<?xml version="1.0" encoding="UTF-8"?>
<compound>
  <version>2.0</version>
  <creation_date>2012-05-31 13:57:21 -0600</creation_date>
  <update_date>2015-09-17 16:24:10 -0600</update_date>
  <accession>ECMDB02908</accession>
  <m2m_id>M2MDB000470</m2m_id>
  <name>Sodium</name>
  <description>Sodium is a metallic element that is soluble in water in nearly all of its compounds, and is thus present in great quantities in the Earth's oceans and other stagnant bodies of water. In these bodies it is mostly counterbalanced by the chloride ion, causing evaporated ocean water solids to consist mostly of sodium chloride, or common table salt. Sodium ion is also a component of many minerals. Export of sodium from the cell provides the driving force for several secondary active transporters membrane transport proteins, which import glucose, amino acids, and other nutrients into the cell by use of the sodium gradient.</description>
  <synonyms>
    <synonym>Sodium</synonym>
    <synonym>Sodium ion</synonym>
  </synonyms>
  <chemical_formula>Na</chemical_formula>
  <average_molecular_weight>22.9898</average_molecular_weight>
  <monisotopic_moleculate_weight>22.989769675</monisotopic_moleculate_weight>
  <iupac_name>sodium(1+) ion</iupac_name>
  <traditional_iupac>sodium(1+) ion</traditional_iupac>
  <cas_registry_number>7440-23-5</cas_registry_number>
  <smiles>[Na+]</smiles>
  <inchi>InChI=1S/Na/q+1</inchi>
  <inchikey>FKNQFGJONOIPTF-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>97.82 oC</value>
    </property>
  </experimental_properties>
  <property>
    <kind>logp</kind>
    <value>-0.77</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>pka_strongest_acidic</kind>
    <value>3.09</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>iupac</kind>
    <value>sodium(1+) ion</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>average_mass</kind>
    <value>22.9898</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>mono_mass</kind>
    <value>22.989769675</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>smiles</kind>
    <value>[Na+]</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>formula</kind>
    <value>Na</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>inchi</kind>
    <value>InChI=1S/Na/q+1</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>inchikey</kind>
    <value>FKNQFGJONOIPTF-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>Glutathione metabolism</name>
      <description>The biosynthesis of glutathione starts with the introduction of L-glutamic acid through either  a glutamate:sodium symporter, glutamate / aspartate : H+ symporter GltP or a 
glutamate / aspartate ABC transporter. Once in the cytoplasm, L-glutamice acid reacts with L-cysteine through an ATP glutamate-cysteine ligase resulting in gamma-glutamylcysteine. This compound reacts which Glycine through an ATP driven glutathione synthetase thus catabolizing Glutathione.
This compound is metabolized through a spontaneous reaction with an oxidized glutaredoxin resulting in a reduced glutaredoxin and an oxidized glutathione. This compound is reduced by a NADPH glutathione reductase resulting in a glutathione. 
</description>
      <pathwhiz_id>PW000833</pathwhiz_id>
      <kegg_map_id>ec00480</kegg_map_id>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>Galactose metabolism</name>
      <description>Galactose can be synthesized through two pathways: melibiose degradation involving an alpha galactosidase and lactose degradation involving a beta galactosidase. Melibiose is first transported inside the cell through the melibiose:Li+/Na+/H+ symporter. Once inside the cell, melibiose is degraded through alpha galactosidase  into an alpha-D-galactose and a beta-D-glucose. The beta-D-glucose is phosphorylated by a glucokinase to produce a beta-D-glucose-6-phosphate which can spontaneously be turned into a alpha D glucose 6 phosphate. This alpha D-glucose-6-phosphate is metabolized into a glucose -1-phosphate through a phosphoglucomutase-1. The glucose -1-phosphate is transformed into a uridine diphosphate glucose through UTP--glucose-1-phosphate uridylyltransferase. The product, uridine diphosphate glucose, can undergo a reversible reaction in which it can be turned into uridine diphosphategalactose through an UDP-glucose 4-epimerase.
