2.0 2012-05-31 13:54:06 -0600 2015-09-17 15:42:08 -0600 ECMDB01532 M2MDB000412 dATP dATP is a special carrier of energy and is the molecule adenosine triphosphate, or ATP. The ATP molecule is composed of three components. At the centre is a sugar molecule, [[ribose] (the same sugar that forms the basis of DNA). Attached to one side of this is a base (a group consisting of linked rings of carbon and nitrogen atoms); in this case the base is adenine. The other side of the sugar is attached to a string of phosphate groups. These phosphates are the key to the activity of ATP. ATP consists of a base, in this case adenine (red), a ribose (magenta) and a phosphate chain (blue). ATP works by losing the endmost phosphate group when instructed to do so by an enzyme. This reaction releases a lot of energy, which the organism can then use to build proteins, etc. 2'-Deoxy-5'-ATP 2'-Deoxy-ATP 2'-Deoxyadenosine 5'-triphosphate 2'-Deoxyadenosine 5'-triphosphoric acid 2'-Deoxyadenosine triphosphate 2'-Deoxyadenosine triphosphoric acid 2'-Deoxyadenosine-5'-triphosphate 2'-Deoxyadenosine-5'-triphosphoric acid 2'-DeoxyATP DATP Deoxy-ATP Deoxyadenosine 5'-triphosphate Deoxyadenosine 5'-triphosphoric acid Deoxyadenosine triphosphate Deoxyadenosine triphosphoric acid Deoxyadenosine-triphosphate Deoxyadenosine-triphosphoric acid C10H12N5O12P3 487.152 486.97172616 ({[({[(2R,3S,5R)-5-(6-amino-9H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy](hydroxy)phosphoryl}oxy)phosphonic acid dATP 1927-31-7 [H][C@]1(O)C[C@@]([H])(O[C@]1([H])COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)N1C=NC2=C(N)N=CN=C12 InChI=1S/C10H16N5O12P3/c11-9-8-10(13-3-12-9)15(4-14-8)7-1-5(16)6(25-7)2-24-29(20,21)27-30(22,23)26-28(17,18)19/h3-7,16H,1-2H2,(H,20,21)(H,22,23)(H2,11,12,13)(H2,17,18,19)/p-4/t5-,6+,7+/m0/s1 SUYVUBYJARFZHO-RRKCRQDMSA-J Solid Cytosol logp -0.66 ALOGPS logs -2.11 ALOGPS solubility 3.83e+00 g/l ALOGPS logp -4.9 ChemAxon pka_strongest_acidic 0.9 ChemAxon pka_strongest_basic 4.03 ChemAxon iupac ({[({[(2R,3S,5R)-5-(6-amino-9H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy](hydroxy)phosphoryl}oxy)phosphonic acid ChemAxon average_mass 487.152 ChemAxon mono_mass 486.97172616 ChemAxon smiles [H][C@]1(O)C[C@@]([H])(O[C@]1([H])COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)N1C=NC2=C(N)N=CN=C12 ChemAxon formula C10H12N5O12P3 ChemAxon inchi InChI=1S/C10H16N5O12P3/c11-9-8-10(13-3-12-9)15(4-14-8)7-1-5(16)6(25-7)2-24-29(20,21)27-30(22,23)26-28(17,18)19/h3-7,16H,1-2H2,(H,20,21)(H,22,23)(H2,11,12,13)(H2,17,18,19)/p-4/t5-,6+,7+/m0/s1 ChemAxon inchikey SUYVUBYJARFZHO-RRKCRQDMSA-J ChemAxon polar_surface_area 258.9 ChemAxon refractivity 94.3 ChemAxon polarizability 38.06 ChemAxon rotatable_bond_count 8 ChemAxon acceptor_count 13 ChemAxon donor_count 6 ChemAxon physiological_charge -3 ChemAxon formal_charge 0 ChemAxon Purine metabolism ec00230 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 Specdb::CMs 19054 Specdb::CMs 38109 Specdb::CMs 173053 Specdb::NmrOneD 1724 Specdb::NmrOneD 148080 Specdb::NmrOneD 148081 Specdb::NmrOneD 148082 Specdb::NmrOneD 148083 Specdb::NmrOneD 148084 Specdb::NmrOneD 148085 Specdb::NmrOneD 148086 Specdb::NmrOneD 148087 Specdb::NmrOneD 148088 Specdb::NmrOneD 148089 Specdb::NmrOneD 148090 Specdb::NmrOneD 148091 Specdb::NmrOneD 148092 Specdb::NmrOneD 148093 Specdb::NmrOneD 148094 Specdb::NmrOneD 148095 Specdb::NmrOneD 148096 Specdb::NmrOneD 148097 Specdb::NmrOneD 148098 Specdb::NmrOneD 148099 Specdb::MsMs 1628 Specdb::MsMs 1629 Specdb::MsMs 1630 Specdb::MsMs 179151 Specdb::MsMs 179152 Specdb::MsMs 179153 Specdb::MsMs 181476 Specdb::MsMs 181477 Specdb::MsMs 181478 Specdb::MsMs 2240717 Specdb::MsMs 2242747 Specdb::MsMs 2243080 Specdb::MsMs 3035690 Specdb::MsMs 3035691 Specdb::MsMs 3035692 Specdb::MsMs 3103793 Specdb::MsMs 3103794 Specdb::MsMs 3103795 Specdb::NmrTwoD 1665 HMDB01532 15993 15194 C00131 16284 DATP DTP Deoxyadenosine triphosphate 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 Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). 