<?xml version="1.0" encoding="UTF-8"?>
<compound>
  <version>2.0</version>
  <creation_date>2012-05-31 14:06:15 -0600</creation_date>
  <update_date>2015-09-13 12:56:14 -0600</update_date>
  <accession>ECMDB04139</accession>
  <m2m_id>M2MDB000632</m2m_id>
  <name>Potassium</name>
  <description>Potassium is an essential electrolyte and part of many minerals. Potassium ion is a major intracellular cation in bacteria, plants and animals. It is necessary for the function of all living cells. There are a number of of potassium transport systems that regulate the intracellular potassium concentration.</description>
  <synonyms>
    <synonym>K+</synonym>
    <synonym>Kalium</synonym>
    <synonym>Potassium</synonym>
    <synonym>Potassium (ion)</synonym>
    <synonym>Potassium (K+)</synonym>
    <synonym>Potassium cation</synonym>
    <synonym>Potassium ion</synonym>
    <synonym>Potassium ion (K+)</synonym>
    <synonym>Potassium ion (K1+)</synonym>
    <synonym>Potassium ion(+)</synonym>
    <synonym>Potassium ion(1+)</synonym>
    <synonym>Potassium monocation</synonym>
    <synonym>Potassium(+)</synonym>
    <synonym>Potassium(1+)</synonym>
    <synonym>Potassium(1+) ion</synonym>
    <synonym>Potassium(I) cation</synonym>
  </synonyms>
  <chemical_formula>K</chemical_formula>
  <average_molecular_weight>39.0983</average_molecular_weight>
  <monisotopic_moleculate_weight>38.963706861</monisotopic_moleculate_weight>
  <iupac_name>potassium(1+) ion</iupac_name>
  <traditional_iupac>potassium(1+) ion</traditional_iupac>
  <cas_registry_number>7440-09-7</cas_registry_number>
  <smiles>[K+]</smiles>
  <inchi>InChI=1S/K/q+1</inchi>
  <inchikey>NPYPAHLBTDXSSS-UHFFFAOYSA-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>
  </predicted_properties>
  <experimental_properties>
    <property>
      <kind>melting_point</kind>
      <value>63.2 oC</value>
    </property>
  </experimental_properties>
  <property>
    <kind>logp</kind>
    <value>0.2</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>pka_strongest_acidic</kind>
    <value>3.09</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>iupac</kind>
    <value>potassium(1+) ion</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>average_mass</kind>
    <value>39.0983</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>mono_mass</kind>
    <value>38.963706861</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>smiles</kind>
    <value>[K+]</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>formula</kind>
    <value>K</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>inchi</kind>
    <value>InChI=1S/K/q+1</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>inchikey</kind>
    <value>NPYPAHLBTDXSSS-UHFFFAOYSA-N</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>polar_surface_area</kind>
    <value>0</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>refractivity</kind>
    <value>0</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>polarizability</kind>
    <value>1.78</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>rotatable_bond_count</kind>
    <value>0</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>acceptor_count</kind>
    <value>0</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>donor_count</kind>
    <value>0</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>physiological_charge</kind>
    <value>1</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>formal_charge</kind>
    <value>1</value>
    <source>ChemAxon</source>
  </property>
  <pathways>
    <pathway>
      <name>Pyrimidine metabolism</name>
      <description>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.</description>
      <pathwhiz_id>PW000942</pathwhiz_id>
      <kegg_map_id>ec00240</kegg_map_id>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>Folate biosynthesis</name>
      <description>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.