Galactose can also be produced by lactose degradation involving a lactose permease to uptake lactose from the environment and a beta-galactosidase to turn lactose into Beta-D-galactose. 
Beta-D-galactose can also be uptaken from the environment through a galactose proton symporter.
Galactose is degraded through the following process:
Beta-D-galactose is introduced into the cytoplasm through a galactose proton symporter, or it can be synthesized from an alpha lactose that is introduced into the cytoplasm through a lactose permease. Alpha lactose interacts with water through a beta-galactosidase resulting in a beta-D-glucose and beta-D-galactose. Beta-D-galactose is isomerized into D-galactose. D-Galactose undergoes phosphorylation through a galactokinase, hence producing galactose 1 phosphate. On the other side of the pathway, a gluose-1-phosphate (product of the interaction of alpha-D-glucose 6-phosphate with a phosphoglucomutase resulting in a alpha-D-glucose-1-phosphate, an isomer of Glucose 1-phosphate, or an isomer of Beta-D-glucose 1-phosphate) interacts with UTP and a hydrogen ion in order to produce a uridine diphosphate glucose. This is followed by the interaction of galactose-1-phosphate with an established amount of uridine diphosphate glucose through a galactose-1-phosphate uridylyltransferase, which in turn output a glucose-1-phosphate and a uridine diphosphate galactose. The glucose -1-phosphate is transformed into a uridine diphosphate glucose through UTP--glucose-1-phosphate uridylyltransferase. The product, uridine diphosphate glucose, can undergo a reversible reaction in which it can be turned into uridine diphosphategalactose through an  UDP-glucose 4-epimerase, and so the cycle can keep going as long as more lactose or galactose is imported into the cell
</description>
      <pathwhiz_id>PW000821</pathwhiz_id>
      <kegg_map_id>ec00052</kegg_map_id>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>Methane metabolism</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec00680</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>D-Glutamine and D-glutamate metabolism</name>
      <description>L-glutamine is transported into the cytoplasm through a glutamine ABC transporter. Once inside, L-glutamine is metabolized with glutaminase to produce an L-glutamic acid. This process can be reversed through a glutamine synthetase resulting in L-glutamine.
L-glutamic acid can also be transported into the cytoplasm through various methods: a glutamate/aspartate:H+ symporter GltP, a glutamate: sodium symporter or a glutamate/aspartate ABC transporter. 
L-glutamic acid can proceed to L-glutamate metabolism or it can undergo a reversible reaction through a glutamate racemase resulting in D-glutamic acid. This compound can also be obtained from D-glutamine interacting with a glutaminase.
D-glutamic acid reacts with UDP-N-acetylmuramoyl-L-alanine through an ATP driven UDP-N-acetylmuramoylalanine-D-glutamate ligase resulting in a UDP-N-acetylmuramoyl-L-alanyl-D-glutamate which is then integrated into the peptidoglycan biosynthesis
 UDP-N-acetylmuramoyl-L-alanine comes from the amino sugar and nucleotide sugar metabolism product, UDP-N-acetylmuraminate which reacts with L-alanine through an ATP-driven UDP-N-acetylmuramate-L-alanine ligase.



</description>
      <pathwhiz_id>PW000769</pathwhiz_id>
      <kegg_map_id>ec00471</kegg_map_id>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>Biosynthesis of siderophore group nonribosomal peptides</name>
      <description>2,3-dihydroxybenzoate is synthesized from chorismate via isochorismate and 2,3-dihydroxy-2,3-dihydrobenzoate. 
