<?xml version="1.0" encoding="UTF-8"?>
<compound>
  <version>2.0</version>
  <creation_date>2012-05-31 14:04:30 -0600</creation_date>
  <update_date>2015-09-13 12:56:13 -0600</update_date>
  <accession>ECMDB04085</accession>
  <m2m_id>M2MDB000601</m2m_id>
  <name>Inosinic acid</name>
  <description>Inosinic acid is a purine nucleotide which has hypoxanthine as the base and one phosphate group esterified to the sugar moiety. It is formed by the deamination of AMP and when hydrolysed produces inosine. Inosinic acid is the ribonucleotide of hypoxanthine and is the first compound formed during the synthesis of purine. (Wikipedia)</description>
  <synonyms>
    <synonym>5'-IMP</synonym>
    <synonym>5'-Inosinate</synonym>
    <synonym>5'-Inosine monophosphate</synonym>
    <synonym>5'-Inosine monophosphoric acid</synonym>
    <synonym>5'-Inosinic acid</synonym>
    <synonym>IMP</synonym>
    <synonym>Inosinate</synonym>
    <synonym>Inosine 5'-monophosphate</synonym>
    <synonym>Inosine 5'-monophosphoric acid</synonym>
    <synonym>Inosine 5'-phosphate</synonym>
    <synonym>Inosine 5'-phosphoric acid</synonym>
    <synonym>Inosine Monophosphate</synonym>
    <synonym>Inosine monophosphoric acid</synonym>
    <synonym>Inosine-5'-monophosphate</synonym>
    <synonym>Inosine-5'-monophosphoric acid</synonym>
    <synonym>Inosine-5'-phosphate</synonym>
    <synonym>Inosine-5'-phosphoric acid</synonym>
    <synonym>Inosinic acid</synonym>
    <synonym>Ribosylhypoxanthine monophosphate</synonym>
    <synonym>Ribosylhypoxanthine monophosphoric acid</synonym>
  </synonyms>
  <chemical_formula>C10H13N4O8P</chemical_formula>
  <average_molecular_weight>348.206</average_molecular_weight>
  <monisotopic_moleculate_weight>348.047099924</monisotopic_moleculate_weight>
  <iupac_name>{[(2R,3S,4R,5R)-3,4-dihydroxy-5-(6-oxo-6,9-dihydro-1H-purin-9-yl)oxolan-2-yl]methoxy}phosphonic acid</iupac_name>
  <traditional_iupac>inosine-5'-monophosphate</traditional_iupac>
  <cas_registry_number>131-99-7</cas_registry_number>
  <smiles>O[C@@H]1[C@@H](COP(O)(O)=O)O[C@H]([C@@H]1O)N1C=NC2=C1N=CNC2=O</smiles>
  <inchi>InChI=1S/C10H13N4O8P/c15-6-4(1-21-23(18,19)20)22-10(7(6)16)14-3-13-5-8(14)11-2-12-9(5)17/h2-4,6-7,10,15-16H,1H2,(H,11,12,17)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1</inchi>
  <inchikey>GRSZFWQUAKGDAV-KQYNXXCUSA-N</inchikey>
  <state>Solid</state>
  <cellular_locations>
    <cellular_location>Cytosol</cellular_location>
    <cellular_location>Extra-organism</cellular_location>
    <cellular_location>Periplasm</cellular_location>
  </cellular_locations>
  <predicted_properties>
    <property>
      <kind>logp</kind>
      <value>-2.04</value>
      <source>ALOGPS</source>
    </property>
    <property>
      <kind>logs</kind>
      <value>-2.06</value>
      <source>ALOGPS</source>
    </property>
    <property>
      <kind>solubility</kind>
      <value>3.05e+00 g/l</value>
      <source>ALOGPS</source>
    </property>
  </predicted_properties>
  <experimental_properties>
  </experimental_properties>
  <property>
    <kind>logp</kind>
    <value>-2.9</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>pka_strongest_acidic</kind>
    <value>1.31</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>pka_strongest_basic</kind>
    <value>0.49</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>iupac</kind>
    <value>{[(2R,3S,4R,5R)-3,4-dihydroxy-5-(6-oxo-6,9-dihydro-1H-purin-9-yl)oxolan-2-yl]methoxy}phosphonic acid</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>average_mass</kind>
    <value>348.206</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>mono_mass</kind>
    <value>348.047099924</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>smiles</kind>
    <value>O[C@@H]1[C@@H](COP(O)(O)=O)O[C@H]([C@@H]1O)N1C=NC2=C1N=CNC2=O</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>formula</kind>
    <value>C10H13N4O8P</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>inchi</kind>
    <value>InChI=1S/C10H13N4O8P/c15-6-4(1-21-23(18,19)20)22-10(7(6)16)14-3-13-5-8(14)11-2-12-9(5)17/h2-4,6-7,10,15-16H,1H2,(H,11,12,17)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>inchikey</kind>
    <value>GRSZFWQUAKGDAV-KQYNXXCUSA-N</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>polar_surface_area</kind>
    <value>175.73</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>refractivity</kind>
    <value>72.2</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>polarizability</kind>
    <value>29.14</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>rotatable_bond_count</kind>
