalyzed by single monofunctional enzymes, whereas in bacteria and mammals bifunctional enzymes are often employed [Rubio06]. PW000828 ec00770 Metabolic Phosphonate and phosphinate metabolism ec00440 Two-component system ec02020 Metabolic pathways eco01100 Collection of Reactions without pathways PW001891 Metabolic Quorum Sensing Bacterial Autoinducer 2 (AI-2) mediates the quorum sensing 2 system. AI-2 is catalyzed by the luxS enzyme. This enzyme is found in E.coli and S.typhimurium. In E. coli and most pathogenic bacteria that form AI-2 are spontaneous transformations that include cyclization to (2R,4S)-2-methyl-2,4-dihydroxydihydrofuran-3-one and hydration to the final autoinducer (2R,4S)-2-methyl-2,3,3,4-tetrahydroxytetrahydrofuran. This product is released from the cell through the AI-2 transporter (tqsA). As the level of AI-2 increases, other cells detect it and import it through the autoinducer-2 ABC transporter (lsrACDB). AI-2 is then degraded in the cells by phosphorylating the AI-2 which is then isomerized to P-HPD which follows by the transfer of and acetyl group to coenzyme A and releases dihydroxyacetone phosphate PW000836 Signaling S-adenosyl-L-methionine biosynthesis S-adenosyl-L-methionine biosynthesis(SAM) is synthesized in the cytosol of the cell from L-methionine and ATP. This reaction is catalyzed by methionine adenosyltransferase. L methione is taken up from the environment through a complex reaction coupled transport and then proceeds too synthesize the s adenosylmethionine through a adenosylmethionine synthase. The S-adenosylmethionine then interacts with a hydrogen ion through a adenosylmethionine decarboxylase resulting in a carbon dioxide and a S-adenosyl 3-methioninamine.This compound interacts with a putrescine through a spermidine synthase resulting in a spermidine, a hydrogen ion and a S-methyl-5'-thioadenosine. The latter compound is degraded by interacting with a water molecule through a 5' methylthioadenosine nucleosidase resulting in a adenine and a S-methylthioribose which is then release into the environment PW000837 Metabolic preQ0 metabolism PreQ0 or 7-cyano-7-carbaguanine is biosynthesized by degrading GTP. GTP first interacts with water through a GTP cyclohydrolase resulting in the release of a formate, a hydrogen ion and a 7,8-dihydroneopterin 3'-triphosphate. The latter compound then interacts with water through a 6-carboxy-5,6,7,8-tetrahydropterin synthase resulting in a acetaldehyde, triphosphate, 2 hydrogen ion and 6-carboxy-5,6,7,8-tetrahydropterin. The latter compound then reacts spontaneously with a hydrogen ion resulting in the release of a ammonium molecule and a 7-carboxy-7-deazaguanine. This compound then interacts with ATP and ammonium through 7-cyano-7-deazaguanine synthase resulting in the release of water, phosphate, ADP, hydrogen ion and a 7-cyano-7-carbaguanine. The degradation of 7-cyano-7-deazaguanine can lead to produce a preQ1 or a queuine by reacting with 3 hydrogen ions and 2 NADPH through a 7-cyano-7-deazaguanine reductase. PreQ1 then interacts with a guanine 34 in tRNA through a tRNA-guanine transglycosylase resulting in a release of a guanine and a 7-aminomethyl-7-deazaguanosine 34 in tRNA. This nucleic acid then interacts with SAM through a S-adenosylmethionine tRNA ribosyltransferase-isomerase resulting in a release of a hydrogen ion, L-methionine, adenine and an epoxyqueuosine PW001893 Metabolic Citrate lyase activation The citrate lyase activation starts