The biosynthesis of 2,3-dihydroxybenzoate starts  from chorismate being synthesized into isochorismate through isochorismate synthase entC.  EntC catalyzes the conversion of chorismate to isochorismate. The N-terminal isochorismate lyase domain of EntB hydrolyzes the pyruvate group of isochorismate to produce 2,3-dihydro-2,3-dihydroxybenzoate. The conversion of this latter compound to 2,3-dihydroxybenzoate is catalyzed by the EntA dehydrogenase.This compound then interacts with L-serine and ATP through enterobactin synthase protein complex resulting in the production of enterobactin. Enterobactin is exported into the periplasmic space through the enterobactin exporter entS. The compound is the export to the environment through the outer membrane protein TolC. In the environment enterobactin reacts with iron to produce Ferric enterobactin. This compound is imported into the periplasmic space through a ferric enterobactin outermembrane transport complex. The compound then enters the cytoplasm through a ferric enterobactin ABC transporter.Once inside the cytoplasm, ferric enterobactin spontaneously releases the iron  ion from the enterobactin.
</description>
      <pathwhiz_id>PW000760</pathwhiz_id>
      <kegg_map_id>ec01053</kegg_map_id>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>ABC transporters</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec02010</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>GLYCINE BIOSYNTHESIS</name>
      <description>One step pathway for glycine biosynthesis dependent on L-serine, is a major source of one-carbon units in the form of 5,10-methylene tetrahydrofolate. L-serine is enters cell through transporters (serine / threonine:H+ symporter TdcC, serine/threonine: Na symporter , serine:H+ symporter SdaC )  and then proceeds through reversible reaction with a tetrahydrofolic acid through a serine hydroxymethyltransferase enzyme in order to produce glycine, 5,10-methylene tetrahydrofolate and water</description>
      <pathwhiz_id>PW000808</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>L-glutamate metabolism</name>
      <description>
There are various ways by which glutamate enters the cytoplasm in E.coli. through a glutamate:sodium symporter, glutamate / aspartate : H+ symporter GltP or a
glutamate / aspartate ABC transporter.
There are various ways by which E. coli synthesizes glutamate from L-glutamine or oxoglutaric acid.
L-glutamine, introduced into the cytoplasm by glutamine ABC transporter, can either interact with glutaminase resulting in ammonia and L-glutamic acid, or react with oxoglutaric acid, and hydrogen ion through an NADPH driven glutamate synthase resulting in L-glutamic acid.
L-glutamic acid is metabolized into L-glutamine  by reacting with ammonium through a ATP driven glutamine synthase. L-glutamic acid can also be metabolized into L-aspartic acid by reacting with oxalacetic acid through an aspartate transaminase  resulting in n oxoglutaric acid and L-aspartic acid. L-aspartic acid is metabolized into fumaric acid through an 
aspartate ammonia-lyase. Fumaric acid can be introduced into the cytoplasm through 3 methods: 
dicarboxylate transporter , C4 dicarboxylate / C4 monocarboxylate transporter DauA, and C4 dicarboxylate / orotate:H+ symporter
</description>
      <pathwhiz_id>PW000789</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>Porphyrin metabolism</name>
      <description>The metabolism of porphyrin begins with with glutamic acid being processed by an ATP-driven glutamyl-tRNA synthetase by interacting with hydrogen ion and tRNA(Glu), resulting in amo, pyrophosphate and L-glutamyl-tRNA(Glu) Glutamic acid. Glutamic acid can be obtained as a result of L-glutamate metabolism pathway, glutamate / aspartate : H+ symporter GltP, glutamate:sodium symporter or a glutamate / aspartate ABC transporter .
L-glutamyl-tRNA(Glu) Glutamic acid interacts with a NADPH glutamyl-tRNA reductase resulting in a NADP, a tRNA(Glu) and a (S)-4-amino-5-oxopentanoate. 
This compound interacts with a glutamate-1-semialdehyde aminotransferase resulting a 5-aminolevulinic acid. This compound interacts with a porphobilinogen synthase resulting in a hydrogen ion, water and porphobilinogen. The latter compound interacts with water resulting in hydroxymethylbilane synthase resulting in ammonium, and hydroxymethylbilane. 
 Hydroxymethylbilane can either be dehydrated to produce uroporphyrinogen I or interact with a uroporphyrinogen III synthase resulting in a water molecule and a uroporphyrinogen III.