    <value>4</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>acceptor_count</kind>
    <value>9</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>donor_count</kind>
    <value>5</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>physiological_charge</kind>
    <value>-2</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>formal_charge</kind>
    <value>0</value>
    <source>ChemAxon</source>
  </property>
  <pathways>
    <pathway>
      <name>Alanine, aspartate and glutamate metabolism</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec00250</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>Purine metabolism</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec00230</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>Drug metabolism - other enzymes</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec00983</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>Metabolic pathways</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>eco01100</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>Aspartate metabolism</name>
      <description>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
</description>
      <pathwhiz_id>PW000787</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>purine nucleotides de novo biosynthesis</name>
      <description>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


</description>
      <pathwhiz_id>PW000910</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>purine nucleotides de novo biosynthesis 1435709748</name>
      <description/>
      <pathwhiz_id>PW000960</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>adenine and adenosine salvage I</name>
      <description>The salvage of adenine begins with adenine being transporter into the cytosol through a adeP hydrogen symporter. Once in the cytosol adenine is degraded by reacting with a ribose-1-phosphate through an adenosine phosphorylase resulting in the release of a phosphate and adenosine. Adenosine is then deaminated by reacting with water, a hydrogen ion and an adenosine deaminase resulting in the release of an ammonium and a inosine . Inosine then reacts with a phosphate through a inosine phosphorylase resulting in the release of a ribose 1-phosphate and a hypoxanthine. Hypoxanthine reacts with a PRPP through a hypoxanthine phosphoribosyltransferase resulting in the release of a pyrophosphate and a IMP molecule.</description>
      <pathwhiz_id>PW002069</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>adenine and adenosine salvage II</name>
      <description>The salvage of adenine begins with adenine being transporter into the cytosol through a adeP hydrogen symporter. Once in the cytosol adenine is degraded by reacting with a ribose-1-phosphate through an adenosine phosphorylase resulting in the release of a phosphate and adenosine. Adenosine is then deaminated by reacting with water, a hydrogen ion and an adenosine deaminase resulting in the release of an ammonium and a inosine . Inosine can then be phosphorylated through an ATP driven inosine kinase resulting in the release of an ADP, a hydrogen ion and a IMP</description>
      <pathwhiz_id>PW002071</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>purine nucleotides de novo biosynthesis 2</name>
      <description>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</description>
      <pathwhiz_id>PW002033</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>adenine and adenosine salvage III</name>
      <ecocyc_pathway_id>PWY-6609</ecocyc_pathway_id>
    </pathway>
    <pathway>
      <name>adenine and adenosine salvage V</name>
      <ecocyc_pathway_id>PWY-6611</ecocyc_pathway_id>
    </pathway>
    <pathway>
      <name>adenosine nucleotides &lt;i&gt;de novo&lt;/i&gt; biosynthesis</name>
      <ecocyc_pathway_id>PWY-6126</ecocyc_pathway_id>
    </pathway>
    <pathway>
      <name>guanosine nucleotides &lt;i&gt;de novo&lt;/i&gt; biosynthesis</name>
      <ecocyc_pathway_id>PWY-6125</ecocyc_pathway_id>
    </pathway>
    <pathway>
      <name>inosine-5'-phosphate biosynthesis I</name>
      <ecocyc_pathway_id>PWY-6123</ecocyc_pathway_id>
    </pathway>
  </pathways>
