2.02012-05-31 13:54:06 -06002015-09-17 15:42:08 -0600ECMDB01532M2MDB000412dATPdATP 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'-ATP2'-Deoxy-ATP2'-Deoxyadenosine 5'-triphosphate2'-Deoxyadenosine 5'-triphosphoric acid2'-Deoxyadenosine triphosphate2'-Deoxyadenosine triphosphoric acid2'-Deoxyadenosine-5'-triphosphate2'-Deoxyadenosine-5'-triphosphoric acid2'-DeoxyATPDATPDeoxy-ATPDeoxyadenosine 5'-triphosphateDeoxyadenosine 5'-triphosphoric acidDeoxyadenosine triphosphateDeoxyadenosine triphosphoric acidDeoxyadenosine-triphosphateDeoxyadenosine-triphosphoric acidC10H12N5O12P3487.152486.97172616({[({[(2R,3S,5R)-5-(6-amino-9H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy](hydroxy)phosphoryl}oxy)phosphonic aciddATP1927-31-7[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=C12InChI=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/s1SUYVUBYJARFZHO-RRKCRQDMSA-JSolidCytosollogp-0.66logs-2.11solubility3.83e+00 g/llogp-4.9pka_strongest_acidic0.9pka_strongest_basic4.03iupac({[({[(2R,3S,5R)-5-(6-amino-9H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy](hydroxy)phosphoryl}oxy)phosphonic acidaverage_mass487.152mono_mass486.97172616smiles[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=C12formulaC10H12N5O12P3inchiInChI=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/s1inchikeySUYVUBYJARFZHO-RRKCRQDMSA-Jpolar_surface_area258.9refractivity94.3polarizability38.06rotatable_bond_count8acceptor_count13donor_count6physiological_charge-3formal_charge0Purine metabolismec00230purine nucleotides de novo biosynthesisThe 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
PW000910Metabolicpurine nucleotides de novo biosynthesis 1435709748PW000960Metabolicpurine nucleotides de novo biosynthesis 2The 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 dATPPW002033Metabolicadenosine nucleotides <i>de novo</i> biosynthesisPWY-6126Specdb::CMs19054Specdb::CMs38109Specdb::CMs173053Specdb::NmrOneD1724Specdb::NmrOneD148080Specdb::NmrOneD148081Specdb::NmrOneD148082Specdb::NmrOneD148083Specdb::NmrOneD148084Specdb::NmrOneD148085Specdb::NmrOneD148086Specdb::NmrOneD148087Specdb::NmrOneD148088Specdb::NmrOneD148089Specdb::NmrOneD148090Specdb::NmrOneD148091Specdb::NmrOneD148092Specdb::NmrOneD148093Specdb::NmrOneD148094Specdb::NmrOneD148095Specdb::NmrOneD148096Specdb::NmrOneD148097Specdb::NmrOneD148098Specdb::NmrOneD148099Specdb::MsMs2240717Specdb::MsMs2242747Specdb::MsMs2243080Specdb::MsMs1628Specdb::MsMs1629Specdb::MsMs1630Specdb::MsMs181476Specdb::MsMs181477Specdb::MsMs181478Specdb::MsMs3035690Specdb::MsMs3035691Specdb::MsMs3035692Specdb::MsMs179151Specdb::MsMs179152Specdb::MsMs179153Specdb::MsMs3103793Specdb::MsMs3103794Specdb::MsMs3103795Specdb::NmrTwoD1665HMDB015321599315194C0013116284DATPDTPDeoxyadenosine triphosphateKeseler, 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-D590.21097882Kanehisa, 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-D114.22080510van 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 370:17-25.17765195Bennett, 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 5:593-599.19561621Ishii, 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 316:593-597.17379776Nespoli L, Porta F, Locatelli F, Aversa F, Carotti A, Lanfranchi A, Gibardi A, Marchesi ME, Abate L, Martelli MF, et al.: Successful lectin-separated bone marrow transplantation in adenosine deaminase deficiency-related severe immunodeficiency. Haematologica. 1990 Nov-Dec;75(6):546-50.2098297Hoffbrand AV, Ganeshaguru K, Hooton JW, Tattersall MH: Effect of iron deficiency and desferrioxamine on DNA synthesis in human cells. Br J Haematol. 1976 Aug;33(4):517-26.1009024Waddell D, Ullman B: Characterization of a cultured human T-cell line with genetically altered ribonucleotide reductase activity. Model for immunodeficiency. J Biol Chem. 1983 Apr 10;258(7):4226-31.6339493Bory C, Boulieu R, Souillet G, Chantin C, Guibaud P, Hershfield MS: Effect of polyethylene glycol-modified adenosine deaminase (PEG-ADA) therapy in two ADA-deficient children: measurement of erythrocyte deoxyadenosine triphosphate as a useful tool. Adv Exp Med Biol. 1991;309A:173-6.1789201Dang-Vu AP, Olsen EA, Vollmer RT, Greenberg ML, Hershfield MS: Treatment of cutaneous T cell lymphoma with 2'-deoxycoformycin (pentostatin). 