2.0 2012-05-31 13:47:33 -0600 2015-06-03 15:53:50 -0600 ECMDB01201 M2MDB000296 Guanosine diphosphate Guanosine 5'-(trihydrogen diphosphate). A guanine nucleotide containing two phosphate groups esterified to the sugar moiety. It is an ester of pyrophosphoric acid with the nucleoside guanosine. GDP consists of the pyrophosphate group, the pentose sugar ribose, and the nucleobase guanine. GDP is the product of GTP dephosphorylation by GTPases, e.g. the G-proteins that are involved in signal transduction. 5'-GDP GDP Guanosine 5'-(trihydrogen pyrophosphate) Guanosine 5'-(trihydrogen pyrophosphoric acid) Guanosine 5'-diphosphate Guanosine 5'-diphosphoric acid Guanosine 5'-pyrophosphate Guanosine 5'-pyrophosphoric acid Guanosine diphosphoric acid Guanosine mono(trihydrogen diphosphate) Guanosine mono(trihydrogen diphosphoric acid) Guanosine pyrophosphate Guanosine pyrophosphoric acid Guanosine-5'-diphosphate Guanosine-5'-diphosphoric acid Guanosine-diphosphate Guanosine-diphosphoric acid PpG C10H15N5O11P2 443.2005 443.024329371 [({[(2R,3S,4R,5R)-5-(2-amino-6-oxo-6,9-dihydro-3H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy]phosphonic acid {[(2R,3S,4R,5R)-5-(2-amino-6-oxo-3H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy(hydroxy)phosphoryl}oxyphosphonic acid 146-91-8 NC1=NC2=C(N=CN2[C@@H]2O[C@H](COP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]2O)C(=O)N1 InChI=1S/C10H15N5O11P2/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(25-9)1-24-28(22,23)26-27(19,20)21/h2-3,5-6,9,16-17H,1H2,(H,22,23)(H2,19,20,21)(H3,11,13,14,18)/t3-,5-,6-,9-/m1/s1 QGWNDRXFNXRZMB-UUOKFMHZSA-N Solid Cytosol Extra-organism Periplasm logp -1.51 ALOGPS logs -2.00 ALOGPS solubility 4.44e+00 g/l ALOGPS logp -3.7 ChemAxon pka_strongest_acidic 1.71 ChemAxon pka_strongest_basic 2.55 ChemAxon iupac [({[(2R,3S,4R,5R)-5-(2-amino-6-oxo-6,9-dihydro-3H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy]phosphonic acid ChemAxon average_mass 443.2005 ChemAxon mono_mass 443.024329371 ChemAxon smiles NC1=NC2=C(N=CN2[C@@H]2O[C@H](COP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]2O)C(=O)N1 ChemAxon formula C10H15N5O11P2 ChemAxon inchi InChI=1S/C10H15N5O11P2/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(25-9)1-24-28(22,23)26-27(19,20)21/h2-3,5-6,9,16-17H,1H2,(H,22,23)(H2,19,20,21)(H3,11,13,14,18)/t3-,5-,6-,9-/m1/s1 ChemAxon inchikey QGWNDRXFNXRZMB-UUOKFMHZSA-N ChemAxon polar_surface_area 248.28 ChemAxon refractivity 85.93 ChemAxon polarizability 34.74 ChemAxon rotatable_bond_count 6 ChemAxon acceptor_count 13 ChemAxon donor_count 7 ChemAxon physiological_charge -3 ChemAxon formal_charge 0 ChemAxon Alanine, aspartate and glutamate metabolism ec00250 Purine metabolism ec00230 Porphyrin and chlorophyll metabolism ec00860 Metabolic pathways eco01100 Aspartate metabolism Aspartate (seen in the center) is synthesized from and degraded to oxaloacetate , an intermediate of the TCA cycle, by a reversible transamination reaction with glutamate. As shown here, AspC is the principal transaminase that catalyzes this reaction, but TyrB also catalyzes it. Null mutations in aspC do not confer aspartate auxotrophy; null mutations in both aspC and tyrB do. Aspartate is a constituent of proteins and participates in several other biosyntheses as shown here( NAD biosynthesis and Beta-Alanine Metabolism . Approximately 27 percent of the cell's nitrogen flows through aspartate Aspartate can be synthesized from fumaric acid through a aspartate ammonia lyase. Aspartate also participates in the synthesis of L-asparagine through two different methods, either through aspartate ammonia ligase or asparagine synthetase B. Aspartate is also a precursor of fumaric