  <spectra>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>2210</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>12309</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>31049</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>32262</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>37338</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>153039</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1052745</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1052748</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1052750</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1052752</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1052754</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1052755</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1052757</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1052760</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1052762</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1052763</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1052765</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1052767</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1052769</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1052770</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1052772</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1052774</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1052776</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1052778</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1052781</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>1142</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>4857</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>4858</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6012</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6013</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6014</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6015</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6016</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6017</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6018</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6019</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6020</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6021</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6022</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6023</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6024</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6025</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6026</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6027</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6028</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6029</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6030</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6031</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>277</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>278</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>279</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>3341</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>3342</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>178446</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>178447</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>178448</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>180765</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>180766</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>180767</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>439080</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>448024</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2235630</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2237725</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2239841</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2241882</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2243958</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2243989</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2244107</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2246001</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2246086</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2246181</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2246201</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2248069</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrTwoD</type>
      <spectrum_id>983</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrTwoD</type>
      <spectrum_id>1187</spectrum_id>
    </spectrum>
  </spectra>
  <hmdb_id>HMDB00175</hmdb_id>
  <pubchem_compound_id>8582</pubchem_compound_id>
  <chemspider_id>8264</chemspider_id>
  <kegg_id>C00130</kegg_id>
  <chebi_id>17202</chebi_id>
  <biocyc_id>IMP</biocyc_id>
  <het_id>IMP</het_id>
  <wikipidia>Inosinic acid</wikipidia>
  <foodb_id/>
  <general_references>
    <reference>
      <reference_text>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.</reference_text>
      <pubmed_id>21097882</pubmed_id>
