2.0 2012-05-31 13:48:52 -0600 2015-09-13 12:56:10 -0600 ECMDB01273 M2MDB000319 Guanosine triphosphate Guanosine triphosphate (GTP) is a guanine nucleotide containing three phosphate groups esterified to the sugar moiety. GTP functions as a carrier of phosphates and pyrophosphates involved in channeling chemical energy into specific biosynthetic pathways. GTP activates the signal transducing G proteins which are involved in various cellular processes including proliferation, differentiation, and activation of several intracellular kinase cascades. Proliferation and apoptosis are regulated in part by the hydrolysis of GTP by small GTPases Ras and Rho. Another type of small GTPase, Rab, plays a role in the docking and fusion of vesicles and may also be involved in vesicle formation. In addition to its role in signal transduction, GTP also serves as an energy-rich precursor of mononucleotide units in the enzymatic biosynthesis of DNA and RNA. 5'-GTP GTG GTP Guanosine 5'-(tetrahydrogen triphosphate) Guanosine 5'-(tetrahydrogen triphosphoric acid) Guanosine 5'-triphosphate Guanosine 5'-triphosphorate Guanosine 5'-triphosphoric acid Guanosine mono(tetrahydrogen triphosphate) (ester) Guanosine mono(tetrahydrogen triphosphoric acid) (ester) Guanosine Triphosphate Guanosine triphosphoric acid Guanosine-triphosphate Guanosine-triphosphoric acid Guanylyl imidodiphosphate Guanylyl imidodiphosphoric acid H4gtp C10H16N5O14P3 523.1804 522.990659781 ({[({[(2R,3S,4R,5R)-5-(2-amino-6-oxo-6,9-dihydro-1H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy](hydroxy)phosphoryl}oxy)phosphonic acid triphosphate, guanosine 86-01-1 NC1=NC2=C(N=CN2[C@@H]2O[C@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]2O)C(=O)N1 InChI=1S/C10H16N5O14P3/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(27-9)1-26-31(22,23)29-32(24,25)28-30(19,20)21/h2-3,5-6,9,16-17H,1H2,(H,22,23)(H,24,25)(H2,19,20,21)(H3,11,13,14,18)/t3-,5-,6-,9-/m1/s1 XKMLYUALXHKNFT-UUOKFMHZSA-N Solid Cytosol Extra-organism Periplasm logp -0.63 ALOGPS logs -1.70 ALOGPS solubility 1.04e+01 g/l ALOGPS logp -3.7 ChemAxon pka_strongest_acidic 0.9 ChemAxon pka_strongest_basic -1.9 ChemAxon iupac ({[({[(2R,3S,4R,5R)-5-(2-amino-6-oxo-6,9-dihydro-1H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy](hydroxy)phosphoryl}oxy)phosphonic acid ChemAxon average_mass 523.1804 ChemAxon mono_mass 522.990659781 ChemAxon smiles NC1=NC2=C(N=CN2[C@@H]2O[C@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]2O)C(=O)N1 ChemAxon formula C10H16N5O14P3 ChemAxon inchi InChI=1S/C10H16N5O14P3/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(27-9)1-26-31(22,23)29-32(24,25)28-30(19,20)21/h2-3,5-6,9,16-17H,1H2,(H,22,23)(H,24,25)(H2,19,20,21)(H3,11,13,14,18)/t3-,5-,6-,9-/m1/s1 ChemAxon inchikey XKMLYUALXHKNFT-UUOKFMHZSA-N ChemAxon polar_surface_area 294.81 ChemAxon refractivity 97.24 ChemAxon polarizability 39.81 ChemAxon rotatable_bond_count 8 ChemAxon acceptor_count 14 ChemAxon donor_count 8 ChemAxon physiological_charge -3 ChemAxon formal_charge 0 ChemAxon Alanine, aspartate and glutamate metabolism ec00250 Purine metabolism ec00230 Pyrimidine metabolism The metabolism of pyrimidines begins with L-glutamine interacting with water molecule and a hydrogen carbonate through an ATP driven carbamoyl phosphate synthetase resulting in a hydrogen ion, an ADP, a phosphate, an L-glutamic acid and a carbamoyl phosphate. The latter compound interacts with an L-aspartic acid through a aspartate transcarbamylase resulting in a phosphate, a hydrogen ion and a N-carbamoyl-L-aspartate. The latter compound interacts with a hydrogen ion through a dihydroorotase resulting in the release of a water molecule and a 4,5-dihydroorotic acid. This compound interacts with an ubiquinone-1 through a dihydroorotate dehydrogenase, type 2 resulting in a release of an ubiquinol-1 and an orotic acid. The orotic acid then interacts with a phosphoribosyl pyrophosphate through a orotate phosphoribosyltransferase resulting in a pyrophosphate and an orotidylic acid. The latter compound then interacts with a hydrogen ion through an orotidine-5 '-phosphate decarboxylase, resulting in an release of carbon dioxide and an Uridine 5' monophosphate. The Uridine 5' monophosphate process to get phosphorylated by an ATP driven UMP kinase resulting in the release of an ADP and an Uridine 5--diphosphate. Uridine 5-diphosphate can be metabolized in multiple ways in order to produce a Deoxyuridine triphosphate. 1.-Uridine 5-diphosphate interacts with a reduced thioredoxin through a ribonucleoside diphosphate reductase 1 resulting in the release of a water molecule and an oxidized thioredoxin and an dUDP. The dUDP is then phosphorylated by an ATP through a nucleoside diphosphate kinase resulting in the release of an ADP and a DeoxyUridine triphosphate. 2.-Uridine 5-diphosphate interacts with a reduced NrdH glutaredoxin-like protein through a Ribonucleoside-diphosphate reductase 1 resulting in a release of a water molecule, an oxidized NrdH glutaredoxin-like protein and a dUDP. The dUDP is then phosphorylated by an ATP through a nucleoside diphosphate kinase resulting in the release of an ADP and a DeoxyUridine triphosphate. 