</description>
      <pathwhiz_id>PW000908</pathwhiz_id>
      <kegg_map_id>ec00790</kegg_map_id>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>Two-component system</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec02020</kegg_map_id>
      <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>Thiamin diphosphate biosynthesis</name>
      <description/>
      <pathwhiz_id>PW002028</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>
  </pathways>
  <spectra>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>25736</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>25737</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>25738</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>32294</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>32295</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>32296</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2400558</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2400559</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2400560</spectrum_id>
    </spectrum>
  </spectra>
  <hmdb_id>HMDB00586</hmdb_id>
  <pubchem_compound_id>813</pubchem_compound_id>
  <chemspider_id>791</chemspider_id>
  <kegg_id>C00238</kegg_id>
  <chebi_id>26216</chebi_id>
  <biocyc_id>K+</biocyc_id>
  <het_id>K</het_id>
  <wikipidia>Potassium</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>SCHULTZ, S. G., WILSON, N. L., EPSTEIN, W. (1962). "Cation transport in Escherichia coli. II. Intracellular chloride concentration." J Gen Physiol 46:159-166.</reference_text>
      <pubmed_id>13909522</pubmed_id>
    </reference>
    <reference>
      <reference_text>Schaafsma A, de Vries PJ, Saris WH: Delay of natural bone loss by higher intakes of specific minerals and vitamins. Crit Rev Food Sci Nutr. 2001 May;41(4):225-49.</reference_text>
      <pubmed_id>11401244</pubmed_id>
    </reference>
    <reference>
      <reference_text>Preuss HG: Diet, genetics and hypertension.  J Am Coll Nutr. 1997 Aug;16(4):296-305.</reference_text>
      <pubmed_id>9263178</pubmed_id>
    </reference>
    <reference>
      <reference_text>Beede DK: Mineral and water nutrition.  Vet Clin North Am Food Anim Pract. 1991 Jul;7(2):373-90.</reference_text>
      <pubmed_id>1893277</pubmed_id>
    </reference>
    <reference>
      <reference_text>Brooks G: Potassium additive algorithm for use in continuous renal replacement therapy. Nurs Crit Care. 2006 Nov-Dec;11(6):273-80.</reference_text>
      <pubmed_id>17883675</pubmed_id>
    </reference>
  </general_references>
  <synthesis_reference>Alberti, Augusto.  Recovering potassium salts from the refuse liquor of the manufacture of tartaric acid.    (1910),     US  957295  19100510  CAN 4:13164  AN 1910:13164</synthesis_reference>
  <msds_url>http://hmdb.ca/system/metabolites/msds/000/000/505/original/HMDB00586.pdf?1358895376</msds_url>
  <enzymes>
    <enzyme>
      <name>Potassium-transporting ATPase A chain</name>
      <uniprot_id>P03959</uniprot_id>
      <uniprot_name>ATKA_ECOLI</uniprot_name>
      <gene_name>kdpA</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P03959.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Potassium-transporting ATPase B chain</name>
      <uniprot_id>P03960</uniprot_id>
      <uniprot_name>ATKB_ECOLI</uniprot_name>
      <gene_name>kdpB</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P03960.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Potassium-transporting ATPase C chain</name>
      <uniprot_id>P03961</uniprot_id>
      <uniprot_name>ATKC_ECOLI</uniprot_name>
      <gene_name>kdpC</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P03961.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Protein kdpF</name>
      <uniprot_id>P36937</uniprot_id>
      <uniprot_name>KDPF_ECOLI</uniprot_name>
      <gene_name>kdpF</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P36937.xml</protein_url>
    </enzyme>
  </enzymes>
  <transporters>
    <enzyme>
      <name>Potassium-transporting ATPase A chain</name>
      <uniprot_id>P03959</uniprot_id>
      <uniprot_name>ATKA_ECOLI</uniprot_name>
      <gene_name>kdpA</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P03959.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Potassium-transporting ATPase B chain</name>
      <uniprot_id>P03960</uniprot_id>
      <uniprot_name>ATKB_ECOLI</uniprot_name>
      <gene_name>kdpB</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P03960.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Potassium-transporting ATPase C chain</name>
      <uniprot_id>P03961</uniprot_id>
      <uniprot_name>ATKC_ECOLI</uniprot_name>
      <gene_name>kdpC</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P03961.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Multidrug translocase mdfA</name>
      <uniprot_id>P0AEY8</uniprot_id>
      <uniprot_name>MDFA_ECOLI</uniprot_name>
      <gene_name>cmr</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AEY8.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Trk system potassium uptake protein trkG</name>
      <uniprot_id>P23849</uniprot_id>
      <uniprot_name>TRKG_ECOLI</uniprot_name>
      <gene_name>trkG</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P23849.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Calcium/proton antiporter</name>
      <uniprot_id>P31801</uniprot_id>
      <uniprot_name>CHAA_ECOLI</uniprot_name>
      <gene_name>chaA</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P31801.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Low affinity potassium transport system protein kup</name>
      <uniprot_id>P63183</uniprot_id>
      <uniprot_name>KUP_ECOLI</uniprot_name>