with a 3-dephospho-CoA reacting with ATP and a hydrogen ion through a triphosphoribosyl-dephospho-CoA synthase resulting in a adenine and a 2'-(5'-triphospho-alpha-D-ribosyl)-3'-dephospho-CoA. The latter compound in turn reacts with with a citrate lyase acyl-carrier protein through a apo-citrate lyase phosphoribosyl-dephospho-CoA transferase resulting in the release of a pyrophosphate and a hydrogen ion and a holo citrate lyase acyl-carrier protein.This protein complex can either react with a hydrogen ion and a acetate resulting in the release of a water and an acetyl-holo citrate lyase acyl-carrier protein. The holo acyl-carrier protein creacts with an ATP and an acetate through a citrate lyase synthase resulting in the release of an AMP, a pyrophosphate and an acetyl-holo citrate lyase acyl-ccarrier protein. The holo citrate lyase acyl-carrier protein can also interact with an S-acetyl phosphopantethiene resulting in the release of a 4-phosphopantethiene and an acetyl-holo citrate lyase acyl-carrier protein. PW002075 Metabolic adenine and adenosine salvage I The salvage of adenine begins with adenine being transporter into the cytosol through a adeP hydrogen symporter. Once in the cytosol adenine is degraded by reacting with a ribose-1-phosphate through an adenosine phosphorylase resulting in the release of a phosphate and adenosine. Adenosine is then deaminated by reacting with water, a hydrogen ion and an adenosine deaminase resulting in the release of an ammonium and a inosine . Inosine then reacts with a phosphate through a inosine phosphorylase resulting in the release of a ribose 1-phosphate and a hypoxanthine. Hypoxanthine reacts with a PRPP through a hypoxanthine phosphoribosyltransferase resulting in the release of a pyrophosphate and a IMP molecule. PW002069 Metabolic adenine and adenosine salvage II The salvage of adenine begins with adenine being transporter into the cytosol through a adeP hydrogen symporter. Once in the cytosol adenine is degraded by reacting with a ribose-1-phosphate through an adenosine phosphorylase resulting in the release of a phosphate and adenosine. Adenosine is then deaminated by reacting with water, a hydrogen ion and an adenosine deaminase resulting in the release of an ammonium and a inosine . Inosine can then be phosphorylated through an ATP driven inosine kinase resulting in the release of an ADP, a hydrogen ion and a IMP PW002071 Metabolic adenine and adenosine salvage III Adenosine is first incorporated into the cytosol through either a nupG or a nupC transporter. Once in the cytosol, adenosine is degraded into adenine by reacting with a water and a adenosine nucleosidase, releasing a D-ribofuranose and a adenine. The adenine then reacts with a PRPP through a adenine phosphoribosyltransferase resulting in the release of a pyrophosphate and an AMP PW002072 Metabolic methylphosphonate degradation I The pathway of methylphosphonate degradation starts with methylphosphonate being degrade by an ATP driven methylphosphonate degradation complex resulting in a alpha-D-ribose-1-methylphosphonate-5-triphosphate. This compound in turn is degraded by a water driven RPnTP hydrolase resulting in the release of a hydrogen ion, a pyrophosphate and a alpha-Dribose-1-methylphosphonate 5-phosphate. The latter compound is then involved with a carbon-phosphorous lyase resulting in the release of a methane and a 5-phospho-alpha-D-ribose 1,2-cyclic phosphate. This compound in turn gets degraded