3.-Uridine 5-diphosphate is phosphorylated by an ATP-driven nucleoside diphosphate kinase resulting in an ADP and an Uridinetriphosphate. The latter compound interacts with a reduced flavodoxin through ribonucleoside-triphosphate reductase resulting in the release of an oxidized flavodoxin, a water molecule and a Deoxyuridine triphosphate 4.-Uridine 5-diphosphate is phosphorylated by an ATP-driven nucleoside diphosphate kinase resulting in an ADP and an Uridinetriphosphate The uridine triphosphate interacts with a L-glutamine and a water molecule through an ATP driven CTP synthase resulting in an ADP, a phosphate, a hydrogen ion, an L-glutamic acid and a cytidine triphosphate. The cytidine triphosphate interacts with a reduced flavodoxin through a ribonucleoside-triphosphate reductase resulting in the release of a water molecule, an oxidized flavodoxin and a dCTP. The dCTP interacts with a water molecule and a hydrogen ion through a dCTP deaminase resulting in a release of an ammonium molecule and a Deoxyuridine triphosphate. 5.-Uridine 5-diphosphate is phosphorylated by an ATP-driven nucleoside diphosphate kinase resulting in an ADP and an Uridinetriphosphate The uridine triphosphate interacts with a L-glutamine and a water molecule through an ATP driven CTP synthase resulting in an ADP, a phosphate, a hydrogen ion, an L-glutamic acid and a cytidine triphosphate. The cytidine triphosphate then interacts spontaneously with a water molecule resulting in the release of a phosphate, a hydrogen ion and a CDP. The CDP then interacts with a reduced NrdH glutaredoxin-like protein through a ribonucleoside-diphosphate reductase 2 resulting in the release of a water molecule, an oxidized NrdH glutaredoxin-like protein and a dCDP. The dCDP is then phosphorylated through an ATP driven nucleoside diphosphate kinase resulting in an ADP and a dCTP. The dCTP interacts with a water molecule and a hydrogen ion through a dCTP deaminase resulting in a release of an ammonium molecule and a Deoxyuridine triphosphate. 6.-Uridine 5-diphosphate is phosphorylated by an ATP-driven nucleoside diphosphate kinase resulting in an ADP and an Uridinetriphosphate The uridine triphosphate interacts with a L-glutamine and a water molecule through an ATP driven CTP synthase resulting in an ADP, a phosphate, a hydrogen ion, an L-glutamic acid and a cytidine triphosphate. The cytidine triphosphate then interacts spontaneously with a water molecule resulting in the release of a phosphate, a hydrogen ion and a CDP. The CDP interacts with a reduced thioredoxin through a ribonucleoside diphosphate reductase 1 resulting in a release of a water molecule, an oxidized thioredoxin and a dCDP. The dCDP is then phosphorylated through an ATP driven nucleoside diphosphate kinase resulting in an ADP and a dCTP. The dCTP interacts with a water molecule and a hydrogen ion through a dCTP deaminase resulting in a release of an ammonium molecule and a Deoxyuridine triphosphate. The deoxyuridine triphosphate then interacts with a water molecule through a nucleoside triphosphate pyrophosphohydrolase resulting in a release of a hydrogen ion, a phosphate and a dUMP. The dUMP then interacts with a methenyltetrahydrofolate through a thymidylate synthase resulting in a dihydrofolic acid and a 5-thymidylic acid. Then 5-thymidylic acid is then phosphorylated through a nucleoside diphosphate kinase resulting in the release of an ADP and thymidine 5'-triphosphate. PW000942 ec00240 Metabolic Folate biosynthesis The biosynthesis of folic acid begins with a product of purine nucleotides de novo biosynthesis pathway, GTP. This compound is involved in a reaction with water through a GTP cyclohydrolase 1 protein complex, resulting in a hydrogen ion, formic acid and 7,8-dihydroneopterin 3-triphosphate. The latter compound is dephosphatased through a dihydroneopterin triphosphate pyrophosphohydrolase resulting in the release of a pyrophosphate, hydrogen ion and 7,8-dihydroneopterin 3-phosphate. The latter compound reacts with water spontaneously resulting in the release of a phosphate and a 7,8 -dihydroneopterin. This compound reacts with a dihydroneopterin aldolase, releasing a glycoaldehyde and 6-hydroxymethyl-7,9-dihydropterin. The latter compound is phosphorylated with a ATP-driven 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase resulting in a (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate. Chorismate is metabolized by reacting with L-glutamine through a 4-amino-4-deoxychorismate synthase resulting in L-glutamic acid and 4-amino-4-deoxychorismate. The latter compound then reacts through an aminodeoxychorismate lyase resulting in pyruvic acid,hydrogen ion and p-aminobenzoic acid. (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate and p-aminobenzoic acid react through a dihydropteroate synthase resulting in pyrophosphate and 7,8-dihydropteroic acid. This compound reacts with L-glutamic acid through an ATP driven bifunctional folylpolyglutamate synthetase / dihydrofolate synthetase resulting in a 7,8-dihydrofolate monoglutamate. This compound is reduced through an NADPH mediated dihydrofolate reductase resulting in