      <gene_name>kup</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P63183.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Trk system potassium uptake protein trkA</name>
      <uniprot_id>P0AGI8</uniprot_id>
      <uniprot_name>TRKA_ECOLI</uniprot_name>
      <gene_name>trkA</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AGI8.xml</protein_url>
    </enzyme>
    <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>Trk system potassium uptake protein trkH</name>
      <uniprot_id>P0AFZ7</uniprot_id>
      <uniprot_name>TRKH_ECOLI</uniprot_name>
      <gene_name>trkH</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AFZ7.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Peptide transport system ATP-binding protein sapD</name>
      <uniprot_id>P0AAH4</uniprot_id>
      <uniprot_name>SAPD_ECOLI</uniprot_name>
      <gene_name>sapD</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AAH4.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Glutathione-regulated potassium-efflux system protein kefC</name>
      <uniprot_id>P03819</uniprot_id>
      <uniprot_name>KEFC_ECOLI</uniprot_name>
      <gene_name>kefC</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P03819.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>Glutathione-regulated potassium-efflux system protein kefB</name>
      <uniprot_id>P45522</uniprot_id>
      <uniprot_name>KEFB_ECOLI</uniprot_name>
      <gene_name>kefB</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P45522.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Protein kdpF</name>
      <uniprot_id>P36937</uniprot_id>
      <uniprot_name>KDPF_ECOLI</uniprot_name>
      <gene_name>kdpF</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P36937.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>
    <enzyme>
      <name>Putative potassium channel protein</name>
      <uniprot_id>P31069</uniprot_id>
      <uniprot_name>KCH_ECOLI</uniprot_name>
      <gene_name>kch</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P31069.xml</protein_url>
    </enzyme>
  </transporters>
  <reactions>
    <reaction_text>Adenosine triphosphate + Water + Potassium &gt; ADP + Hydrogen ion + Potassium + Phosphate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>TRANS-RXN-2</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + Water + Potassium &gt; ADP + Hydrogen ion + Potassium + Phosphate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>TRANS-RXN-2</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Potassium + Water + Adenosine triphosphate &gt; Potassium + Phosphate + ADP + Hydrogen ion</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>TRANS-RXN-2</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Potassium + Water + Adenosine triphosphate &gt; Potassium + Phosphate + ADP + Hydrogen ion</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>TRANS-RXN-2</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>ADP + Phosphate + 4 Hydrogen ion + Heme + Nickel(2+) + Iron chelate + Taurine + Molybdate + Magnesium + Fe3+ + Potassium + Polyamine + vitamin B12 + Sulfate + glycerol-3-phosphate + Phosphonate + D-Maltose &lt;&gt; Adenosine triphosphate +3 Hydrogen ion + Water</reaction_text>
    <kegg_reaction_id>R00086</kegg_reaction_id>
    <ecocyc_id>RXN0-1061</ecocyc_id>
    <pw_reaction_id/>
  </reactions>
  <concentrations>
    <growth_media>16 mM NaH2PO4; 32 mM Na2HPO4; 5 mM (NH4)2SO4; 40 mM NaCl; 5 mM KCl; 0.4 mM MgSO4, 55 mM glucose</growth_media>
    <growth_system>Shake flask</growth_system>
    <concentration>9600.0</concentration>
    <concentration_units>uM</concentration_units>
    <internal/>
    <error>1100.0</error>
    <temperature>37 oC</temperature>
    <strain>K12</strain>
    <growth_status>Stationary Phase (50 mM chloride in media)</growth_status>
    <molecules>38400000</molecules>
    <molecules_error>4400000</molecules_error>
    <reference>
      <reference_text>SCHULTZ, S. G., WILSON, N. L., EPSTEIN, W. (1962). "Cation transport in Escherichia coli. II. Intracellular chloride concentration." J Gen Physiol 46:159-166.</reference_text>
      <pubmed_id>13909522</pubmed_id>
    </reference>
    <growth_media>16 mM NaH2PO4; 32 mM Na2HPO4; 5 mM (NH4)2SO4; 40 mM NaCl; 5 mM KCl; 0.4 mM MgSO4, 55 mM glucose</growth_media>
    <growth_system>Shake flask</growth_system>
    <concentration>224000.0</concentration>
    <concentration_units>uM</concentration_units>
    <internal/>
    <error>8000.0</error>
    <temperature>37 oC</temperature>
    <strain>K12</strain>
    <growth_status>Mid-Log Phase (50 mM chloride in media)</growth_status>
    <molecules>896000000</molecules>
    <molecules_error>32000000</molecules_error>
    <reference>
      <reference_text>SCHULTZ, S. G., WILSON, N. L., EPSTEIN, W. (1962). "Cation transport in Escherichia coli. II. Intracellular chloride concentration." J Gen Physiol 46:159-166.</reference_text>
      <pubmed_id>13909522</pubmed_id>
    </reference>
    <growth_media/>
    <growth_system/>
    <concentration>225000.0</concentration>
    <concentration_units>uM</concentration_units>
    <internal/>
    <error>25000.0</error>
    <temperature/>
    <strain>K-12</strain>
    <growth_status/>
    <molecules>900000000</molecules>
    <molecules_error>100000000</molecules_error>
    <reference>
      <reference_text>1. Cybercell Database: &lt;a href='http://ccdb.wishartlab.com/CCDB/cgi-bin/STAT_NEW.cgi'&gt;http://ccdb.wishartlab.com/CCDB/cgi-bin/STAT_NEW.cgi&lt;/a&gt; &lt;br&gt;	2. Phillips R., Kondev, J., Theriot, J. (2008) “Physical Biology of the Cell” Garland Science, New York, NY.</reference_text>
      <pubmed_id/>
    </reference>
  </concentrations>
</compound>
