2.02012-05-31 13:51:38 -06002015-09-13 12:56:11 -0600ECMDB01397M2MDB000369Guanosine monophosphateGuanosine 5'-monophosphate. A guanine nucleotide containing one phosphate group esterified to the sugar moiety and found widely in nature.5'-GMPE 626GGMPGuanidine monophosphateGuanidine monophosphoric acidGuanosine 5'-monophosphateGuanosine 5'-monophosphoric acidGuanosine 5'-phosphateGuanosine 5'-phosphorateGuanosine 5'-phosphoric acidGuanosine monophosphateGuanosine monophosphoric acidGuanosine-5'-monophosphateGuanosine-5'-monophosphoric acidGuanosine-5'-phosphateGuanosine-5'-phosphoric acidGuanosine-monophosphateGuanosine-monophosphoric acidGuanosine-phosphateGuanosine-phosphoric acidGuanylateGuanylic acidC10H14N5O8P363.2206363.057998961{[(2R,3S,4R,5R)-5-(2-amino-6-oxo-6,9-dihydro-1H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}phosphonic acidguanylate85-32-5NC1=NC2=C(N=CN2[C@@H]2O[C@H](COP(O)(O)=O)[C@@H](O)[C@H]2O)C(=O)N1InChI=1S/C10H14N5O8P/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(23-9)1-22-24(19,20)21/h2-3,5-6,9,16-17H,1H2,(H2,19,20,21)(H3,11,13,14,18)/t3-,5-,6-,9-/m1/s1RQFCJASXJCIDSX-UUOKFMHZSA-NSolidCytosolExtra-organismPeriplasmlogp-1.99logs-2.01solubility3.56e+00 g/llogp-3.1pka_strongest_acidic1.29pka_strongest_basic0.38iupac{[(2R,3S,4R,5R)-5-(2-amino-6-oxo-6,9-dihydro-1H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}phosphonic acidaverage_mass363.2206mono_mass363.057998961smilesNC1=NC2=C(N=CN2[C@@H]2O[C@H](COP(O)(O)=O)[C@@H](O)[C@H]2O)C(=O)N1formulaC10H14N5O8PinchiInChI=1S/C10H14N5O8P/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(23-9)1-22-24(19,20)21/h2-3,5-6,9,16-17H,1H2,(H2,19,20,21)(H3,11,13,14,18)/t3-,5-,6-,9-/m1/s1inchikeyRQFCJASXJCIDSX-UUOKFMHZSA-Npolar_surface_area201.75refractivity75.49polarizability30.7rotatable_bond_count4acceptor_count10donor_count6physiological_charge-2formal_charge0Purine metabolismec00230Drug metabolism - other enzymesec00983Porphyrin and chlorophyll metabolismec00860Metabolic pathwayseco01100purine 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 1435709748PW000960Metabolicguanine and guanosine salvageGuanosine can be converted into guanine through a phosphate driven guanosine phosphorylase resulting in the release of an alpha-D-ribose 1 phosphate and a guanine. This compound in turn reacts with a PRPP through a guanine phosphoribosyltransferase resulting in the release of a pyrophosphate and a GMP.
Guanosine can also react with and ATP driven guanosine kinase resulting in the release of an ADP, s hydrogen ion and a GMP
PW002074Metabolicpurine 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 dATPPW002033Metabolicguanosine nucleotides <i>de novo</i> biosynthesisPWY-6125guanosine nucleotides degradation IIIPWY-6608guanine and guanosine salvage IPWY-6620guanine and guanosine salvage IIIPWY-6618adenosylcobalamin salvage from cobinamide ICOBALSYN-PWY-1Specdb::CMs2237Specdb::CMs14103Specdb::CMs31322Specdb::CMs32072Specdb::CMs38054Specdb::CMs173909Specdb::NmrOneD1696Specdb::NmrOneD9242Specdb::NmrOneD9243Specdb::NmrOneD9244Specdb::NmrOneD9245Specdb::NmrOneD9246Specdb::NmrOneD9247Specdb::NmrOneD9248Specdb::NmrOneD9249Specdb::NmrOneD9250Specdb::NmrOneD9251Specdb::NmrOneD9252Specdb::NmrOneD9253Specdb::NmrOneD9254Specdb::NmrOneD9255Specdb::NmrOneD9256Specdb::NmrOneD9257Specdb::NmrOneD9258Specdb::NmrOneD9259Specdb::NmrOneD9260Specdb::NmrOneD9261Specdb::MsMs1553Specdb::MsMs1554Specdb::MsMs1555Specdb::MsMs5249Specdb::MsMs5250Specdb::MsMs5251Specdb::MsMs5252Specdb::MsMs5253Specdb::MsMs179082Specdb::MsMs179083Specdb::MsMs179084Specdb::MsMs181407Specdb::MsMs181408Specdb::MsMs181409Specdb::MsMs439075Specdb::MsMs439194Specdb::MsMs448016Specdb::MsMs448017Specdb::MsMs448138Specdb::MsMs2253179Specdb::MsMs2255276Specdb::MsMs2255309Specdb::MsMs2257209Specdb::MsMs2257354Specdb::MsMs2259191Specdb::NmrTwoD1637HMDB0139768046545C0014417345GMPG25GMPKeseler, I. 