    </reference>
    <reference>
      <reference_text>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.</reference_text>
      <pubmed_id>22080510</pubmed_id>
    </reference>
    <reference>
      <reference_text>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.</reference_text>
      <pubmed_id>17765195</pubmed_id>
    </reference>
    <reference>
      <reference_text>Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). "Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948.</reference_text>
      <pubmed_id>18331064</pubmed_id>
    </reference>
    <reference>
      <reference_text>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.</reference_text>
      <pubmed_id>19561621</pubmed_id>
    </reference>
    <reference>
      <reference_text>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.</reference_text>
      <pubmed_id>17379776</pubmed_id>
    </reference>
    <reference>
      <reference_text>Nakayama Y, Kinoshita A, Tomita M: Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition. Theor Biol Med Model. 2005 May 9;2(1):18.</reference_text>
      <pubmed_id>15882454</pubmed_id>
    </reference>
    <reference>
      <reference_text>Castro-Gago M, Cid E, Trabazo S, Pavon P, Camina F, Rodriguez-Segade S, Einis Punal J, Rodriguez-Nunez A: Cerebrospinal fluid purine metabolites and pyrimidine bases after brief febrile convulsions. Epilepsia. 1995 May;36(5):471-4.</reference_text>
      <pubmed_id>7614924</pubmed_id>
    </reference>
    <reference>
      <reference_text>Scott GS, Spitsin SV, Kean RB, Mikheeva T, Koprowski H, Hooper DC: Therapeutic intervention in experimental allergic encephalomyelitis by administration of uric acid precursors. Proc Natl Acad Sci U S A. 2002 Dec 10;99(25):16303-8. Epub 2002 Nov 25.</reference_text>
      <pubmed_id>12451183</pubmed_id>
    </reference>
    <reference>
      <reference_text>McConell GK, Shinewell J, Stephens TJ, Stathis CG, Canny BJ, Snow RJ: Creatine supplementation reduces muscle inosine monophosphate during endurance exercise in humans. Med Sci Sports Exerc. 2005 Dec;37(12):2054-61.</reference_text>
      <pubmed_id>16331129</pubmed_id>
    </reference>
    <reference>
      <reference_text>Green HJ, Grant SM, Phillips SM, Enns DL, Tarnopolsky MA, Sutton JR: Reduced muscle lactate during prolonged exercise following induced plasma volume expansion. Can J Physiol Pharmacol. 1997 Dec;75(12):1280-6.</reference_text>
      <pubmed_id>9534937</pubmed_id>
    </reference>
    <reference>
      <reference_text>Rodriguez-Nunez A, Cid E, Rodriguez-Garcia J, Camina F, Rodriguez-Segade S, Castro-Gago M: Concentrations of nucleotides, nucleosides, purine bases, oxypurines, uric acid, and neuron-specific enolase in the cerebrospinal fluid of children with sepsis. J Child Neurol. 2001 Sep;16(9):704-6.</reference_text>
      <pubmed_id>11575617</pubmed_id>
    </reference>
    <reference>
      <reference_text>Pouw EM, Schols AM, van der Vusse GJ, Wouters EF: Elevated inosine monophosphate levels in resting muscle of patients with stable chronic obstructive pulmonary disease. Am J Respir Crit Care Med. 1998 Feb;157(2):453-7.</reference_text>
      <pubmed_id>9476857</pubmed_id>
    </reference>
    <reference>
      <reference_text>Allison AC, Eugui EM: Purine metabolism and immunosuppressive effects of mycophenolate mofetil (MMF). Clin Transplant. 1996 Feb;10(1 Pt 2):77-84.</reference_text>
      <pubmed_id>8680053</pubmed_id>
    </reference>
    <reference>
      <reference_text>van Hall G, van der Vusse GJ, Soderlund K, Wagenmakers AJ: Deamination of amino acids as a source for ammonia production in human skeletal muscle during prolonged exercise. J Physiol. 1995 Nov 15;489 ( Pt 1):251-61.</reference_text>
      <pubmed_id>8583409</pubmed_id>
    </reference>
    <reference>
      <reference_text>McConell G, Snow RJ, Proietto J, Hargreaves M: Muscle metabolism during prolonged exercise in humans: influence of carbohydrate availability. J Appl Physiol. 1999 Sep;87(3):1083-6.</reference_text>
      <pubmed_id>10484580</pubmed_id>
    </reference>
    <reference>
      <reference_text>Klupp J, Pfitzmann R, Langrehr JM, Neuhaus P: Indications of mycophenolate mofetil in liver transplantation.  Transplantation. 2005 Sep 27;80(1 Suppl):S142-6.</reference_text>
      <pubmed_id>16286893</pubmed_id>
    </reference>
    <reference>
      <reference_text>Bangsbo J, Gollnick PD, Graham TE, Juel C, Kiens B, Mizuno M, Saltin B: Anaerobic energy production and O2 deficit-debt relationship during exhaustive exercise in humans. J Physiol. 1990 Mar;422:539-59.</reference_text>