Uroporphyrinogen I interacts with hydrogen ion through a uroporphyrinogen decarboxylase resulting in a carbon dioxide and a coproporphyrinogen I
Uroporphyrinogen III can be metabolized into precorrin by interacting with a S-adenosylmethionine through a siroheme synthase resulting in hydrogen ion, an s-adenosylhomocysteine and a precorrin-1. On the other hand, Uroporphyrinogen III interacts with hydrogen ion through a uroporphyrinogen decarboxylase resulting in a carbon dioxide and a Coproporphyrinogen III.
Precorrin-1 reacts with a S-adenosylmethionine through a siroheme synthase resulting in a S-adenosylhomocysteine and a Precorrin-2. The latter compound is processed by a NAD dependent uroporphyrin III C-methyltransferase [multifunctional] resulting in a NADH and a sirohydrochlorin. This compound then interacts with Fe 2+ 
uroporphyrin III C-methyltransferase [multifunctional] resulting in a hydrogen ion and a siroheme. The siroheme is then processed in sulfur metabolism pathway.
Uroporphyrinogen III can be processed in anaerobic or aerobic condition. 
Anaerobic:
Uroporphyrinogen III interacts with an oxygen molecule, a hydrogen ion through a coproporphyrinogen III oxidase resulting in water, carbon dioxide and protoporphyrinogen IX. The latter compound then interacts with an 3 oxygen molecule through a protoporphyrinogen oxidase resulting in 3 hydrogen peroxide and a Protoporphyrin IX
Aerobic:
Uroporphyrinogen III reacts with S-adenosylmethionine through a coproporphyrinogen III dehydrogenase resulting in carbon dioxide, 5-deoxyadenosine, L-methionine and protoporphyrinogen IX. The latter compound interacts with a meanquinone through a protoporphyrinogen oxidase resulting in protoporphyrin IX.

The protoporphyrin IX interacts with Fe 2+ through a ferrochelatase resulting in a hydrogen ion and a ferroheme b. The ferroheme b can either be incorporated into the oxidative phosphorylation as a cofactor of the enzymes involved in that pathway or it can interact with hydrogen peroxide through a catalase HPII resulting in a heme D. Heme D can then be incorporated into the oxidative phosphyrlation pathway as a cofactor of the enzymes involved in that pathway. Ferroheme b can also interact with water and a farnesyl pyrophosphate through a heme O synthase resulting in a release of pyrophosphate and heme O. Heme O is then incorporated into the Oxidative phosphorylation pathway.
</description>
      <pathwhiz_id>PW000936</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>inner membrane transport</name>
      <description>list of inner membrane transport complexes, transporting compounds from the periplasmic space to the cytosol
This pathway should be updated regularly with the new inner membrae transports added</description>
      <pathwhiz_id>PW000786</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>isoleucine biosynthesis</name>
      <description>Isoleucine biosynthesis begins with L-threonine from the threonine biosynthesis pathway. L-threonine interacts with a threonine dehydratase biosynthetic releasing water, a hydrogen ion and (2Z)-2-aminobut-2-enoate. This compound is isomerized into a 2-iminobutanoate which interacts with water and a hydrogen ion spontaneously, resulting in the release of ammonium and 2-ketobutyric acid. This compound reacts with pyruvic acid and hydrogen ion through an acetohydroxybutanoate synthase / acetolactate synthase 2 resulting in carbon dioxide and (S)-2-Aceto-2-hydroxybutanoic acid. The latter compound is reduced by an NADPH driven acetohydroxy acid isomeroreductase releasing NADP and acetohydroxy acid isomeroreductase. The latter compound is dehydrated by a dihydroxy acid dehydratase resulting in  3-methyl-2-oxovaleric acid.This compound reacts in a reversible reaction with L-glutamic acid through a Branched-chain-amino-acid aminotransferase resulting in oxoglutaric acid and L-isoleucine.
L-isoleucine can also be transported into  the cytoplasm through two different methods:  a branched chain amino acid ABC transporter or a 
branched chain amino acid transporter BrnQ





y.