by a water driven 5-phospho-alpha-D-ribosyl 1,2-cyclic phosphate phosphodiesterase resulting in the release of a hydrogen ion and a alpha-D-ribose 1,5-biphosphate. PW002065 Metabolic purine deoxyribonucleosides degradation PW002077 Metabolic purine ribonucleosides degradation Purine ribonucleoside degradation leads to the production of alpha-D-ribose-1-phosphate. Xanthosine is transported into the cytosol through a xapB. Once in the cytosol xanthosine interacts with phosphate through a xanthosine phosphorylase resulting in the release of a xanthine and a alpha-D-ribose-1-phosphate. Adenosine is transported through a nupC or a nupG transporter, once inside the cytosol it can either react with a phosphate through a adenosine phosphorylase resultin in the release of a adenine and an alpha-D-ribose-1-phosphate. Adenosine reacts with water and hydrogen ion through a adenosine deaminase resulting in the release of ammonium and inosine. Inosine reacts with phosphate through a inosine phosphorylase resulting in the release of a hypoxanthine and an alpha-D-ribose-1-phosphate. Guanosine reacts with a phosphate through a guanosine phosphorylase resulting in the release of a guanine and a alpha-D-ribose-1-phosphate. PW002076 Metabolic S-adenosyl-L-methionine cycle The S-adenosyl-L-methionine cycle starts with S-adenosyl-L-methionine reacting with (a demethylated methyl donor ) dimethylglycine resulting in the release of a hydrogen ion, a betain (a methylated methyl donor) and a S-adenosyl-L-homocysteine. The s-adenosyl-L-homocysteine reacts with a water molecule through a S-adenosylhomocysteine nucleosidase resulting in the release of a adenine and a ribosyl-L-homocysteine. This compound in turn reacts with a s-ribosylhomocysteine lyase resulting in the release of a l-homocysteine and a autoinducer 2. The L-homocysteine reacts with a N5-methyl-tetrahydropteroyl tri-L-glutamate through a methionine synthase resulting in the release of a tetrahydropteroyl tri-L-glutamate and a methione. The methionine in turn reacts with a water molecule and ATP molecule through a methionine adenosyltransferase resulting in the release of a diphosphate, a phosphate and a s-adenosyl-L-methionine. PW002080 Metabolic Spermidine biosynthesis and metabolism Spermidine metabolism starts with S-adenosyl-L-methionine reacting with a hydrogen ion through a adenosylmethionine decarboxylase resulting in the release of a carbon dioxide and a S-adenosyl 3-(methylthio)propylamine. The later compound in turn reacts with putrescine resulting in the release of a hydrogen ion, a spermidine and a S-methyl-5'-thioadenosine. S-methyl-5'-thioadenosine in turn reacts with a water molecule through a 5-methylthioadenosine nucleosidase resulting in the release of a adenine and a S-methyl-5-thio-D-ribose which in in turn is released into the environment. PW002085 Metabolic methylphosphonate degradation PWY0-1533 adenine and adenosine salvage III PWY-6609 adenine and adenosine salvage V PWY-6611 purine ribonucleosides degradation to ribose-1-phosphate PWY0-1296 adenine and adenosine salvage II PWY-6605 purine deoxyribonucleosides degradation PWY0-1297 queuosine biosynthesis PWY-6700 2'-(5'-phosphoribosyl)-3'-dephospho-CoA biosynthesis I (citrate lyase) P2-PWY <i>S</i>-adenosyl-L-methionine cycle I PWY-6151 autoinducer AI-2 biosynthesis I PWY-6153 adenosine nucleotides degradation III PWY-6617 <i>S</i>-methyl-5'-thioadenosine degradation IV PWY0-1391 Specdb::CMs 288 Specdb::CMs 