a tetrahydrofate. This product goes on to a one carbon pool by folate pathway. PW000908 ec00790 Metabolic Porphyrin and chlorophyll metabolism ec00860 Riboflavin metabolism ec00740 Sulfur relay system ec04122 Metabolic pathways eco01100 Amino sugar and nucleotide sugar metabolism II The synthesis of amino sugars and nucleotide sugars starts with the phosphorylation of N-Acetylmuramic acid (MurNac) through its transport from the periplasmic space to the cytoplasm. Once in the cytoplasm, MurNac and water undergo a reversible reaction through a N-acetylmuramic acid 6-phosphate etherase, producing a D-lactic acid and N-Acetyl-D-Glucosamine 6-phosphate. This latter compound can also be introduced into the cytoplasm through a phosphorylating PTS permase in the inner membrane that allows for the transport of N-Acetyl-D-glucosamine from the periplasmic space. N-Acetyl-D-Glucosamine 6-phosphate can also be obtained from chitin dependent reactions. Chitin is hydrated through a bifunctional chitinase to produce chitobiose. This in turn gets hydrated by a beta-hexosaminidase to produce N-acetyl-D-glucosamine. The latter undergoes an atp dependent phosphorylation leading to the production of N-Acetyl-D-Glucosamine 6-phosphate. N-Acetyl-D-Glucosamine 6-phosphate is then be deacetylated in order to produce Glucosamine 6-phosphate through a N-acetylglucosamine-6-phosphate deacetylase. This compound is then deaminased into Beta-D-fructofuranose 6-phosphate through a glucosamine-6-phosphate deaminase. The beta-D-fructofuranose 6 -phosphate is isomerized in a reversible reaction into an alpha-D-mannose 6-phosphate. This compound can also be introduced into the cell from the periplasmic space through a mannose PTS permease that phosphorylates an alpha-D-mannose. Alpha-D-mannose 6-phosphate undergoes a reversible reaction through a phosphomannomutase to produce an alpha-D-mannose 1-phosphate. The alpha-D-mannose 1-phosphate enters the nucleotide sugar metabolism through a reaction with GTP producing a GDP-mannose and releasing a pyrophosphate, all through a mannose-1-phosphate guanylyltransferase. GDP-mannose is then dehydrated to produce GDP-4-dehydro-6-deoxy-alpha-D-mannose through a GDP-mannose 4,6-dehydratase. This compound is then used to synthesize GDP-Beta-L-fucose through a NADPH dependent GDP-L-fucose synthase. Alpha-D-glucose is introduced into the cytoplasm through a glucose PTS permease, which phosphorylates the compound in order to produce an alpha-D-glucose 6-phosphate. This compound is then modified through a phosphoglucomutase 1 to yield alpha-D-glucose 1-phosphate. This compound can either be adenylated to produce ADP-glucose or uridylylated to produce galactose 1-phosphate through glucose-1-phosphate adenyllyltransferase and galactose-1-phosphate uridylyltransferase respectively. PW000887 Metabolic 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 GTP degradation GTP, produced in the nucleotide de novo biosyntheis pathway, interacts with a water molecule through a GTP cyclohydrolase resulting in a formate, hydrogen ion and a 7,8-dihydroneopterin 3'-triphosphate. The latter compound interacts with a water molecule through a dihydroneopterin triphosphate pyrophosphohydrolase resulting in the release of a pyrophosphate, a hydrogen ion and a 7,8-dihydroneopterin 3'-phosphate. The latter compound interacts with water spontaneously resulting in the release of a phosphate and a 7,8 dihydroneopterin. The latter compound interacts with a dihydroneopterin aldolase resulting in the release of a glycolaldehyde and a 6-hydroxymethyl-7,8-dihydropterin. This compound then is then diphosphorylated by reacting with a ATP driven 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase resulting in the release of a hydrogen ion, an AMP and 6-hydroxymethyl-7,8-dihydropterin diphosphate. GTP interacts with a cyclic pyranopterin monophosphate synthase resulting in the release of a diphosphate and a cyclic pyranopterin phosphate. The latter compound interacts with a thiocarboxylated small subunit of molybdopterin synthase (a protein) and a water molecule through a molybdopterin synthase resulting in the release of 4 hydrogen ions, 2 small subunits of molybdopterin synthase and a molybdopterin. The molybdopterin interacts with an ATP and a hydrogen ion through a molybdopterin adenylyltransferase resulting in the release of a diphosphate and a molybdopterin adenine dinucleotide. PW001888 Metabolic Mannose Metabolism D-mannose can serve as a total source of carbon and energy for growth of E. coli. Alpha-D-mannose is introduced into the cytoplasm through a mannose PTS permease. Because mannose is taken up via a phosphotransferase system (PTS), the first intracellular species is D-mannose-6-phosphate. mannose-6-phosphate isomerase converts D-mannose-6-phosphate to D-fructose-6-phosphate, an intermediate of glycolysis, and hence it flows through the pathways of central metabolism to satisfy the cell's need for precursor metabolites, reducing power, and metabolic energy. The first two enzymes in the pathway (SEE VERTICAL SECTION) catalyze isomerizations that interconvert phosphorylated aldohexoses (β-D-glucose-6-phosphate, D-mannose-6-phosphate) and phosphorylated ketohexoses (D-fructose-6-phosphate). The reaction catalyzed by mannose-6-phosphate isomerase that produces D-mannose-6-phosphate is the first committed step in the biosynthesis of the activated mannose donor GDP-α-D-mannose. D-mannose-6-phosphate is then converted to GDP-D-mannose by the interaction of phosphomannomutase and mannose-1-phosphate guanylyltransferase . As for the bottom part L-fucose is biosynthesized as the sugar nucleotide GDP-L-fucose. Its biosynthesis from GDP-D-mannose begins with dehydration of this compound to GDP-4-dehydro-6-deoxy-D-mannose by the product of gene gmd. Then the bifunctional GDP-fucose synthase catalyzes the two-step (epimerase/reductase) synthesis of GDP-fucose from GDP-4-dehydro-6-deoxy-D-mannose via a GDP-4-dehydro-6-L-deoxygalactose intermediate. L-fucose is then incorporated into the colanic acid building blocks biosynthesis pathway. PW000822 Metabolic adenosylcobalamin salvage from cobinamide Cobinamide is incorporated from the extracellular space through a transport system into the cytosol. Once inside the cytosol, cobinamide interacts with ATP through a cobinamide adenosyl transferase resulting in the release of a triphosphate and an adenosylcobinamide. The latter compound is then phosphorylated through an ATP-dependent cobinamide kinase resulting in the release of ADP, a hydrogen ion and adenosyl-cobinamide phosphate. This last compound then interacts with GTP and a hydrogen ion through a cobinamide-P guanylyltransferase resulting in the release of a pyrophosphate and an adenosylcobinamide-GDP. A dimethylbenzimidazole interacts with a nicotinate D-ribonucleotide through a nicotinate-nucleotide dimethylbenzumidazole phosphoribosyltransferase resulting in the release of a nicotinate, a hydrogen ion and an alpha-ribazole 5' phosphate. The adenosylcobinamide-GDP and the alpha-ribazole 5' phosphate interact together through a cobalamin 5' phosphate synthase resulting in the release of a hydrogen ion, a GMP and Adenosylcobalamin 5'-phosphate. The latter compound then interacts with a water molecule through an adenosylcbalamin 5' phosphate phosphatase resulting in the release of a phosphate and a coenzyme B12. Likewise a cobalamin molecule can interact with ATP through a cobalamin adenosyltransferase resulting in the release of a triphosphate and a coenzyme B12 PW001884 Metabolic colanic acid building blocks biosynthesis The colonic acid building blocks biosynthesis starts with a Beta-D-Glucose undergoing a transport reaction mediated by a glucose PTS permease. The permease phosphorylates the Beta-D-Glucose, producing a Beta-D-Glucose 6-phosphate. This compound can either change to an Alpha-D-Glucose 6-phosphate spontaneously or into a fructose 6-phosphate through a glucose-6-phosphate isomerase. The latter compound can also be present in E.coli through the interaction of D-fructose and a mannose PTS permease which phosphorylate the D-fructose. Fructose 6-phosphate interacts in a reversible reaction with mannose-6-phosphate isomerase in order to produce a Alpha-D-mannose 6-phosphate. This compound can also be present in E.coli through the interaction of Alpha-D-mannose and a mannose PTS permease which phosphorylates the alpha-D-mannose. Alpha-D-mannose 6-phosphate interacts in a reversible reaction with a phosphomannomutase to produce a alpha-D-mannose 1-phosphate. This compound in turn with a hydrogen ion and gtp undergoes a reaction with a mannose-1-phosphate guanylyltransferase, releasing a pyrophosphate and producing a guanosine diphosphate mannose. Guanosine diphosphate mannose interacts with gdp-mannose 4,6-dehydratase releasing a water, and gdp-4-dehydro-6-deoxy-D-mannose. This compound in turn with hydrogen ion and NADPH interact with GDP-L-fucose synthase releasing NADP and producing a GDP-L-fucose. The Alpha-D-Glucose 6-phosphate interacts in a reversible reaction with phosphoglucomutase-1 to produce a alpha-D-glucose 1-phosphate. This in turn with UTP and hydrogen ion interact with UTP--glucose-1-phosphate uridyleltransferase releasing a pyrophosphate and UDP-glucose. UDP-glucose can either interact with galactose-1-phosphate uridylyltransferase to produce a UDP-galactose or in turn with NAD and water interact with UDP-glucose 6-dehydrogenase releasing a NADH and a hydrogen ion and producing a UDP-glucuronate. GDP-L-fucose, UDP-glucose, UDP-galactose and UDP-glucuronate are sugars that need to be activated in the form of nucleotide sugar prior to their assembly into colanic acid, also known as M antigen. Colanic acid is an extracellular polysaccharide which has been linked to a cluster of 19 genes(wca). PW000951 Metabolic preQ0 metabolism PreQ0 or 7-cyano-7-carbaguanine is biosynthesized by degrading GTP. GTP first interacts with water through a GTP cyclohydrolase resulting in the release of a formate, a hydrogen ion and a 7,8-dihydroneopterin 3'-triphosphate. The latter compound then interacts with water through a 6-carboxy-5,6,7,8-tetrahydropterin synthase resulting in a acetaldehyde, triphosphate, 2 hydrogen ion and 6-carboxy-5,6,7,8-tetrahydropterin. The latter