acid. Again it has two possible ways of synthesizing it. First set of reactions follows an adenylo succinate synthetase that yields adenylsuccinic acid and then adenylosuccinate lyase in turns leads to fumaric acid. The second way is through argininosuccinate synthase that yields argininosuccinic acid and then argininosuccinate lyase in turns leads to fumaric acid PW000787 Metabolic purine nucleotides de novo biosynthesis The biosynthesis of purine nucleotides is a complex process that begins with a phosphoribosyl pyrophosphate. This compound interacts with water and L-glutamine through a amidophosphoribosyl transferase resulting in a pyrophosphate, L-glutamic acid and a 5-phosphoribosylamine. The latter compound proceeds to interact with a glycine through an ATP driven phosphoribosylamine-glycine ligase resulting in the addition of glycine to the compound. This reaction releases an ADP, a phosphate, a hydrogen ion and a N1-(5-phospho-β-D-ribosyl)glycinamide. The latter compound interacts with formic acid, through an ATP driven phosphoribosylglycinamide formyltransferase 2 resulting in a phosphate, an ADP, a hydrogen ion and a 5-phosphoribosyl-N-formylglycinamide. The latter compound interacts with L-glutamine, and water through an ATP-driven phosphoribosylformylglycinamide synthetase resulting in a release of a phosphate, an ADP, a hydrogen ion, a L-glutamic acid and a 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine. The latter compound interacts with an ATP driven phosphoribosylformylglycinamide cyclo-ligase resulting in a release of ADP, a phosphate, a hydrogen ion and a 5-aminoimidazole ribonucleotide. The latter compound interacts with a hydrogen carbonate through an ATP driven N5-carboxyaminoimidazole ribonucleotide synthetase resulting in a release of a phosphate, an ADP, a hydrogen ion and a N5-carboxyaminoimidazole ribonucleotide.The latter compound then interacts with a N5-carboxyaminoimidazole ribonucleotide mutase resulting in a 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate. This compound interacts with an L-aspartic acid through an ATP driven phosphoribosylaminoimidazole-succinocarboxamide synthase resulting in a phosphate, an ADP, a hydrogen ion and a SAICAR. SAICAR interacts with an adenylosuccinate lyase resulting in a fumaric acid and an AICAR. AICAR interacts with a formyltetrahydrofolate through a AICAR transformylase / IMP cyclohydrolase resulting in a release of a tetrahydropterol mono-l-glutamate and a FAICAR. The latter compound, FAICAR, interacts in a reversible reaction through a AICAR transformylase / IMP cyclohydrolase resulting in a release of water and Inosinic acid. Inosinic acid can be metabolized to produce dGTP and dATP three different methods each. dGTP: Inosinic acid, water and NAD are processed by IMP dehydrogenase resulting in a release of NADH, a hydrogen ion and Xanthylic acid. Xanthylic acid interacts with L-glutamine, and water through an ATP driven GMP synthetase resulting in pyrophosphate, AMP, L-glutamic acid, a hydrogen ion and Guanosine monophosphate. The latter compound is the phosphorylated by reacting with an ATP driven guanylate kinase resulting in a release of ADP and a Gaunosine diphosphate. Guanosine diphosphate can be metabolized in three different ways: 1.-Guanosine diphosphate is phosphorylated by an ATP-driven nucleoside diphosphate kinase resulting in an ADP and a Guanosine triphosphate. This compound interacts with a reduced flavodoxin protein through a ribonucleoside-triphosphate reductase resulting in a oxidized flavodoxin a water moleculer and a dGTP 2.