289 Specdb::CMs 290 Specdb::CMs 1580 Specdb::CMs 1634 Specdb::CMs 1639 Specdb::CMs 3464 Specdb::CMs 30172 Specdb::CMs 30472 Specdb::CMs 30821 Specdb::CMs 30964 Specdb::CMs 30965 Specdb::CMs 30966 Specdb::CMs 32043 Specdb::CMs 155635 Specdb::EiMs 411 Specdb::NmrOneD 1043 Specdb::NmrOneD 2599 Specdb::NmrOneD 3302 Specdb::NmrOneD 5412 Specdb::NmrOneD 5413 Specdb::NmrOneD 5414 Specdb::NmrOneD 5415 Specdb::NmrOneD 5416 Specdb::NmrOneD 5417 Specdb::NmrOneD 5418 Specdb::NmrOneD 5419 Specdb::NmrOneD 5420 Specdb::NmrOneD 5421 Specdb::NmrOneD 5422 Specdb::NmrOneD 5423 Specdb::NmrOneD 5424 Specdb::NmrOneD 5425 Specdb::NmrOneD 5426 Specdb::NmrOneD 5427 Specdb::NmrOneD 5428 Specdb::NmrOneD 5429 Specdb::NmrOneD 5430 Specdb::NmrOneD 5431 Specdb::MsMs 2622 Specdb::MsMs 2628 Specdb::MsMs 2629 Specdb::MsMs 438799 Specdb::MsMs 439015 Specdb::MsMs 439016 Specdb::MsMs 440031 Specdb::MsMs 440100 Specdb::MsMs 2226196 Specdb::MsMs 2226223 Specdb::MsMs 2228463 Specdb::MsMs 2228526 Specdb::MsMs 2228579 Specdb::MsMs 2228590 Specdb::MsMs 2230819 Specdb::MsMs 2230838 Specdb::MsMs 2230891 Specdb::MsMs 2231003 Specdb::MsMs 2233177 Specdb::MsMs 2233440 Specdb::MsMs 2235516 Specdb::MsMs 2256339 Specdb::MsMs 2258262 Specdb::MsMs 57 Specdb::MsMs 58 Specdb::NmrTwoD 938 Specdb::NmrTwoD 1101 HMDB00034 190 185 C00147 16708 ADENINE ANE Adenine Keseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590. 21097882 Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114. 22080510 Vijayendran, C., Barsch, A., Friehs, K., Niehaus, K., Becker, A., Flaschel, E. (2008). "Perceiving molecular evolution processes in Escherichia coli by comprehensive metabolite and gene expression profiling." Genome Biol 9:R72. 18402659 van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25. 17765195 Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). "Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948. 18331064 Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599. 19561621 Ishii, N., Nakahigashi, K., Baba, T., Robert, M., Soga, T., Kanai, A., Hirasawa, T., Naba, M., Hirai, K., Hoque, A., Ho, P. Y., Kakazu, Y., Sugawara, K., Igarashi, S., Harada, S., Masuda, T., Sugiyama, N., Togashi, T., Hasegawa, M., Takai, Y., Yugi, K., Arakawa, K., Iwata, N., Toya, Y., Nakayama, Y., Nishioka, T., Shimizu, K., Mori, H., Tomita, M. (2007). "Multiple high-throughput analyses monitor the response of E. coli to perturbations." Science 316:593-597. 17379776 Sreekumar A, Poisson LM, Rajendiran TM, Khan AP, Cao Q, Yu J, Laxman B, Mehra R, Lonigro RJ, Li Y, Nyati MK, Ahsan A, Kalyana-Sundaram S, Han B, Cao X, Byun J, Omenn GS, Ghosh D, Pennathur S, Alexander DC, Berger A, Shuster JR, Wei JT, Varambally S, Beecher C, Chinnaiyan AM: Metabolomic profiles delineate potential role for sarcosine in prostate cancer progression. Nature. 2009 Feb 12;457(7231):910-4. 19212411 Eells JT, Spector R: Purine and pyrimidine base and nucleoside concentrations in human cerebrospinal fluid and plasma. Neurochem Res. 1983 Nov;8(11):1451-7. 6656991 Di Pietro V, Perruzza I, Amorini AM, Balducci A, Ceccarelli L, Lazzarino G, Barsotti P, Giardina B, Tavazzi B: Clinical, biochemical and molecular diagnosis of a compound homozygote for the 254 bp deletion-8 bp insertion of the APRT gene suffering from severe renal failure. Clin Biochem. 2006 Oct 19;. 17126311 Moriyama H, Iizuka T, Nagai M, Hoshi K: Adenine, an inhibitor of platelet aggregation, from the leaves of Cassia alata. Biol Pharm Bull. 2003 Sep;26(9):1361-4. 