compound then reacts spontaneously with a hydrogen ion resulting in the release of a ammonium molecule and a 7-carboxy-7-deazaguanine. This compound then interacts with ATP and ammonium through 7-cyano-7-deazaguanine synthase resulting in the release of water, phosphate, ADP, hydrogen ion and a 7-cyano-7-carbaguanine. The degradation of 7-cyano-7-deazaguanine can lead to produce a preQ1 or a queuine by reacting with 3 hydrogen ions and 2 NADPH through a 7-cyano-7-deazaguanine reductase. PreQ1 then interacts with a guanine 34 in tRNA through a tRNA-guanine transglycosylase resulting in a release of a guanine and a 7-aminomethyl-7-deazaguanosine 34 in tRNA. This nucleic acid then interacts with SAM through a S-adenosylmethionine tRNA ribosyltransferase-isomerase resulting in a release of a hydrogen ion, L-methionine, adenine and an epoxyqueuosine PW001893 Metabolic 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 Flavin biosynthesis The process of flavin biosynthesis starts with GTP being metabolized by interacting with 3 molecules of water through a GTP cyclohydrolase resulting in a release of formic acid, a pyrophosphate, two hydrog ions and 2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one or 2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine. Either of these compounds interacts with a water molecule and a hydrogen ion through a fused diaminohydroxyphosphoribosylaminopyrimidine deaminase / 5-amino-6-(5-phosphoribosylamino)uracil reductase resulting in an ammonium and 5-amino-6-(5-phospho-D-ribosylamino)uracil. This compound then interacts with a hydrogen ion through a NADPH dependent fused diaminohydroxyphosphoribosylaminopyrimidine deaminase / 5-amino-6-(5-phosphoribosylamino)uracil reductase resulting in the release of a NADP and a 5-amino-6-(5-phospho-D-ribitylamino)uracil. This compound then interacts with a water molecule through a 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase resulting in a release of a phosphate, and a 5-amino-6-(D-ribitylamino)uracil. D-ribulose 5-phosphate interacts with a3,4-dihydroxy-2-butanone 4-phosphate synthase resulting in the release of formic acid, a hydrogen ion and 1-deoxy-L-glycero-tetrulose 4-phosphate. A 5-amino-6-(D-ribitylamino)uracil and 1-deoxy-L-glycero-tetrulose 4-phosphate interact through a 6,7-dimethyl-8-ribityllumazine synthase resulting in the release of 2 water molecules, a phosphate, a hydrogen ion and a 6,7-dimethyl-8-(1-D-ribityl)lumazine. The latter compound then interacts with a hydrogen ion through a riboflavin synthase resulting in the release of a riboflavin and a 5-amino-6-(d-ribitylamino)uracil. The riboflavin is then phosphorylated through an ATP dependent riboflavin kinase resulting in the release of a ADP, a hydrogen ion and a FLAVIN MONONUCLEOTIDE. The flavin mononucleotide interad with a hydrogen ion and an ATP through the riboflavin kinase resulting in the release of a pyrophosphate and Flavin Adenine dinucleotide. This compound is then exported into the periplasm through a FMN/FAD exporter. PW001971 Metabolic guanylyl molybdenum cofactor biosynthesis The transition element molybdenum (Mo) has been long known as an essential micronutrient across the kingdoms of plants, animals, fungi and bacteria. However, molybdate itself is catalytically inactive and, with the exception of bacterial nitrogenase, needs to be activated through complexation by a special cofactor. There are several molybdenum cofactors, including molybdopterin (MPT), guanylyl molybdenum cofactor (MGD), cytidylyl molybdenum cofactor, or others [Rajagopalan92]. The chemical nature and biosynthesis of molybdenum cofactors have been investigated in detail in bacteria [Wuebbens95, Pitterle93, Pitterle93a, Rajagopalan92, SantamariaArauj04] and plants [Schwarz06]. All of the cofactors are synthesized from molybdopterin (MPT). The MPT structure is conserved in all organisms and it has been demonstrated that its biosynthesis is preserved in bacteria and plants alike. It is produced from GTP via cyclic pyranopterin phosphate (see molybdenum cofactor biosynthesis). The variability of the molybdenum cofactors found in bacteria is achieved by the attachment of GMP, AMP, IMP, or CMP to the phosphate group of MPT. In Escherichia coli, both guanylyl molybdenum cofactor and cytidylyl molybdenum cofactor are present. bis(molybdenum cofactor) synthase [multifunctional] catalyzes the transfer of the guanine nucleotide from GTP, releasing the β- and γ-phosphates of GTP as pyrophosphate and forming guanylyl molybdenum cofactor. (EcoCyc) PW002032 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 Tetrahydromonapterin Biosynthesis 5,6,7,8-tetrahydromonapterin is the major tetrahydropterin in E. coli, although the biological role of tetrahydromonapterin in E. coli is currently unknown. It was shown to be a cofactor for the phenylalanine hydroxylase PhhA of Pseudomonas aeruginosa, but no enzyme requiring tetrahydromonapterin as a cofactor has yet been discovered in E. coli. Production of tetrahydromonapterin far exceeds production of folate, indicating that the majority of 7,8-dihydroneopterin 3'-triphosphate, the product of the first