      <pubmed_id>2352192</pubmed_id>
    </reference>
    <reference>
      <reference_text>McCauley TG, Hamaguchi N, Stanton M: Aptamer-based biosensor arrays for detection and quantification of biological macromolecules. Anal Biochem. 2003 Aug 15;319(2):244-50.</reference_text>
      <pubmed_id>12871718</pubmed_id>
    </reference>
    <reference>
      <reference_text>Rush JW, MacLean DA, Hultman E, Graham TE: Exercise causes branched-chain oxoacid dehydrogenase dephosphorylation but not AMP deaminase binding. J Appl Physiol. 1995 Jun;78(6):2193-200.</reference_text>
      <pubmed_id>7665417</pubmed_id>
    </reference>
    <reference>
      <reference_text>McConell GK, Canny BJ, Daddo MC, Nance MJ, Snow RJ: Effect of carbohydrate ingestion on glucose kinetics and muscle metabolism during intense endurance exercise. J Appl Physiol. 2000 Nov;89(5):1690-8.</reference_text>
      <pubmed_id>11053315</pubmed_id>
    </reference>
    <reference>
      <reference_text>Swart PJ, Beljaars E, Smit C, Pasma A, Schuitemaker H, Meijer DK: Comparative pharmacokinetic, immunologic and hematologic studies on the anti-HIV-1/2 compounds aconitylated and succinylated HSA. J Drug Target. 1996;4(2):109-16.</reference_text>
      <pubmed_id>8894971</pubmed_id>
    </reference>
  </general_references>
  <synthesis_reference>Park, Yeong Hun; Cho, Gwang Myeong; Baek, Min Ji; Hong, Guk Gi; Lee, Jin Nam.  Method for preparing 5'-inosinic acid by using microbe capable of over-expressing purC gene.  Repub. Korea  (2007),  7pp. </synthesis_reference>
  <msds_url>http://hmdb.ca/system/metabolites/msds/000/000/124/original/HMDB00175.pdf?1358461512</msds_url>
  <enzymes>
    <enzyme>
      <name>Protein ushA</name>
      <uniprot_id>P07024</uniprot_id>
      <uniprot_name>USHA_ECOLI</uniprot_name>
      <gene_name>ushA</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P07024.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Adenylosuccinate synthetase</name>
      <uniprot_id>P0A7D4</uniprot_id>
      <uniprot_name>PURA_ECOLI</uniprot_name>
      <gene_name>purA</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0A7D4.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Multifunctional protein surE</name>
      <uniprot_id>P0A840</uniprot_id>
      <uniprot_name>SURE_ECOLI</uniprot_name>
      <gene_name>surE</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0A840.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>5'-nucleotidase yjjG</name>
      <uniprot_id>P0A8Y1</uniprot_id>
      <uniprot_name>YJJG_ECOLI</uniprot_name>
      <gene_name>yjjG</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0A8Y1.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Hypoxanthine phosphoribosyltransferase</name>
      <uniprot_id>P0A9M2</uniprot_id>
      <uniprot_name>HPRT_ECOLI</uniprot_name>
      <gene_name>hpt</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0A9M2.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Xanthine phosphoribosyltransferase</name>
      <uniprot_id>P0A9M5</uniprot_id>
      <uniprot_name>XGPT_ECOLI</uniprot_name>
      <gene_name>gpt</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0A9M5.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Inosine-5'-monophosphate dehydrogenase</name>
      <uniprot_id>P0ADG7</uniprot_id>
      <uniprot_name>IMDH_ECOLI</uniprot_name>
      <gene_name>guaB</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0ADG7.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Class B acid phosphatase</name>
      <uniprot_id>P0AE22</uniprot_id>
      <uniprot_name>APHA_ECOLI</uniprot_name>
      <gene_name>aphA</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AE22.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Inosine-guanosine kinase</name>
      <uniprot_id>P0AEW6</uniprot_id>
      <uniprot_name>INGK_ECOLI</uniprot_name>
      <gene_name>gsk</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AEW6.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Protein mazG</name>
      <uniprot_id>P0AEY3</uniprot_id>
      <uniprot_name>MAZG_ECOLI</uniprot_name>
      <gene_name>mazG</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AEY3.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Bifunctional purine biosynthesis protein purH</name>
      <uniprot_id>P15639</uniprot_id>
      <uniprot_name>PUR9_ECOLI</uniprot_name>
      <gene_name>purH</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P15639.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Nucleoside-triphosphatase rdgB</name>
      <uniprot_id>P52061</uniprot_id>
      <uniprot_name>RDGB_ECOLI</uniprot_name>