12951489 Liu Y, Xu G, Xu C, Garcia L, Lin CC, Yeh LT: Ultra sensitive method for the determination of 9-(2-phosphonylmethoxyethyl)adenine in human serum by liquid chromatography-tandem mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci. 2004 Apr 25;803(2):293-8. 15063338 Terry KL, De Vivo I, Titus-Ernstoff L, Shih MC, Cramer DW: Androgen receptor cytosine, adenine, guanine repeats, and haplotypes in relation to ovarian cancer risk. Cancer Res. 2005 Jul 1;65(13):5974-81. 15994977 Steiner MC, Evans R, Deacon SJ, Singh SJ, Patel P, Fox J, Greenhaff PL, Morgan MD: Adenine nucleotide loss in the skeletal muscles during exercise in chronic obstructive pulmonary disease. Thorax. 2005 Nov;60(11):932-6. Epub 2005 Jul 29. 16055624 Whitehead JW, Lee GP, Gharagozloo P, Hofer P, Gehrig A, Wintergerst P, Smyth D, McCoull W, Hachicha M, Patel A, Kyle DJ: 8-Substituted analogues of 3-(3-cyclopentyloxy-4-methoxy-benzyl)-8-isopropyl-adenine: highly potent and selective PDE4 inhibitors. J Med Chem. 2005 Feb 24;48(4):1237-43. 15715490 Reimers HJ, Packham MA, Mustard JF: Labeling of the releasable adenine nucleotides of washed human platelets. Blood. 1977 Jan;49(1):89-99. 401462 Hartmann S, Okun JG, Schmidt C, Langhans CD, Garbade SF, Burgard P, Haas D, Sass JO, Nyhan WL, Hoffmann GF: Comprehensive detection of disorders of purine and pyrimidine metabolism by HPLC with electrospray ionization tandem mass spectrometry. Clin Chem. 2006 Jun;52(6):1127-37. Epub 2006 Apr 13. 16613999 Ohdoi C, Nyhan WL, Kuhara T: Chemical diagnosis of Lesch-Nyhan syndrome using gas chromatography-mass spectrometry detection. J Chromatogr B Analyt Technol Biomed Life Sci. 2003 Jul 15;792(1):123-30. 12829005 Ruiz-Stewart I, Kazerounian S, Pitari GM, Schulz S, Waldman SA: Soluble guanylate cyclase is allosterically inhibited by direct interaction with 2-substituted adenine nucleotides. Eur J Biochem. 2002 Apr;269(8):2186-93. 11985597 Rolfes RJ: Regulation of purine nucleotide biosynthesis: in yeast and beyond. Biochem Soc Trans. 2006 Nov;34(Pt 5):786-90. 17052198 Simoni RE, Gomes LN, Scalco FB, Oliveira CP, Aquino Neto FR, de Oliveira ML: Uric acid changes in urine and plasma: an effective tool in screening for purine inborn errors of metabolism and other pathological conditions. J Inherit Metab Dis. 2007 Jun;30(3):295-309. Epub 2007 May 19. 17520339 Baddiley, J.; Lythgoe, B.; Todd, A. R. Synthesis of purine nucleosides. II. A new and convenient synthesis of adenine. Journal of the Chemical Society (1943), 386-7. http://hmdb.ca/system/metabolites/msds/000/000/024/original/HMDB00034.pdf?1358893297 Hypoxanthine phosphoribosyltransferase P0A9M2 HPRT_ECOLI hpt http://ecmdb.ca/proteins/P0A9M2.xml Purine nucleoside phosphorylase deoD-type P0ABP8 DEOD_ECOLI deoD http://ecmdb.ca/proteins/P0ABP8.xml AMP nucleosidase P0AE12 AMN_ECOLI amn http://ecmdb.ca/proteins/P0AE12.xml 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase P0AF12 MTNN_ECOLI mtnN http://ecmdb.ca/proteins/P0AF12.xml Riboflavin synthase alpha chain P0AFU8 RISA_ECOLI ribE http://ecmdb.ca/proteins/P0AFU8.xml Non-specific ribonucleoside hydrolase rihC P22564 RIHC_ECOLI rihC http://ecmdb.ca/proteins/P22564.xml Adenine deaminase P31441 ADEC_ECOLI ade http://ecmdb.ca/proteins/P31441.xml Pyrimidine-specific ribonucleoside hydrolase rihB P33022 RIHB_ECOLI rihB http://ecmdb.ca/proteins/P33022.xml Adenine phosphoribosyltransferase P69503 APT_ECOLI apt http://ecmdb.ca/proteins/P69503.xml 