committed step of the superpathway of tetrahydrofolate biosynthesis and salvage pathway, is diverted from folate biosynthesis to this pathway. High levels of monapterin are found in the growth medium. PW002043 Metabolic molybdenum cofactor biosynthesis PWY-6823 adenosine nucleotides <i>de novo</i> biosynthesis PWY-6126 ppGpp biosynthesis PPGPPMET-PWY 6-hydroxymethyl-dihydropterin diphosphate biosynthesis I PWY-6147 guanosine nucleotides <i>de novo</i> biosynthesis PWY-6125 salvage pathways of pyrimidine ribonucleotides PWY0-163 flavin biosynthesis I (bacteria and plants) RIBOSYN2-PWY preQ₀ biosynthesis PWY-6703 GDP-mannose biosynthesis PWY-5659 adenosylcobalamin salvage from cobinamide I COBALSYN-PWY-1 guanylyl molybdenum cofactor biosynthesis PWY-5964 Specdb::CMs 23794 Specdb::CMs 38006 Specdb::NmrOneD 1676 Specdb::NmrOneD 147110 Specdb::NmrOneD 147111 Specdb::NmrOneD 147112 Specdb::NmrOneD 147113 Specdb::NmrOneD 147114 Specdb::NmrOneD 147115 Specdb::NmrOneD 147116 Specdb::NmrOneD 147117 Specdb::NmrOneD 147118 Specdb::NmrOneD 147119 Specdb::NmrOneD 147120 Specdb::NmrOneD 147121 Specdb::NmrOneD 147122 Specdb::NmrOneD 147123 Specdb::NmrOneD 147124 Specdb::NmrOneD 147125 Specdb::NmrOneD 147126 Specdb::NmrOneD 147127 Specdb::NmrOneD 147128 Specdb::NmrOneD 147129 Specdb::NmrOneD 166624 Specdb::MsMs 1501 Specdb::MsMs 1502 Specdb::MsMs 1503 Specdb::MsMs 178131 Specdb::MsMs 178132 Specdb::MsMs 178133 Specdb::MsMs 180447 Specdb::MsMs 180448 Specdb::MsMs 180449 Specdb::MsMs 2252396 Specdb::MsMs 2254070 Specdb::MsMs 2254439 Specdb::MsMs 2256151 Specdb::MsMs 2256484 Specdb::MsMs 2258087 Specdb::MsMs 2771987 Specdb::MsMs 2771988 Specdb::MsMs 2771989 Specdb::MsMs 2910233 Specdb::MsMs 2910234 Specdb::MsMs 2910235 Specdb::NmrTwoD 1617 HMDB01273 6830 6569 C00044 15996 GTP GTP Guanosine 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). "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 Iwanaga N, Yamamasu S, Tachibana D, Nishio J, Nakai Y, Shintaku H, Ishiko O: Activity of synthetic enzymes of tetrahydrobiopterin in the human placenta. Int J Mol Med. 2004 Jan;13(1):117-20. 14654981 Naylor EW, Ennis D, Davidson AG, Wong LT, Applegarth DA, Niederwieser A: Guanosine triphosphate cyclohydrolase I deficiency: early diagnosis by routine urine pteridine screening. Pediatrics. 1987 Mar;79(3):374-8. 3822637 Lester HA, Steer ML, Levitzki A: Prostaglandin-stimulated GTP hydrolysis associated with activation of adenylate cyclase in human platelet membranes. Proc Natl Acad Sci U S A. 1982 Feb;79(3):719-23. 6121325 Reichert LE Jr, Dattatreyamurty B: The follicle-stimulating hormone (FSH) receptor in testis: interaction with FSH, mechanism of signal transduction, and properties of the purified receptor. Biol Reprod. 1989 Jan;40(1):13-26. 2493820 Schmidt VA, Scudder L, Devoe CE, Bernards A, Cupit LD, Bahou WF: IQGAP2 functions as a GTP-dependent effector protein in thrombin-induced platelet cytoskeletal reorganization. Blood. 2003 Apr 15;101(8):3021-8. Epub 2002 Dec 19. 12515716 Chen Q, He Y, Yang K: Gene therapy for Parkinson's disease: progress and challenges. Curr Gene Ther. 2005 Feb;5(1):71-80. 15638712 Stiller, Regine; Thiem, Joachim. Preparative enzymatic conversion of guanosine-5'-monophosphate to guanosine-5'-triphosphate. Synlett (1990), (11), 709-10. http://hmdb.ca/system/metabolites/msds/000/001/141/original/HMDB01273.pdf?1358462086 Adenylate cyclase P00936 CYAA_ECOLI cyaA http://ecmdb.ca/proteins/P00936.xml Periplasmic AppA protein P07102 PPA_ECOLI appA http://ecmdb.ca/proteins/P07102.xml GTP cyclohydrolase 1 P0A6T5 GCH1_ECOLI folE http://ecmdb.ca/proteins/P0A6T5.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 GTP cyclohydrolase-2 P0A7I7 RIBA_ECOLI ribA http://ecmdb.ca/proteins/P0A7I7.xml DNA-directed RNA polymerase subunit alpha P0A7Z4 RPOA_ECOLI rpoA http://ecmdb.ca/proteins/P0A7Z4.xml DNA-directed RNA polymerase subunit omega P0A800 RPOZ_ECOLI rpoZ http://ecmdb.ca/proteins/P0A800.xml Uridine kinase P0A8F4 URK_ECOLI udk http://ecmdb.ca/proteins/P0A8F4.xml DNA-directed RNA polymerase subunit beta' P0A8T7 RPOC_ECOLI rpoC http://ecmdb.ca/proteins/P0A8T7.xml DNA-directed RNA polymerase subunit beta P0A8V2 RPOB_ECOLI rpoB http://ecmdb.ca/proteins/P0A8V2.xml Anaerobic ribonucleoside-triphosphate reductase-activating protein P0A9N8 NRDG_ECOLI nrdG http://ecmdb.ca/proteins/P0A9N8.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 Protein mazG P0AEY3 MAZG_ECOLI mazG http://ecmdb.ca/proteins/P0AEY3.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 Deoxyguanosinetriphosphate triphosphohydrolase P15723 DGTP_ECOLI dgt http://ecmdb.ca/proteins/P15723.