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Kokai Tokkyo Koho (1979), 3 pp.http://hmdb.ca/system/metabolites/msds/000/001/259/original/HMDB01397.pdf?1358462926GMP synthase [glutamine-hydrolyzing]P04079GUAA_ECOLIguaAhttp://ecmdb.ca/proteins/P04079.xmlProtein ushAP07024USHA_ECOLIushAhttp://ecmdb.ca/proteins/P07024.xmlMultifunctional protein surEP0A840SURE_ECOLIsurEhttp://ecmdb.ca/proteins/P0A840.xml5'-nucleotidase yjjGP0A8Y1YJJG_ECOLIyjjGhttp://ecmdb.ca/proteins/P0A8Y1.xmlHypoxanthine phosphoribosyltransferaseP0A9M2HPRT_ECOLIhpthttp://ecmdb.ca/proteins/P0A9M2.xmlXanthine phosphoribosyltransferaseP0A9M5XGPT_ECOLIgpthttp://ecmdb.ca/proteins/P0A9M5.xmlClass B acid phosphataseP0AE22APHA_ECOLIaphAhttp://ecmdb.ca/proteins/P0AE22.xmlPhosphatase nudJP0AEI6NUDJ_ECOLInudJhttp://ecmdb.ca/proteins/P0AEI6.xmlInosine-guanosine kinaseP0AEW6INGK_ECOLIgskhttp://ecmdb.ca/proteins/P0AEW6.xmlProtein mazGP0AEY3MAZG_ECOLImazGhttp://ecmdb.ca/proteins/P0AEY3.xmlCobalamin synthaseP36561COBS_ECOLIcobShttp://ecmdb.ca/proteins/P36561.xmlNucleoside-triphosphatase rdgBP52061RDGB_ECOLIrdgBhttp://ecmdb.ca/proteins/P52061.xmlGuanylate kinaseP60546KGUA_ECOLIgmkhttp://ecmdb.ca/proteins/P60546.xmlGMP reductaseP60560GUAC_ECOLIguaChttp://ecmdb.ca/proteins/P60560.xmlAdenine phosphoribosyltransferaseP69503APT_ECOLIapthttp://ecmdb.ca/proteins/P69503.xmlOxygen sensor protein DosPP76129DOSP_ECOLIdosPhttp://ecmdb.ca/proteins/P76129.xml5'-nucleotidase yfbRP76491YFBR_ECOLIyfbRhttp://ecmdb.ca/proteins/P76491.xmlGDP-mannose pyrophosphatase nudKP37128NUDK_ECOLInudKhttp://ecmdb.ca/proteins/P37128.xmlMutator mutT proteinP08337MUTT_ECOLImutThttp://ecmdb.ca/proteins/P08337.xmlOuter membrane protein NP77747OMPN_ECOLIompNhttp://ecmdb.ca/proteins/P77747.xmlOuter membrane pore protein EP02932PHOE_ECOLIphoEhttp://ecmdb.ca/proteins/P02932.xmlOuter membrane protein FP02931OMPF_ECOLIompFhttp://ecmdb.ca/proteins/P02931.xmlOuter membrane protein CP06996OMPC_ECOLIompChttp://ecmdb.ca/proteins/P06996.xmlGuanosine triphosphate + Water > Guanosine monophosphate + Hydrogen ion + PyrophosphateR00426Guanine + Phosphoribosyl pyrophosphate > Guanosine monophosphate + PyrophosphateR01229GUANPRIBOSYLTRAN-RXNGuanosine monophosphate + Water > Guanosine + PhosphateGuanosine monophosphate + 2 Hydrogen ion + NADPH > Inosinic acid + NADP + AmmoniumAdenosine triphosphate + Guanosine > ADP + Guanosine monophosphate + Hydrogen ionR01228GUANOSINEKIN-RXNCyclic GMP + Water > Guanosine monophosphate + Hydrogen ionAdenosylcobinamide-GDP + N1-(alpha-D-ribosyl)-5,6-dimethyl-benzimidazole > Adenosylcobalamin + Guanosine monophosphate + Hydrogen ionR05223COBALAMINSYN-RXNGuanosine diphosphate mannose + Water > Guanosine monophosphate +2 Hydrogen ion + D-Mannose 1-phosphateRXN0-5108Adenosine triphosphate + L-Glutamine + Water + Xanthylic acid > Adenosine monophosphate + L-Glutamate + Guanosine monophosphate +2 Hydrogen ion + PyrophosphateR01231GMP-SYN-GLUT-RXNAdenosine triphosphate + Guanosine monophosphate <> ADP + Guanosine diphosphateR00332GUANYL-KIN-RXNGuanosine triphosphate + Water <> Guanosine monophosphate + PyrophosphateR00426Inosinic acid + Ammonia + NADP <> Guanosine monophosphate + NADPH + Hydrogen ionR01134Guanosine monophosphate + Water <> Guanosine + PhosphateR01227Adenosine triphosphate + Guanosine <> ADP + Guanosine monophosphateR01228Guanosine monophosphate + Pyrophosphate <> Guanine + Phosphoribosyl pyrophosphateR01229Adenosine triphosphate + Xanthylic acid + Ammonia <> Adenosine monophosphate + Pyrophosphate + Guanosine monophosphateR01230Adenosine triphosphate + Xanthylic acid + L-Glutamine + Water <> Adenosine monophosphate + Pyrophosphate + Guanosine monophosphate + L-GlutamateR01231Adenosylcobalamin + Guanosine monophosphate <> Adenosylcobinamide-GDP + N1-(alpha-D-ribosyl)-5,6-dimethyl-benzimidazoleR05223Guanosine diphosphate mannose + Water > Hydrogen ion + Guanosine monophosphate + D-Mannose 1-phosphateRXN0-5108Adenosylcobinamide-GDP + N1-(5-Phospho-a-D-ribosyl)-5,6-dimethylbenzimidazole > adenosylcobalamin 5'-phosphate + Guanosine monophosphate + Hydrogen ionCOBALAMIN5PSYN-RXNAdenosylcobinamide-GDP + N1-(alpha-D-ribosyl)-5,6-dimethyl-benzimidazole Hydrogen ion + Adenosylcobalamin + Guanosine monophosphateCOBALAMINSYN-RXNAmmonia + Inosinic acid + NADP < Hydrogen ion + Guanosine monophosphate + NADPHR01134GMP-REDUCT-RXNWater + L-Glutamine + Xanthylic acid + Adenosine triphosphate > Hydrogen ion + L-Glutamate + Guanosine monophosphate + Pyrophosphate + Adenosine monophosphateR01231GMP-SYN-GLUT-RXNAdenosine triphosphate + Xanthylic acid + Ammonia > Hydrogen ion + Adenosine monophosphate + Pyrophosphate + Guanosine monophosphateR01230GMP-SYN-NH3-RXNGuanosine diphosphate + Water > Hydrogen ion + Guanosine monophosphate + PhosphateGUANOSINE-DIPHOSPHATASE-RXNGMP-Lysine + Water > Guanosine monophosphate + N-alpha-acetyl lysine methyl esterRXN0-4121GDP-cobinamide + alpha-ribazole > Cob(I)alamin + Guanosine monophosphateAdenosine triphosphate + Xanthylic acid + L-Glutamine + Water > Adenosine monophosphate + Pyrophosphate + Guanosine monophosphate + L-GlutamateInosinic acid + Ammonia + NADP > Guanosine monophosphate + NADPHR01134GMP-REDUCT-RXNAdenosine triphosphate + Guanosine monophosphate > ADP + Guanosine diphosphateGuanosine diphosphate mannose + Water > Guanosine monophosphate + Alpha-D-mannose 1-phosphateAdenosylcobinamide-GDP + N1-(alpha-D-ribosyl)-5,6-dimethyl-benzimidazole + N1-(5-Phospho-a-D-ribosyl)-5,6-dimethylbenzimidazole <> Guanosine monophosphate + Adenosylcobalamin + Adenosylcobalamin 5'-phosphateR05223 Adenosine triphosphate + Xanthylic acid + L-Glutamine + Water + Ammonia <> Adenosine monophosphate + Pyrophosphate + Guanosine monophosphate + L-GlutamateR01231 Xanthylic acid + Adenosine triphosphate + L-Glutamine + Water > Adenosine monophosphate + Pyrophosphate + L-Glutamic acid +2 Hydrogen ion + Guanosine monophosphate + L-GlutamatePW_R003427Guanosine monophosphate + Adenosine triphosphate > Adenosine diphosphate + Guanosine diphosphate + ADPPW_R003428Guanine + Phosphoribosyl pyrophosphate > Pyrophosphate + Guanosine monophosphatePW_R006059Guanosine triphosphate + Water > Guanosine monophosphate + Hydrogen ion + PyrophosphateGuanine + Phosphoribosyl pyrophosphate > Guanosine monophosphate + PyrophosphateAdenosine triphosphate + L-Glutamine + Water + Xanthylic acid > Adenosine monophosphate + L-Glutamate + Guanosine monophosphate +2 Hydrogen ion + PyrophosphateGuanosine triphosphate + Water > Guanosine monophosphate + Hydrogen ion + PyrophosphateGuanine + Phosphoribosyl pyrophosphate > Guanosine monophosphate + PyrophosphateAdenosine triphosphate + L-Glutamine + Water + Xanthylic acid > Adenosine monophosphate + L-Glutamate + Guanosine monophosphate +2 Hydrogen ion + PyrophosphateGuanosine triphosphate + Water > Guanosine monophosphate + Hydrogen ion + 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 culture23.7uM0.037 oCK12 NCM3722Mid-Log Phase948000Bennett, 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/h70.2uM0.037 oCBW25113Stationary Phase, glucose limited2808000Ishii, 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