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase P77231 CITG_ECOLI citG http://ecmdb.ca/proteins/P77231.xml Alpha-ketoglutarate-dependent dioxygenase AlkB P05050 alkB http://ecmdb.ca/proteins/P05050.xml S-adenosylmethionine:tRNA ribosyltransferase-isomerase P0A7F9 QUEA_ECOLI queA http://ecmdb.ca/proteins/P0A7F9.xml Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL P16679 PHNL_ECOLI phnL http://ecmdb.ca/proteins/P16679.xml Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnI P16687 PHNI_ECOLI phnI http://ecmdb.ca/proteins/P16687.xml Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnH P16686 PHNH_ECOLI phnH http://ecmdb.ca/proteins/P16686.xml Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnG P16685 PHNG_ECOLI phnG http://ecmdb.ca/proteins/P16685.xml Xanthine permease XanP P0AGM9 XANP_ECOLI xanP http://ecmdb.ca/proteins/P0AGM9.xml Probable adenine permease PurP P31466 PURP_ECOLI purP http://ecmdb.ca/proteins/P31466.xml Outer membrane protein N P77747 OMPN_ECOLI ompN http://ecmdb.ca/proteins/P77747.xml Outer membrane pore protein E P02932 PHOE_ECOLI phoE http://ecmdb.ca/proteins/P02932.xml Outer membrane protein F P02931 OMPF_ECOLI ompF http://ecmdb.ca/proteins/P02931.xml Outer membrane protein C P06996 OMPC_ECOLI ompC http://ecmdb.ca/proteins/P06996.xml Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnG P16685 PHNG_ECOLI phnG http://ecmdb.ca/proteins/P16685.xml Adenosine + Water > Adenine + Ribose R01245 S-Adenosylhomocysteine + Water <> Adenine + S-Ribosyl-L-homocysteine R00194 ADENOSYLHOMOCYSTEINE-NUCLEOSIDASE-RXN 5'-Methylthioadenosine + Water > 5-Methylthioribose + Adenine R01401 METHYLTHIOADENOSINE-NUCLEOSIDASE-RXN 5'-Deoxyadenosine + Water > 5'-Deoxyribose + Adenine RXN0-6550 Adenine + Phosphoribosyl pyrophosphate <> Adenosine monophosphate + Pyrophosphate R00190 ADENPRIBOSYLTRAN-RXN Adenosine triphosphate + Dephospho-CoA > 2'-(5-Triphosphoribosyl)-3'-dephospho-CoA + Adenine 2.7.8.25-RXN Adenosine monophosphate + Water <> Adenine + D-Ribose-5-phosphate R00182 AMP-NUCLEOSID-RXN Adenine + Hydrogen ion + Water > Hypoxanthine + Ammonium Adenosine + Phosphate <> Adenine + Ribose-1-phosphate ADENPHOSPHOR-RXN Deoxyadenosine + Phosphate <> Deoxyribose 1-phosphate + Adenine R02557 Adenosine monophosphate + Pyrophosphate <> Adenine + Phosphoribosyl pyrophosphate R00190 Adenine + Water <> Hypoxanthine + Ammonia R01244 Adenosine + Water <> Adenine + Ribose R01245 5'-Methylthioadenosine + Water <> Adenine + 5-Methylthioribose R01401 Adenosine + Phosphate <> Adenine + alpha-D-Ribose 1-phosphate R01561 Methylphosphonate + Adenosine triphosphate > &alpha;-D-ribose-1-methylphosphonate-5-triphosphate + Adenine RXN0-6732 Hydrogen ion + Dephospho-CoA + Adenosine triphosphate > 2'-(5-Triphosphoribosyl)-3'-dephospho-CoA + Adenine 2.7.8.25-RXN Water + Adenine > Ammonia + Hypoxanthine R01244 ADENINE-DEAMINASE-RXN Adenosine + Water > D-ribose + Adenine ADENOSINE-NUCLEOSIDASE-RXN S-Ribosyl-L-homocysteine + Adenine < S-Adenosylhomocysteine + Water R00194 ADENOSYLHOMOCYSTEINE-NUCLEOSIDASE-RXN Pyrophosphate + Adenosine monophosphate < Phosphoribosyl pyrophosphate + Adenine ADENPRIBOSYLTRAN-RXN Water + Adenosine monophosphate > D-Ribose-5-phosphate + Adenine AMP-NUCLEOSID-RXN Deoxyadenosine + Phosphate <> Adenine + deoxyribose-1-phosphate DEOXYADENPHOSPHOR-RXN N1-Methyladenine + Oxygen + Oxoglutaric acid > Hydrogen ion + Adenine + Carbon dioxide + Formaldehyde + Succinic acid RXN0-984 1-Ethyladenine + Oxygen + Oxoglutaric acid > Adenine + Carbon dioxide + Acetaldehyde + Succinic acid RXN0-986 Adenosine monophosphate + Pyrophosphate > Adenine + Phosphoribosyl pyrophosphate S-Adenosylhomocysteine + Water > S-Ribosyl-L-homocysteine + Adenine 5'-Methylthioadenosine + Water > S-methyl-5-thio-D-ribose + Adenine S-adenosyl-L-methionine + 7-Aminomethyl-7-deazaguanosine > L-Methionine + Adenine + epoxyqueuosine Adenosine triphosphate + Dephospho-CoA <> 2'-(5-Triphosphoribosyl)-3'-dephospho-CoA + Adenine R09675 Adenosine triphosphate + Methylphosphonate <> alpha-D-Ribose 1-methylphosphonate 5-triphosphate + Adenine R10185 S-Adenosylhomocysteine + Water > Adenine + S-ribosyl-L-homocysteine + S-ribosyl-L-homocysteine PW_R003067 5'-S-methyl-5'-thioadenosine + Water > 5-Methylthioribose + Adenine PW_R005167 7-aminomethyl-7-deazaguanosine34 in tRNA + S-adenosyl-L-methionine > Hydrogen ion + L-Methionine + Adenine + epoxyqueuosine PW_R005185 S-Adenosylhomocysteine + Water > Adenine PW_R006077 Adenosine + Water > beta-D-ribofuranose + Adenine PW_R006054 Methylphosphonate + Adenosine triphosphate > Adenine + alpha-D-Ribose 1-methylphosphonate 5-triphosphate PW_R006035 Adenine + Ribose-1-phosphate > Phosphate + Adenosine PW_R006047 Adenosine + Phosphate > Adenine + Ribose-1-phosphate PW_R006066 Deoxyadenosine + Phosphate > Adenine + Deoxyribose 1-phosphate PW_R006069 Adenine + Phosphoribosyl pyrophosphate > Pyrophosphate + Adenosine monophosphate PW_R006055 Adenosine triphosphate + Methylphosphonate <> alpha-D-Ribose 1-methylphosphonate 5-triphosphate + Adenine Adenosine monophosphate + Water <> Adenine + D-Ribose-5-phosphate Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glucose Shake flask and filter culture 1.47 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 5880 0 Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599. 19561621 Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glycerol Shake flask and filter culture 1.47 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 5880 0 Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599. 19561621 Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L acetate Shake flask and filter culture 1.47 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 5880 0 Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599. 19561621 48 mM Na2HPO4, 22 mM KH2PO4, 10 mM NaCl, 45 mM (NH4)2SO4, supplemented with 1 mM MgSO4, 1 mg/l thiamine·HCl, 5.6 mg/l CaCl2, 8 mg/l FeCl3, 1 mg/l MnCl2·4H2O, 1.7 mg/l ZnCl2, 0.43 mg/l CuCl2·2H2O, 0.6 mg/l CoCl2·2H2O and 0.6 mg/l Na2MoO4·2H2O. 4 g/L Gluco Bioreactor, pH controlled, O2 and CO2 controlled, dilution rate: 0.2/h 102.0 uM 0.0 37 oC BW25113 Stationary Phase, glucose limited 408000 0 Ishii, N., Nakahigashi, K., Baba, T., Robert, M., Soga, T., Kanai, A., Hirasawa, T., Naba, M., Hirai, K., Hoque, A., Ho, P. Y., Kakazu, Y., Sugawara, K., Igarashi, S., Harada, S., Masuda, T., Sugiyama, N., Togashi, T., Hasegawa, M., Takai, Y., Yugi, K., Arakawa, K., Iwata, N., Toya, Y., Nakayama, Y., Nishioka, T., Shimizu, K., Mori, H., Tomita, M. (2007). "Multiple high-throughput analyses monitor the response of E. coli to perturbations." Science 316:593-597. 17379776 Luria-Bertani (LB) media Shake flask 34.5 uM true 10.0 37 oC BL21 DE3 Stationary phase cultures (overnight culture) 138000 40000 Lin, Z., Johnson, L. C., Weissbach, H., Brot, N., Lively, M. O., Lowther, W. T. (2007). "Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function." Proc Natl Acad Sci U S A 104:9597-9602. 17535911