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 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 Putative ribosome biogenesis GTPase RsgA P39286 RSGA_ECOLI rsgA http://ecmdb.ca/proteins/P39286.xml Nucleoside-triphosphatase rdgB P52061 RDGB_ECOLI rdgB http://ecmdb.ca/proteins/P52061.xml Adenylate kinase P69441 KAD_ECOLI adk http://ecmdb.ca/proteins/P69441.xml Molybdopterin-guanine dinucleotide biosynthesis protein A P32173 MOBA_ECOLI mobA http://ecmdb.ca/proteins/P32173.xml Molybdopterin-guanine dinucleotide biosynthesis protein B P32125 MOBB_ECOLI mobB http://ecmdb.ca/proteins/P32125.xml Flavodoxin-2 P0ABY4 FLAW_ECOLI fldB http://ecmdb.ca/proteins/P0ABY4.xml Molybdenum cofactor biosynthesis protein A P30745 MOAA_ECOLI moaA http://ecmdb.ca/proteins/P30745.xml Flavodoxin-1 P61949 FLAV_ECOLI fldA http://ecmdb.ca/proteins/P61949.xml Molybdenum cofactor biosynthesis protein C P0A738 MOAC_ECOLI moaC http://ecmdb.ca/proteins/P0A738.xml Mutator mutT protein P08337 MUTT_ECOLI mutT http://ecmdb.ca/proteins/P08337.xml diguanylate cyclase; cold- and stationary phase-induced oxygen-dependent biofilm regulator; positively regulates csgBAC and pgaABCD P0AA89 dosC http://ecmdb.ca/proteins/P0AA89.xml diguanylate cyclase P76245 yeaP http://ecmdb.ca/proteins/P76245.xml Probable diguanylate cyclase AdrA P0AAP1 ADRA_ECOLI adrA http://ecmdb.ca/proteins/P0AAP1.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 2 Flavodoxin reduced + Guanosine triphosphate + 2 Hydrogen ion > dGTP +2 flavodoxin semi oxidized + Water Guanosine triphosphate + Water > Guanosine monophosphate + Hydrogen ion + Pyrophosphate R00426 Adenosine triphosphate + Guanosine diphosphate <> ADP + Guanosine triphosphate R00330 GDPKIN-RXN Guanosine triphosphate + Water <> Cyclic pyranopterin monophosphate + Pyrophosphate R09394 Adenosine triphosphate + Guanosine triphosphate + Water + Sulfate > Adenosine phosphosulfate + Guanosine diphosphate + Phosphate + Pyrophosphate bis-molybdenum cofactor + Guanosine triphosphate + Hydrogen ion > bis-molybdopterin mono-guanine dinucleotide + Pyrophosphate Guanosine triphosphate + Hydrogen ion + Molybdopterin > Molybdopterin guanine dinucleotide + Pyrophosphate bis-molybdopterin mono-guanine dinucleotide + Guanosine triphosphate + Hydrogen ion > Bis-molybdopterin guanine dinucleotide + Pyrophosphate tungsten bispterin cofactor + Guanosine triphosphate + Hydrogen ion > tungsten bispterin cofactor mono-guanine dinucleotide + Pyrophosphate tungsten bispterin cofactor mono-guanine dinucleotide + Guanosine triphosphate + Hydrogen ion > tungsten bispterin cofactor guanine dinucleotide + Pyrophosphate Guanosine triphosphate + Water > Guanosine + Triphosphate Adenosine monophosphate + Guanosine triphosphate <> ADP + Guanosine diphosphate Guanosine triphosphate + Water > Guanosine diphosphate + Hydrogen ion + Phosphate 3.6.5.1-RXN Guanosine triphosphate + 3 Water <> 2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + Formic acid +2 Hydrogen ion + Pyrophosphate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine R00425 GTP-CYCLOHYDRO-II-RXN Adenosyl cobinamide phosphate + Guanosine triphosphate + Hydrogen ion > Adenosylcobinamide-GDP + Pyrophosphate R05222 COBINPGUANYLYLTRANS-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 Guanosine triphosphate + Water > Dihydroneopterin triphosphate + Formic acid + Hydrogen ion GTP-CYCLOHYDRO-I-RXN Adenosine triphosphate + Guanosine triphosphate <> Adenosine monophosphate + Guanosine 3'-diphosphate 5'-triphosphate + Hydrogen ion R00429 GTPPYPHOSKIN-RXN Guanosine 3'-diphosphate 5'-triphosphate + Water > Guanosine triphosphate + Pyrophosphate RXN0-6427 L-Aspartic acid + Guanosine triphosphate + Inosinic acid <> Adenylsuccinic acid + Guanosine diphosphate +2 Hydrogen ion + Phosphate R01135 Guanosine triphosphate + Hydrogen ion + Water > Ammonium + Xanthosine 5-triphosphate Guanosine triphosphate + 3 Water <> Formic acid + 2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + Pyrophosphate R00425 Guanosine triphosphate + Water <> Guanosine monophosphate + Pyrophosphate R00426 Guanosine triphosphate + Water <> Formamidopyrimidine nucleoside triphosphate R00428 Adenosine triphosphate + Guanosine triphosphate <> Adenosine monophosphate + Guanosine 3'-diphosphate 5'-triphosphate R00429 Guanosine triphosphate + Pyruvic acid <> Guanosine diphosphate + Phosphoenolpyruvic acid R00430 Guanosine triphosphate <> Cyclic GMP + Pyrophosphate R00434 GUANYLCYC-RXN Guanosine triphosphate + RNA <> Pyrophosphate + RNA R00441 Guanosine triphosphate + Cytidine <> Guanosine diphosphate + Cytidine monophosphate R00517 Guanosine triphosphate + D-Mannose 1-phosphate <> Pyrophosphate + Guanosine diphosphate mannose R00885 2.7.7.13-RXN Guanosine triphosphate + Uridine <> Guanosine diphosphate + Uridine 5'-monophosphate R00968 Guanosine triphosphate + Inosinic acid + L-Aspartic acid <> Guanosine diphosphate + Phosphate + Adenylsuccinic acid R01135 dGTP + Thioredoxin disulfide + Water <> Guanosine triphosphate + Thioredoxin R02020 Adenosyl cobinamide phosphate + Guanosine triphosphate <> Adenosylcobinamide-GDP + Pyrophosphate R05222 Adenosyl cobinamide + Guanosine triphosphate <> Adenosyl cobinamide phosphate + Guanosine diphosphate R06558 2 Guanosine triphosphate <> 3',5'-Cyclic diGMP +2 Pyrophosphate + Cyclic di-3',5'-guanylate R08057 Guanosine triphosphate + hydroxyl radical > Hydrogen ion + 8-oxo-GTP RXN-11409 Hydrogen ion + D-Mannose 1-phosphate + Guanosine triphosphate > Guanosine diphosphate mannose + Pyrophosphate 2.7.7.13-RXN L-Aspartic acid + Inosinic acid + Guanosine triphosphate > Hydrogen ion + adenylo-succinate + Phosphate + Guanosine diphosphate ADENYLOSUCCINATE-SYNTHASE-RXN Guanosine diphosphate + Adenosine triphosphate > Guanosine triphosphate + ADP GDPKIN-RXN Water + Guanosine triphosphate > Hydrogen ion + Pyrophosphate + 2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + Formic acid GTP-CYCLOHYDRO-II-RXN Guanosine triphosphate + Adenosine triphosphate > Guanosine 3'-diphosphate 5'-triphosphate + Adenosine monophosphate GTPPYPHOSKIN-RXN Guanosine triphosphate > Cyclic pyranopterin monophosphate + Pyrophosphate RXN-8340 Hydrogen ion + molybdenum cofactor + Guanosine triphosphate <> Molybdopterin guanine dinucleotide + Pyrophosphate RXN0-262 Guanosine triphosphate > cyclic di-3',5'-guanylate + Pyrophosphate RXN0-5359 Guanosine 3'-diphosphate 5'-triphosphate + Water > Hydrogen ion + Guanosine triphosphate + Pyrophosphate RXN0-6427 2 Guanosine triphosphate >2 Pyrophosphate + Cyclic di-3',5'-guanylate Guanosine triphosphate + adenosylcobinamide phosphate > Pyrophosphate + Adenosylcobinamide-GDP Guanosine triphosphate + Water > Formic acid + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate Guanosine triphosphate + Water > Guanosine diphosphate + Inorganic phosphate Guanosine triphosphate + Alpha-D-mannose 1-phosphate > Pyrophosphate + Guanosine diphosphate mannose Guanosine triphosphate + Molybdopterin > Pyrophosphate + Guanylyl molybdenum cofactor Guanosine triphosphate + Inosinic acid + L-Aspartic acid > Guanosine diphosphate + Inorganic phosphate + N(6)-(1,2-dicarboxyethyl)AMP Guanosine triphosphate + 3 Water > Formic acid + 2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + Pyrophosphate Adenosine triphosphate + Guanosine triphosphate + Adenosyl cobinamide <> Adenosyl cobinamide phosphate + ADP + Guanosine diphosphate R05221 R06558 Guanosine triphosphate + Water <> Formic acid + Dihydroneopterin triphosphate R00424 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 D-Mannose 1-phosphate + Guanosine triphosphate + Hydrogen ion > Pyrophosphate + Guanosine diphosphate mannose PW_R002961 α-D-mannose 1-phosphate + Guanosine triphosphate + Hydrogen ion > Guanosine diphosphate mannose + Pyrophosphate PW_R003361 Guanosine triphosphate + Water > Formic acid + Hydrogen ion + 7,8-dihydroneopterin 3'-triphosphate PW_R003396 Guanosine diphosphate + Adenosine triphosphate > Adenosine diphosphate + Guanosine triphosphate + ADP PW_R003429 Guanosine triphosphate + a reduced flavodoxin > dGTP + an oxidized flavodoxin + Water PW_R003430 adenosylcobinamide phosphate + Guanosine triphosphate + Hydrogen ion > Pyrophosphate + Adenosylcobinamide-GDP + Adenosylcobinamide-GDP PW_R005141 Guanosine triphosphate > Cyclic pyranopterin monophosphate + Pyrophosphate PW_R005152 Guanosine triphosphate + 3 Water > Formic acid + Pyrophosphate +2 Hydrogen ion + 2,5-Diamino-6-(5'-phosphoribosylamino)-4-pyrimidineone PW_R005542 Guanosine triphosphate + Water > 2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + Hydrogen ion + Formic acid + Pyrophosphate PW_R005545 Bis-molybdopterin guanine dinucleotide + Guanosine triphosphate + Hydrogen ion + Molybdopterin guanine dinucleotide > Guanylyl molybdenum cofactor + Pyrophosphate PW_R005942 Guanosine triphosphate + Water > Guanosine monophosphate + Hydrogen ion + Pyrophosphate Adenosine triphosphate + Guanosine triphosphate <> Adenosine monophosphate + Guanosine 3'-diphosphate 5'-triphosphate + Hydrogen ion Adenosyl cobinamide phosphate + Guanosine triphosphate + Hydrogen ion > Adenosylcobinamide-GDP + Pyrophosphate dGTP + Thioredoxin disulfide + Water <> Guanosine triphosphate + Thioredoxin Guanosine triphosphate + D-Mannose 1-phosphate <> Pyrophosphate + Guanosine diphosphate mannose Guanosine triphosphate + Water <> Cyclic pyranopterin monophosphate + Pyrophosphate Guanosine triphosphate + 3 Water <>2 2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + Formic acid +2 Hydrogen ion + Pyrophosphate +2 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine L-Aspartic acid + Guanosine triphosphate + Inosinic acid <> Adenylsuccinic acid + Guanosine diphosphate +2 Hydrogen ion + Phosphate Guanosine triphosphate <> Cyclic GMP + Pyrophosphate Guanosine triphosphate + RNA <> Pyrophosphate Guanosine triphosphate + Water > Guanosine monophosphate + Hydrogen ion + Pyrophosphate Adenosine triphosphate + Guanosine triphosphate <> Adenosine monophosphate + Guanosine 3'-diphosphate 5'-triphosphate + Hydrogen ion Guanosine triphosphate + D-Mannose 1-phosphate <> Pyrophosphate + Guanosine diphosphate mannose Guanosine triphosphate + Water > Guanosine monophosphate + Hydrogen ion + Pyrophosphate 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 390.0 uM 24.0 37 oC K12 Stationary Phase, glucose limited 1560000 96000 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 4870.0 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 19480000 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 2690.0 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 10760000 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 1250.0 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 5000000 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 589.0 uM 0.0 37 oC BW25113 Stationary Phase, glucose limited 2356000 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