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Biochemical and Biophysical Research Communications (1960), 3 392-6. http://hmdb.ca/system/metabolites/msds/000/001/388/original/dATP_MSDS.pdf?1369421953 DNA polymerase I P00582 DPO1_ECOLI polA http://ecmdb.ca/proteins/P00582.xml DNA polymerase III subunit epsilon P03007 DPO3E_ECOLI dnaQ http://ecmdb.ca/proteins/P03007.xml DNA polymerase III subunit tau P06710 DPO3X_ECOLI dnaX http://ecmdb.ca/proteins/P06710.xml Nucleoside diphosphate kinase P0A763 NDK_ECOLI ndk http://ecmdb.ca/proteins/P0A763.xml Uridine kinase P0A8F4 URK_ECOLI udk http://ecmdb.ca/proteins/P0A8F4.xml DNA polymerase III subunit beta P0A988 DPO3B_ECOLI dnaN http://ecmdb.ca/proteins/P0A988.xml Anaerobic ribonucleoside-triphosphate reductase-activating protein P0A9N8 NRDG_ECOLI nrdG http://ecmdb.ca/proteins/P0A9N8.xml DNA polymerase III subunit theta P0ABS8 HOLE_ECOLI holE http://ecmdb.ca/proteins/P0ABS8.xml Pyruvate kinase I P0AD61 KPYK1_ECOLI pykF http://ecmdb.ca/proteins/P0AD61.xml Protein mazG P0AEY3 MAZG_ECOLI mazG http://ecmdb.ca/proteins/P0AEY3.xml Dihydroneopterin triphosphate pyrophosphatase P0AFC0 NUDB_ECOLI nudB http://ecmdb.ca/proteins/P0AFC0.xml DNA polymerase III subunit alpha P10443 DPO3A_ECOLI dnaE http://ecmdb.ca/proteins/P10443.xml Pyruvate kinase II P21599 KPYK2_ECOLI pykA http://ecmdb.ca/proteins/P21599.xml DNA polymerase III subunit delta P28630 HOLA_ECOLI holA http://ecmdb.ca/proteins/P28630.xml DNA polymerase III subunit delta' P28631 HOLB_ECOLI holB http://ecmdb.ca/proteins/P28631.xml DNA polymerase III subunit psi P28632 HOLD_ECOLI holD http://ecmdb.ca/proteins/P28632.xml Ferredoxin--NADP reductase P28861 FENR_ECOLI fpr http://ecmdb.ca/proteins/P28861.xml Anaerobic ribonucleoside-triphosphate reductase P28903 NRDD_ECOLI nrdD http://ecmdb.ca/proteins/P28903.xml DNA polymerase III subunit chi P28905 HOLC_ECOLI holC http://ecmdb.ca/proteins/P28905.xml Adenylate kinase P69441 KAD_ECOLI adk http://ecmdb.ca/proteins/P69441.xml Flavodoxin-2 P0ABY4 FLAW_ECOLI fldB http://ecmdb.ca/proteins/P0ABY4.xml Flavodoxin-1 P61949 FLAV_ECOLI fldA http://ecmdb.ca/proteins/P61949.xml Nucleoside diphosphate kinase P0A763 NDK_ECOLI ndk http://ecmdb.ca/proteins/P0A763.xml Adenosine triphosphate + 2 Flavodoxin reduced + 2 Hydrogen ion > dATP +2 flavodoxin semi oxidized + Water Adenosine triphosphate + dADP <> ADP + dATP R01137 DADPKIN-RXN dATP + Water > Deoxyadenosine monophosphate + Hydrogen ion + Pyrophosphate RXN0-384 dATP + Hydrogen ion + Water > 2'-Deoxyinosine triphosphate + Ammonium dATP + DNA <> Pyrophosphate + DNA R00375 dATP + Pyruvic acid <> dADP + Phosphoenolpyruvic acid R01138 dATP + Cytidine <> dADP + Cytidine monophosphate R01548 dATP + Uridine <> dADP + Uridine 5'-monophosphate R01549 dATP + Thioredoxin disulfide + Water <> Adenosine triphosphate + Thioredoxin R02014 dADP + Adenosine triphosphate > dATP + ADP DADPKIN-RXN dADP + Adenosine triphosphate + dADP > Adenosine diphosphate + dATP + ADP + dATP PW_R003438 Adenosine triphosphate + a reduced flavodoxin > an oxidized flavodoxin + Water + dATP + dATP PW_R003435 dATP + DNA <> Pyrophosphate dATP + Thioredoxin disulfide + Water <> Adenosine triphosphate + Thioredoxin dATP + DNA <> Pyrophosphate dATP + DNA <> Pyrophosphate dATP + DNA <> Pyrophosphate 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 15.5 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 62000 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 51.0 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 204000 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 68.5 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 274000 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 58.8 uM 0.0 37 oC BW25113 Stationary Phase, glucose limited 235200 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