-Guanosine diphosphate interacts with a reduced NrdH glutaredoxin-like proteins through a ribonucleoside-diphosphate reductase 2 resulting in the release of an oxidized NrdH glutaredoxin-like protein, a water molecule and a dGDP. The dGDP is then phosphorylated by interacting with an ATP-driven nucleoside diphosphate kinase resulting in an ADP and dGTP. 3.-Guanosine diphosphate interacts with a reduced thioredoxin ribonucleoside diphosphate reductase 1 resulting in a release of a water molecule, an oxidized thioredoxin and a dGDP. The dGDP is then phosphorylated by interacting with an ATP-driven nucleoside diphosphate kinase resulting in an ADP and dGTP. dATP: Inosinic acid interacts with L-aspartic acid through an GTP driven adenylosuccinate synthase results in the release of GDP, a hydrogen ion, a phosphate and N(6)-(1,2-dicarboxyethyl)AMP. The latter compound is then cleaved by a adenylosuccinate lyase resulting in a fumaric acid and an Adenosine monophosphate. This compound is then phosphorylated by an adenylate kinase resulting in the release of ATP and an adenosine diphosphate. Adenosine diphosphate can be metabolized in three different ways: 1.-Adenosine diphosphate is involved in a reversible reaction by interacting with a hydrogen ion and a phosphate through a ATP synthase / thiamin triphosphate synthase resulting in a hydrogen ion, a water molecule and an Adenosine triphosphate. The adenosine triphosphate interacts with a reduced flavodoxin through a ribonucleoside-triphosphate reductase resulting in an oxidized flavodoxin, a water molecule and a dATP 2.- Adenosine diphosphate interacts with an reduced thioredoxin through a ribonucleoside diphosphate reductase 1 resulting in a release of a water molecule, a oxidized thioredoxin and a dADP. The dADP is then phosphorylated by a nucleoside diphosphate kinase resulting in the release of ADP and a dATP 3.- Adenosine diphosphate interacts with an reduced NrdH glutaredoxin-like protein through a ribonucleoside diphosphate reductase 2 resulting in a release of a water molecule, a oxidized glutaredoxin-like protein and a dADP. The dADP is then phosphorylated by a nucleoside diphosphate kinase resulting in the release of ADP and a dATP PW000910 Metabolic purine nucleotides de novo biosynthesis 1435709748 PW000960 Metabolic purine nucleotides de novo biosynthesis 2 The biosynthesis of purine nucleotides is a complex process that begins with a phosphoribosyl pyrophosphate. This compound interacts with water and L-glutamine through a amidophosphoribosyl transferase resulting in a pyrophosphate, L-glutamic acid and a 5-phosphoribosylamine. The latter compound proceeds to interact with a glycine through an ATP driven phosphoribosylamine-glycine ligase resulting in the addition of glycine to the compound. This reaction releases an ADP, a phosphate, a hydrogen ion and a N1-(5-phospho-β-D-ribosyl)glycinamide. The latter compound interacts with formic acid, through an ATP driven phosphoribosylglycinamide formyltransferase 2 resulting in a phosphate, an ADP, a hydrogen ion and a 5-phosphoribosyl-N-formylglycinamide. The latter compound interacts with L-glutamine, and water through an ATP-driven phosphoribosylformylglycinamide synthetase resulting in a release of a phosphate, an ADP, a hydrogen ion, a L-glutamic acid and a 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine. The latter compound interacts with an ATP driven phosphoribosylformylglycinamide cyclo-ligase resulting in a release of ADP, a phosphate, a hydrogen ion and a 5-aminoimidazole ribonucleotide. The latter compound interacts with a hydrogen carbonate through an ATP driven N5-carboxyaminoimidazole ribonucleotide synthetase resulting in a release of a phosphate, an ADP, a hydrogen ion and a