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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?1369421953DNA polymerase IP00582DPO1_ECOLIpolAhttp://ecmdb.ca/proteins/P00582.xmlDNA polymerase III subunit epsilonP03007DPO3E_ECOLIdnaQhttp://ecmdb.ca/proteins/P03007.xmlDNA polymerase III subunit tauP06710DPO3X_ECOLIdnaXhttp://ecmdb.ca/proteins/P06710.xmlNucleoside diphosphate kinaseP0A763NDK_ECOLIndkhttp://ecmdb.ca/proteins/P0A763.xmlUridine kinaseP0A8F4URK_ECOLIudkhttp://ecmdb.ca/proteins/P0A8F4.xmlDNA polymerase III subunit betaP0A988DPO3B_ECOLIdnaNhttp://ecmdb.ca/proteins/P0A988.xmlAnaerobic ribonucleoside-triphosphate reductase-activating proteinP0A9N8NRDG_ECOLInrdGhttp://ecmdb.ca/proteins/P0A9N8.xmlDNA polymerase III subunit thetaP0ABS8HOLE_ECOLIholEhttp://ecmdb.ca/proteins/P0ABS8.xmlPyruvate kinase IP0AD61KPYK1_ECOLIpykFhttp://ecmdb.ca/proteins/P0AD61.xmlProtein mazGP0AEY3MAZG_ECOLImazGhttp://ecmdb.ca/proteins/P0AEY3.xmlDihydroneopterin triphosphate pyrophosphataseP0AFC0NUDB_ECOLInudBhttp://ecmdb.ca/proteins/P0AFC0.xmlDNA polymerase III subunit alphaP10443DPO3A_ECOLIdnaEhttp://ecmdb.ca/proteins/P10443.xmlPyruvate kinase IIP21599KPYK2_ECOLIpykAhttp://ecmdb.ca/proteins/P21599.xmlDNA polymerase III subunit deltaP28630HOLA_ECOLIholAhttp://ecmdb.ca/proteins/P28630.xmlDNA polymerase III subunit delta'P28631HOLB_ECOLIholBhttp://ecmdb.ca/proteins/P28631.xmlDNA polymerase III subunit psiP28632HOLD_ECOLIholDhttp://ecmdb.ca/proteins/P28632.xmlFerredoxin--NADP reductaseP28861FENR_ECOLIfprhttp://ecmdb.ca/proteins/P28861.xmlAnaerobic ribonucleoside-triphosphate reductaseP28903NRDD_ECOLInrdDhttp://ecmdb.ca/proteins/P28903.xmlDNA polymerase III subunit chiP28905HOLC_ECOLIholChttp://ecmdb.ca/proteins/P28905.xmlAdenylate kinaseP69441KAD_ECOLIadkhttp://ecmdb.ca/proteins/P69441.xmlFlavodoxin-2P0ABY4FLAW_ECOLIfldBhttp://ecmdb.ca/proteins/P0ABY4.xmlFlavodoxin-1P61949FLAV_ECOLIfldAhttp://ecmdb.ca/proteins/P61949.xmlNucleoside diphosphate kinaseP0A763NDK_ECOLIndkhttp://ecmdb.ca/proteins/P0A763.xmlAdenosine triphosphate + 2 Flavodoxin reduced + 2 Hydrogen ion > dATP +2 flavodoxin semi oxidized + WaterAdenosine triphosphate + dADP <> ADP + dATPR01137DADPKIN-RXNdATP + Water > Deoxyadenosine monophosphate + Hydrogen ion + PyrophosphateRXN0-384dATP + Hydrogen ion + Water > 2'-Deoxyinosine triphosphate + AmmoniumdATP + DNA <> Pyrophosphate + DNAR00375dATP + Pyruvic acid <> dADP + Phosphoenolpyruvic acidR01138dATP + Cytidine <> dADP + Cytidine monophosphateR01548dATP + Uridine <> dADP + Uridine 5'-monophosphateR01549dATP + Thioredoxin disulfide + Water <> Adenosine triphosphate + ThioredoxinR02014dADP + Adenosine triphosphate > dATP + ADPDADPKIN-RXNdADP + Adenosine triphosphate + dADP > Adenosine diphosphate + dATP + ADP + dATPPW_R003438Adenosine triphosphate + a reduced flavodoxin > an oxidized flavodoxin + Water + dATP + dATPPW_R003435dATP + DNA <> PyrophosphatedATP + Thioredoxin disulfide + Water <> Adenosine triphosphate + ThioredoxindATP + DNA <> PyrophosphatedATP + DNA <> PyrophosphatedATP + DNA <> PyrophosphateGutnick 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 glucoseShake flask and filter culture15.5uM0.037 oCK12 NCM3722Mid-Log Phase620000Bennett, 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 5:593-599.19561621Gutnick 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 glycerolShake flask and filter culture51.0uM0.037 oCK12 NCM3722Mid-Log Phase2040000Bennett, 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 5:593-599.19561621Gutnick 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 acetateShake flask and filter culture68.5uM0.037 oCK12 NCM3722Mid-Log Phase2740000Bennett, 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 5:593-599.1956162148 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 GlucoBioreactor, pH controlled, O2 and CO2 controlled, dilution rate: 0.2/h58.8uM0.037 oCBW25113Stationary Phase, glucose limited2352000Ishii, 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