      <gene_name>rdgB</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P52061.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>GMP reductase</name>
      <uniprot_id>P60560</uniprot_id>
      <uniprot_name>GUAC_ECOLI</uniprot_name>
      <gene_name>guaC</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P60560.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>5'-nucleotidase yfbR</name>
      <uniprot_id>P76491</uniprot_id>
      <uniprot_name>YFBR_ECOLI</uniprot_name>
      <gene_name>yfbR</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P76491.xml</protein_url>
    </enzyme>
  </enzymes>
  <transporters>
    <enzyme>
      <name>Outer membrane protein N</name>
      <uniprot_id>P77747</uniprot_id>
      <uniprot_name>OMPN_ECOLI</uniprot_name>
      <gene_name>ompN</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P77747.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Outer membrane pore protein E</name>
      <uniprot_id>P02932</uniprot_id>
      <uniprot_name>PHOE_ECOLI</uniprot_name>
      <gene_name>phoE</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P02932.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Outer membrane protein F</name>
      <uniprot_id>P02931</uniprot_id>
      <uniprot_name>OMPF_ECOLI</uniprot_name>
      <gene_name>ompF</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P02931.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Outer membrane protein C</name>
      <uniprot_id>P06996</uniprot_id>
      <uniprot_name>OMPC_ECOLI</uniprot_name>
      <gene_name>ompC</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P06996.xml</protein_url>
    </enzyme>
  </transporters>
  <reactions>
    <reaction_text>Hypoxanthine + Phosphoribosyl pyrophosphate &lt;&gt; Inosinic acid + Pyrophosphate</reaction_text>
    <kegg_reaction_id>R01132</kegg_reaction_id>
    <ecocyc_id>HYPOXANPRIBOSYLTRAN-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Water + Inosinic acid &gt; Inosine + Phosphate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Guanosine monophosphate + 2 Hydrogen ion + NADPH &gt; Inosinic acid + NADP + Ammonium</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + Inosine &lt;&gt; ADP + Hydrogen ion + Inosinic acid</reaction_text>
    <kegg_reaction_id>R01131</kegg_reaction_id>
    <ecocyc_id>INOSINEKIN-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Water + Inosinic acid + NAD &lt;&gt; Hydrogen ion + NADH + Xanthylic acid</reaction_text>
    <kegg_reaction_id>R01130</kegg_reaction_id>
    <ecocyc_id>IMP-DEHYDROG-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Water + Inosine triphosphate &gt; Hydrogen ion + Inosinic acid + Pyrophosphate</reaction_text>
    <kegg_reaction_id>R00720</kegg_reaction_id>
    <ecocyc_id>RXN0-6382</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Water + Inosinic acid &lt;&gt; Phosphoribosyl formamidocarboxamide</reaction_text>
    <kegg_reaction_id>R01127</kegg_reaction_id>
    <ecocyc_id>IMPCYCLOHYDROLASE-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>L-Aspartic acid + Guanosine triphosphate + Inosinic acid &lt;&gt; Adenylsuccinic acid + Guanosine diphosphate +2 Hydrogen ion + Phosphate</reaction_text>
    <kegg_reaction_id>R01135</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Inosine triphosphate + Water &lt;&gt; Inosinic acid + Pyrophosphate</reaction_text>
    <kegg_reaction_id>R00720</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Inosinic acid + Water &lt;&gt; Inosine + Phosphate</reaction_text>
    <kegg_reaction_id>R01126</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + Inosine &lt;&gt; ADP + Inosinic acid</reaction_text>
    <kegg_reaction_id>R01131</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Inosinic acid + Pyrophosphate &lt;&gt; Hypoxanthine + Phosphoribosyl pyrophosphate</reaction_text>
    <kegg_reaction_id>R01132</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Inosinic acid + Ammonia + NADP &lt;&gt; Guanosine monophosphate + NADPH + Hydrogen ion</reaction_text>
    <kegg_reaction_id>R01134</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Guanosine triphosphate + Inosinic acid + L-Aspartic acid &lt;&gt; Guanosine diphosphate + Phosphate + Adenylsuccinic acid</reaction_text>
    <kegg_reaction_id>R01135</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>L-Aspartic acid + Inosinic acid + Guanosine triphosphate &gt; Hydrogen ion + adenylo-succinate + Phosphate + Guanosine diphosphate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>ADENYLOSUCCINATE-SYNTHASE-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Ammonia + Inosinic acid + NADP &lt; Hydrogen ion + Guanosine monophosphate + NADPH</reaction_text>