N5-carboxyaminoimidazole ribonucleotide(5-Phosphoribosyl-5-carboxyaminoimidazole).The latter compound then interacts with a N5-carboxyaminoimidazole ribonucleotide mutase resulting in a 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate. This compound interacts with an L-aspartic acid through an ATP driven phosphoribosylaminoimidazole-succinocarboxamide synthase resulting in a phosphate, an ADP, a hydrogen ion and a SAICAR. SAICAR interacts with an adenylosuccinate lyase resulting in a fumaric acid and an AICAR. AICAR interacts with a formyltetrahydrofolate through a AICAR transformylase / IMP cyclohydrolase resulting in a release of a tetrahydropterol mono-l-glutamate and a FAICAR. The latter compound, FAICAR, interacts in a reversible reaction through a AICAR transformylase / IMP cyclohydrolase resulting in a release of water and Inosinic acid. Inosinic acid can be metabolized to produce dGTP and dATP three different methods each. dGTP: Inosinic acid, water and NAD are processed by IMP dehydrogenase resulting in a release of NADH, a hydrogen ion and Xanthylic acid. Xanthylic acid interacts with L-glutamine, and water through an ATP driven GMP synthetase resulting in pyrophosphate, AMP, L-glutamic acid, a hydrogen ion and Guanosine monophosphate. The latter compound is the phosphorylated by reacting with an ATP driven guanylate kinase resulting in a release of ADP and a Gaunosine diphosphate. Guanosine diphosphate can be metabolized in three different ways: 1.-Guanosine diphosphate is phosphorylated by an ATP-driven nucleoside diphosphate kinase resulting in an ADP and a Guanosine triphosphate. This compound interacts with a reduced flavodoxin protein through a ribonucleoside-triphosphate reductase resulting in a oxidized flavodoxin a water moleculer and a dGTP 2.-Guanosine diphosphate interacts with a reduced NrdH glutaredoxin-like proteins through a ribonucleoside-diphosphate reductase 2 resulting in the release of an oxidized NrdH glutaredoxin-like protein, a water molecule and a dGDP. The dGDP is then phosphorylated by interacting with an ATP-driven nucleoside diphosphate kinase resulting in an ADP and dGTP. 3.-Guanosine diphosphate interacts with a reduced thioredoxin ribonucleoside diphosphate reductase 1 resulting in a release of a water molecule, an oxidized thioredoxin and a dGDP. The dGDP is then phosphorylated by interacting with an ATP-driven nucleoside diphosphate kinase resulting in an ADP and dGTP. dATP: Inosinic acid interacts with L-aspartic acid through an GTP driven adenylosuccinate synthase results in the release of GDP, a hydrogen ion, a phosphate and N(6)-(1,2-dicarboxyethyl)AMP. The latter compound is then cleaved by a adenylosuccinate lyase resulting in a fumaric acid and an Adenosine monophosphate. This compound is then phosphorylated by an adenylate kinase resulting in the release of ATP and an adenosine diphosphate. Adenosine diphosphate can be metabolized in three different ways: 1.-Adenosine diphosphate is involved in a reversible reaction by interacting with a hydrogen ion and a phosphate through a ATP synthase / thiamin triphosphate synthase resulting in a hydrogen ion, a water molecule and an Adenosine triphosphate. The adenosine triphosphate interacts with a reduced flavodoxin through a ribonucleoside-triphosphate reductase resulting in an oxidized flavodoxin, a water molecule and a dATP 2.- Adenosine diphosphate interacts with an reduced thioredoxin through a ribonucleoside diphosphate reductase 1 resulting in a release of a water molecule, a oxidized thioredoxin and a dADP. The dADP is then phosphorylated by a nucleoside diphosphate kinase resulting in the release of ADP and a dATP 3.