</description>
      <pathwhiz_id>PW000818</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>peptidoglycan biosynthesis I</name>
      <description>Peptidoglycan is a net-like polymer which surrounds the cytoplasmic membrane of most bacteria and functions to maintain cell shape and prevent rupture due to the internal turgor.In E. coli K-12, the peptidoglycan consists of glycan strands of alternating subunits of N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid (MurNAc) which are cross-linked by short peptides. The pathway for constructing this net involves two cell compartments: cytoplasm and periplasmic space. 
The pathway starts with a beta-D-fructofuranose going through a mannose  PTS permease, phosphorylating the compund and producing a beta-D-fructofuranose 6 phosphate. This compound can be obtained from the glycolysis and pyruvate dehydrogenase or from an isomerization reaction of Beta-D-glucose 6-phosphate through a glucose-6-phosphate isomerase.The compound Beta-D-fructofuranose 6 phosphate and L-Glutamine react with a glucosamine fructose-6-phosphate aminotransferase, thus producing a glucosamine 6-phosphate  and a l-glutamic acid. The glucosamine 6-phosphate interacts with phosphoglucosamine mutase in a reversible reaction producing glucosamine-1P. Glucosamine-1p and acetyl coa undergo acetylation throuhg a bifunctional protein glmU releasing Coa and a hydrogen ion and producing a N-acetyl-glucosamine 1-phosphate. Glmu, being a bifunctional protein, follows catalyze the interaction of N-acetyl-glucosamine 1-phosphate, hydrogen ion and UTP into UDP-N-acetylglucosamine and pyrophosphate. UDP-N-acetylglucosamine then interacts with phosphoenolpyruvic acid and a UDP-N acetylglucosamine 1- carboxyvinyltransferase realeasing a phosphate and the compound UDP-N-acetyl-alpha-D-glucosamine-enolpyruvate. This compound undergoes a NADPH dependent reduction producing a UDP-N-acetyl-alpha-D-muramate through a UDP-N-acetylenolpyruvoylglucosamine reductase. UDP-N-acetyl-alpha-D-muramate and L-alanine react in an ATP-mediated ligation through a UDP-N-acetylmuramate-alanine ligase releasing an ADP, hydrogen ion, a phosphate and a UDP-N-acetylmuramoyl-L-alanine. This compound interacts with D-glutamic acid and ATP through  UDP-N-acetylmuramoylalanine-D-glutamate ligase releasing ADP, A phosphate and UDP-N-acetylmuramoyl-L-alanyl-D-glutamate. The latter compound then interacts with meso-diaminopimelate in an ATP mediated ligation through a UDP-N-acetylmuramoylalanine-D-glutamate-2,6-diaminopimelate ligase resulting in ADP, phosphate, hydrogen ion and UDP-N-Acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diaminopimelate. This compound in turn with D-alanyl-D-alanine react in an ATP-mediated ligation through UDP-N-Acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase to produce UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gama-D-glutamyl-meso-2,6-diaminopimeloyl-Dalanyl-D-alanine and hydrogen ion, ADP, phosphate. UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gama-D-glutamyl-meso-2,6-diaminopimeloyl-Dalanyl-D-alanine interacts with di-trans,octa-cis-undecaprenyl phosphate through a phospho-N-acetylmuramoyl-pentapeptide-transferase, resulting in UMP and Undecaprenyl-diphospho-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine which in turn reacts with a UDP-N-acetylglucosamine through a N-acetylglucosaminyl transferase to produce a hydrogen, UDP and ditrans,octacis-undecaprenyldiphospho-N-acetyl-(N-acetylglucosaminyl)muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine. This compound ends the cytoplasmic part of the pathway. ditrans,octacis-undecaprenyldiphospho-N-acetyl-(N-acetylglucosaminyl)muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine is transported through a lipi II flippase. Once in the periplasmic space, the compound reacts with a penicillin binding protein 1A prodducing a peptidoglycan dimer, a hydrogen ion, and UDP. The peptidoglycan dimer then reacts with a penicillin binding protein 1B  producing a peptidoglycan with D,D, cross-links and a D-alanine. 