    <kegg_reaction_id>R01134</kegg_reaction_id>
    <ecocyc_id>GMP-REDUCT-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Pyrophosphate + Inosinic acid &lt; Phosphoribosyl pyrophosphate + Hypoxanthine</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>HYPOXANPRIBOSYLTRAN-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Water + NAD + Inosinic acid &gt; Hydrogen ion + NADH + Xanthylic acid</reaction_text>
    <kegg_reaction_id>R01130</kegg_reaction_id>
    <ecocyc_id>IMP-DEHYDROG-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Inosine + Adenosine triphosphate &gt; Hydrogen ion + Inosinic acid + ADP</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>INOSINEKIN-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Inosinic acid + Ammonia + NADP &gt; Guanosine monophosphate + NADPH</reaction_text>
    <kegg_reaction_id>R01134</kegg_reaction_id>
    <ecocyc_id>GMP-REDUCT-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Inosinic acid + Pyrophosphate &gt; Hypoxanthine + Phosphoribosyl pyrophosphate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Inosinic acid + NAD + Water &gt; Xanthylic acid + NADH</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + Inosine &gt; ADP + Inosinic acid</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Inosinic acid + Water &gt; Phosphoribosyl formamidocarboxamide</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Guanosine triphosphate + Inosinic acid + L-Aspartic acid &gt; Guanosine diphosphate + Inorganic phosphate + N(6)-(1,2-dicarboxyethyl)AMP</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Guanosine triphosphate + Inosinic acid + L-Aspartic acid + L-Aspartic acid &gt; Guanosine diphosphate + Phosphate + N(6)-(1,2-dicarboxyethyl)AMP</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id>PW_R002648</pw_reaction_id>
    <reaction_text>Inosinic acid + L-Aspartic acid + Guanosine triphosphate + L-Aspartic acid &gt; Guanosine diphosphate + Phosphate +2 Hydrogen ion + N(6)-(1,2-dicarboxyethyl)AMP + Adenylsuccinic acid</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id>PW_R003424</pw_reaction_id>
    <reaction_text>FAICAR &lt;&gt; Inosinic acid + Water</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id>PW_R003422</pw_reaction_id>
    <reaction_text>Hypoxanthine + Phosphoribosyl pyrophosphate &gt; Inosinic acid + Pyrophosphate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id>PW_R006052</pw_reaction_id>
    <reaction_text>Water + Inosinic acid + NAD &lt;&gt; Hydrogen ion + NADH + Xanthylic acid</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Water + Inosinic acid &lt;&gt; Phosphoribosyl formamidocarboxamide</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>L-Aspartic acid + Guanosine triphosphate + Inosinic acid &lt;&gt; Adenylsuccinic acid + Guanosine diphosphate +2 Hydrogen ion + Phosphate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Water + Inosinic acid + NAD &lt;&gt; Hydrogen ion + NADH + Xanthylic acid</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Water + Inosinic acid &lt;&gt; Phosphoribosyl formamidocarboxamide</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
  </reactions>
  <concentrations>
    <growth_media>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</growth_media>
    <growth_system>Bioreactor, pH controlled, O2 and CO2 controlled, dilution rate: 0.2/h</growth_system>
    <concentration>113.0</concentration>
    <concentration_units>uM</concentration_units>
    <internal/>
    <error>0.0</error>
    <temperature>37 oC</temperature>
    <strain>BW25113</strain>
    <growth_status>Stationary Phase, glucose limited</growth_status>
    <molecules>452000</molecules>
    <molecules_error>0</molecules_error>
    <reference>
      <reference_text>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.</reference_text>
      <pubmed_id>17379776</pubmed_id>
    </reference>
    <growth_media>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</growth_media>
    <growth_system>Shake flask and filter culture</growth_system>
    <concentration>272.0</concentration>
    <concentration_units>uM</concentration_units>
    <internal/>
    <error>0.0</error>
    <temperature>37 oC</temperature>
    <strain>K12 NCM3722</strain>
    <growth_status>Mid-Log Phase</growth_status>
    <molecules>1088000</molecules>
    <molecules_error>0</molecules_error>
    <reference>
      <reference_text>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.</reference_text>
      <pubmed_id>19561621</pubmed_id>
    </reference>
  </concentrations>
</compound>