- Adenosine diphosphate interacts with an reduced NrdH glutaredoxin-like protein through a ribonucleoside diphosphate reductase 2 resulting in a release of a water molecule, a oxidized glutaredoxin-like protein and a dADP. The dADP is then phosphorylated by a nucleoside diphosphate kinase resulting in the release of ADP and a dATP PW002033 Metabolic adenosine nucleotides <i>de novo</i> biosynthesis PWY-6126 ppGpp biosynthesis PPGPPMET-PWY guanosine nucleotides <i>de novo</i> biosynthesis PWY-6125 salvage pathways of pyrimidine ribonucleotides PWY0-163 Specdb::CMs 21480 Specdb::CMs 37972 Specdb::CMs 147095 Specdb::NmrOneD 1660 Specdb::NmrOneD 4813 Specdb::NmrOneD 4814 Specdb::NmrOneD 87452 Specdb::NmrOneD 87453 Specdb::NmrOneD 87454 Specdb::NmrOneD 87455 Specdb::NmrOneD 87456 Specdb::NmrOneD 87457 Specdb::NmrOneD 87458 Specdb::NmrOneD 87459 Specdb::NmrOneD 87460 Specdb::NmrOneD 87461 Specdb::NmrOneD 87462 Specdb::NmrOneD 87463 Specdb::NmrOneD 87464 Specdb::NmrOneD 87465 Specdb::NmrOneD 87466 Specdb::NmrOneD 87467 Specdb::NmrOneD 87468 Specdb::NmrOneD 87469 Specdb::NmrOneD 87470 Specdb::NmrOneD 87471 Specdb::MsMs 1460 Specdb::MsMs 1461 Specdb::MsMs 1462 Specdb::MsMs 179532 Specdb::MsMs 179533 Specdb::MsMs 179534 Specdb::MsMs 181860 Specdb::MsMs 181861 Specdb::MsMs 181862 Specdb::MsMs 440101 Specdb::MsMs 451931 Specdb::MsMs 2226693 Specdb::MsMs 2228051 Specdb::MsMs 2229089 Specdb::MsMs 2230341 Specdb::MsMs 2231416 Specdb::MsMs 2232802 Specdb::MsMs 2233746 Specdb::MsMs 2235181 Specdb::MsMs 2314190 Specdb::MsMs 2314191 Specdb::MsMs 2314192 Specdb::MsMs 2621066 Specdb::MsMs 2621067 Specdb::MsMs 2621068 Specdb::NmrTwoD 1057 Specdb::NmrTwoD 1601 HMDB01201 8977 8630 C00035 17552 GDP GDP GDP 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 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 Buchholz, A., Takors, R., Wandrey, C. (2001). "Quantification of intracellular metabolites in Escherichia coli K12 using liquid chromatographic-electrospray ionization tandem mass spectrometric techniques." Anal Biochem 295:129-137. 11488613 Chantin C, Bonin B, Boulieu R, Bory C: Liquid-chromatographic study of purine metabolism abnormalities in purine nucleoside phosphorylase deficiency. Clin Chem. 1996 Feb;42(2):326-8. 8595732 Edlin, Gordon; Donini, P. Synthesis of guanosine 5'-diphosphate, 2'-(or 3'-) diphosphate, and related nucleotides in a variety of physiological conditions. Journal of Biological Chemistry (1971), 246(13), 4371-3. Ribonucleoside-diphosphate reductase 1 subunit alpha P00452 RIR1_ECOLI nrdA http://ecmdb.ca/proteins/P00452.xml Polyribonucleotide nucleotidyltransferase P05055 PNP_ECOLI pnp http://ecmdb.ca/proteins/P05055.xml Bis(5'-nucleosyl)-tetraphosphatase [symmetrical] P05637 APAH_ECOLI apaH http://ecmdb.ca/proteins/P05637.xml Periplasmic AppA protein P07102 PPA_ECOLI appA http://ecmdb.ca/proteins/P07102.xml Nucleoside diphosphate kinase P0A763 NDK_ECOLI ndk http://ecmdb.ca/proteins/P0A763.xml Adenylosuccinate synthetase P0A7D4 PURA_ECOLI purA http://ecmdb.ca/proteins/P0A7D4.xml Uridine kinase P0A8F4 URK_ECOLI udk http://ecmdb.ca/proteins/P0A8F4.xml Pyruvate kinase I P0AD61 KPYK1_ECOLI pykF http://ecmdb.ca/proteins/P0AD61.xml Bifunctional adenosylcobalamin biosynthesis protein cobU P0AE76 COBU_ECOLI cobU http://ecmdb.ca/proteins/P0AE76.xml Phosphatase nudJ P0AEI6 NUDJ_ECOLI nudJ http://ecmdb.ca/proteins/P0AEI6.xml GTP pyrophosphokinase P0AG20 RELA_ECOLI relA http://ecmdb.ca/proteins/P0AG20.xml Bifunctional (p)ppGpp synthase/hydrolase SpoT P0AG24 SPOT_ECOLI spoT http://ecmdb.ca/proteins/P0AG24.xml Thioredoxin-2 P0AGG4 THIO2_ECOLI trxC http://ecmdb.ca/proteins/P0AGG4.xml Sulfate adenylyltransferase subunit 2 P21156 CYSD_ECOLI cysD http://ecmdb.ca/proteins/P21156.xml Pyruvate kinase II P21599 KPYK2_ECOLI pykA http://ecmdb.ca/proteins/P21599.xml Sulfate adenylyltransferase subunit 1 P23845 CYSN_ECOLI cysN http://ecmdb.ca/proteins/P23845.xml Mannose-1-phosphate guanylyltransferase P24174 MANC_ECOLI manC http://ecmdb.ca/proteins/P24174.xml Anaerobic ribonucleoside-triphosphate reductase P28903 NRDD_ECOLI nrdD http://ecmdb.ca/proteins/P28903.xml GDP-mannose mannosyl hydrolase P32056 NUDD_ECOLI nudD http://ecmdb.ca/proteins/P32056.xml Ribonucleoside-diphosphate reductase 2 subunit beta P37146 RIR4_ECOLI nrdF http://ecmdb.ca/proteins/P37146.xml Putative ribosome biogenesis GTPase RsgA P39286 RSGA_ECOLI rsgA http://ecmdb.ca/proteins/P39286.xml Ribonucleoside-diphosphate reductase 2 subunit alpha P39452 RIR3_ECOLI nrdE http://ecmdb.ca/proteins/P39452.xml Guanylate kinase P60546 KGUA_ECOLI gmk http://ecmdb.ca/proteins/P60546.xml Adenylate kinase P69441 KAD_ECOLI adk http://ecmdb.ca/proteins/P69441.xml Ribonucleoside-diphosphate reductase 1 subunit beta P69924 RIR2_ECOLI nrdB http://ecmdb.ca/proteins/P69924.xml Glutaredoxin-4 P0AC69 GLRX4_ECOLI grxD http://ecmdb.ca/proteins/P0AC69.xml Glutaredoxin-3 P0AC62 GLRX3_ECOLI grxC http://ecmdb.ca/proteins/P0AC62.xml Glutaredoxin-2 P0AC59 GLRX2_ECOLI grxB http://ecmdb.ca/proteins/P0AC59.xml Glutaredoxin-1 P68688 GLRX1_ECOLI grxA http://ecmdb.ca/proteins/P68688.xml Thioredoxin-1 P0AA25 THIO_ECOLI trxA http://ecmdb.ca/proteins/P0AA25.xml Nucleoside diphosphate kinase P0A763 NDK_ECOLI ndk http://ecmdb.ca/proteins/P0A763.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 Guanosine diphosphate + Reduced Thioredoxin > dGDP + Water + Oxidized Thioredoxin Guanosine diphosphate + glutaredoxin > dGDP + glutaredoxin + Water Adenosine triphosphate + Guanosine diphosphate <> ADP + Guanosine triphosphate R00330 GDPKIN-RXN Adenosine triphosphate + Guanosine triphosphate + Water + Sulfate > Adenosine phosphosulfate + Guanosine diphosphate + Phosphate + Pyrophosphate Adenosine triphosphate + Guanosine diphosphate > Adenosine monophosphate + Hydrogen ion + Guanosine 3',5'-bis(diphosphate) GDPPYPHOSKIN-RXN P1,P4-Bis(5'-guanosyl) tetraphosphate + Water >2 Guanosine diphosphate +2 Hydrogen ion Adenosine monophosphate + Guanosine triphosphate <> ADP + Guanosine diphosphate Guanosine triphosphate + Water > Guanosine diphosphate + Hydrogen ion + Phosphate 3.6.5.1-RXN Guanosine diphosphate + Hydrogen ion + D-Mannose 1-phosphate > Guanosine diphosphate mannose + Phosphate Guanosine diphosphate mannose + Water > Guanosine diphosphate + Hydrogen ion + D-Mannose GDPMANMANHYDRO-RXN Cytidine + Guanosine triphosphate > Cytidine monophosphate + Guanosine diphosphate + Hydrogen ion R00517 CYTIDINEKIN-RXN Guanosine triphosphate + Uridine > Guanosine diphosphate + Hydrogen ion + Uridine 5'-monophosphate R00968 URKI-RXN Adenosine triphosphate + Guanosine monophosphate <> ADP + Guanosine diphosphate R00332 GUANYL-KIN-RXN Water + Guanosine 3',5'-bis(diphosphate) <> Guanosine diphosphate + Pyrophosphate R00336 PPGPPSYN-RXN L-Aspartic acid + Guanosine triphosphate + Inosinic acid <> Adenylsuccinic acid + Guanosine diphosphate +2 Hydrogen ion + Phosphate R01135 Guanosine triphosphate + Pyruvic acid <> Guanosine diphosphate + Phosphoenolpyruvic acid R00430 RNA + Phosphate <> RNA + Guanosine diphosphate R00439 Guanosine triphosphate + Cytidine <> Guanosine diphosphate + Cytidine monophosphate R00517 Guanosine triphosphate + Uridine <> Guanosine diphosphate + Uridine 5'-monophosphate R00968 Guanosine triphosphate + Inosinic acid + L-Aspartic acid <> Guanosine diphosphate + Phosphate + Adenylsuccinic acid R01135 dGDP + Thioredoxin disulfide + Water <> Guanosine diphosphate + Thioredoxin R02019 Adenosyl cobinamide + Guanosine triphosphate <> Adenosyl cobinamide phosphate + Guanosine diphosphate R06558 L-Aspartic acid + Inosinic acid + Guanosine triphosphate > Hydrogen ion + adenylo-succinate + Phosphate + Guanosine diphosphate ADENYLOSUCCINATE-SYNTHASE-RXN GDP-&alpha;-D-glucose + Water > Hydrogen ion + b-D-Glucose + Guanosine diphosphate GDP-GLUCOSIDASE-RXN Guanosine diphosphate + Adenosine triphosphate > Guanosine triphosphate + ADP GDPKIN-RXN Adenosine triphosphate + Guanosine diphosphate > Adenosine monophosphate + Guanosine 3',5'-bis(diphosphate) GDPPYPHOSKIN-RXN Guanosine diphosphate + Water > Hydrogen ion + Guanosine monophosphate + Phosphate GUANOSINE-DIPHOSPHATASE-RXN Guanosine 3',5'-bis(diphosphate) + Water > Hydrogen ion + Pyrophosphate + Guanosine diphosphate PPGPPSYN-RXN Guanosine diphosphate mannose + Water > Guanosine diphosphate + D-Mannose Adenosine triphosphate + Guanosine monophosphate > ADP + Guanosine diphosphate Guanosine triphosphate + Water > Guanosine diphosphate + Inorganic phosphate Guanosine triphosphate + Inosinic acid + L-Aspartic acid > Guanosine diphosphate + Inorganic phosphate + N(6)-(1,2-dicarboxyethyl)AMP Guanosine 3',5'-bis(diphosphate) + Water > Guanosine diphosphate + Pyrophosphate Adenosine triphosphate + Guanosine triphosphate + Adenosyl cobinamide <> Adenosyl cobinamide phosphate + ADP + Guanosine diphosphate R05221 R06558 Succinyl-CoA + Phosphate + Guanosine diphosphate + Succinyl-CoA <> Succinic acid + Coenzyme A + Guanosine triphosphate PW_R002578 Guanosine triphosphate + Inosinic acid + L-Aspartic acid + L-Aspartic acid > Guanosine diphosphate + Phosphate + N(6)-(1,2-dicarboxyethyl)AMP PW_R002648 Inosinic acid + L-Aspartic acid + Guanosine triphosphate + L-Aspartic acid > Guanosine diphosphate + Phosphate +2 Hydrogen ion + N(6)-(1,2-dicarboxyethyl)AMP + Adenylsuccinic acid PW_R003424 Guanosine monophosphate + Adenosine triphosphate > Adenosine diphosphate + Guanosine diphosphate + ADP PW_R003428 Guanosine diphosphate + Adenosine triphosphate > Adenosine diphosphate + Guanosine triphosphate + ADP PW_R003429 Guanosine diphosphate + reduced thioredoxin > oxidized thioredoxin + Water + dGDP + dGDP PW_R003431 Guanosine diphosphate + a reduced NrdH glutaredoxin-like protein > Water + an oxidized NrdH glutaredoxin-like protein + dGDP + dGDP PW_R003433 L-Aspartic acid + Guanosine triphosphate + Inosinic acid <> Adenylsuccinic acid + Guanosine diphosphate +2 Hydrogen ion + Phosphate 0.2 g/L NH4Cl, 2.0 g/L (NH4)2SO4, 3.25 g/L KH2PO4, 2.5 g/L K2HPO4, 1.5 g/L NaH2PO4, 0.5 g/L MgSO4; trace substances: 10 mg/L CaCl2, 0.5 mg/L ZnSO4, 0.25 mg/L CuCl2, 0.25 mg/L MnSO4, 0.175 mg/L CoCl2, 0.125 mg/L H3BO3, 2.5 mg/L AlCl3, 0.5 mg/L Na2MoO4, 10 Bioreactor, pH controlled, aerated, dilution rate=0.125 L/h 30.0 uM 2.0 37 oC K12 Stationary Phase, glucose limited 120000 8000 Buchholz, A., Takors, R., Wandrey, C. (2001). "Quantification of intracellular metabolites in Escherichia coli K12 using liquid chromatographic-electrospray ionization tandem mass spectrometric techniques." Anal Biochem 295:129-137. 11488613 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 676.0 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 2704000 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 23.2 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 92800 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 17.7 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 70800 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 180.0 uM 0.0 37 oC BW25113 Stationary Phase, glucose limited 720000 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