</description>
      <pathwhiz_id>PW000906</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>glutathione metabolism II</name>
      <description>The biosynthesis of glutathione starts with the introduction of L-glutamic acid through either  a glutamate:sodium symporter, glutamate / aspartate : H+ symporter GltP or a 
glutamate / aspartate ABC transporter. Once in the cytoplasm, L-glutamice acid reacts with L-cysteine through an ATP glutamate-cysteine ligase resulting in gamma-glutamylcysteine. This compound reacts which Glycine through an ATP driven glutathione synthetase thus catabolizing Glutathione.
This compound is metabolized through a spontaneous reaction with an oxidized glutaredoxin resulting in a reduced glutaredoxin and an oxidized glutathione. This compound is reduced by a NADPH glutathione reductase resulting in a glutathione. 
Glutathione can then be degraded into various different glutathione containg compounds by reacting with a napthalene through a glutathione S-transferase
</description>
      <pathwhiz_id>PW001927</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>glutathione metabolism III</name>
      <description>The biosynthesis of glutathione starts with the introduction of L-glutamic acid through either  a glutamate:sodium symporter, glutamate / aspartate : H+ symporter GltP or a 
glutamate / aspartate ABC transporter. Once in the cytoplasm, L-glutamice acid reacts with L-cysteine through an ATP glutamate-cysteine ligase resulting in gamma-glutamylcysteine. This compound reacts which Glycine through an ATP driven glutathione synthetase thus catabolizing Glutathione.
This compound is metabolized through a spontaneous reaction with an oxidized glutaredoxin resulting in a reduced glutaredoxin and an oxidized glutathione. This compound is reduced by a NADPH glutathione reductase resulting in a glutathione. 
</description>
      <pathwhiz_id>PW002018</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>peptidoglycan biosynthesis I 2</name>
      <description>Peptidoglycan is a net-like polymer which surrounds the cytoplasmic membrane of most bacteria and functions to maintain cell shape and prevent rupture due to the internal turgor.In E. coli K-12, the peptidoglycan consists of glycan strands of alternating subunits of N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid (MurNAc) which are cross-linked by short peptides. The pathway for constructing this net involves two cell compartments: cytoplasm and periplasmic space. The pathway starts with a beta-D-fructofuranose going through a mannose PTS permease, phosphorylating the compund and producing a beta-D-fructofuranose 6 phosphate. This compound can be obtained from the glycolysis and pyruvate dehydrogenase or from an isomerization reaction of Beta-D-glucose 6-phosphate through a glucose-6-phosphate isomerase.The compound Beta-D-fructofuranose 6 phosphate and L-Glutamine react with a glucosamine fructose-6-phosphate aminotransferase, thus producing a glucosamine 6-phosphate and a l-glutamic acid. The glucosamine 6-phosphate interacts with phosphoglucosamine mutase in a reversible reaction producing glucosamine-1P. Glucosamine-1p and acetyl coa undergo acetylation throuhg a bifunctional protein glmU releasing Coa and a hydrogen ion and producing a N-acetyl-glucosamine 1-phosphate. Glmu, being a bifunctional protein, follows catalyze the interaction of N-acetyl-glucosamine 1-phosphate, hydrogen ion and UTP into UDP-N-acetylglucosamine and pyrophosphate. UDP-N-acetylglucosamine then interacts with phosphoenolpyruvic acid and a UDP-N acetylglucosamine 1- carboxyvinyltransferase realeasing a phosphate and the compound UDP-N-acetyl-alpha-D-glucosamine-enolpyruvate. This compound undergoes a NADPH dependent reduction producing a UDP-N-acetyl-alpha-D-muramate through a UDP-N-acetylenolpyruvoylglucosamine reductase. UDP-N-acetyl-alpha-D-muramate and L-alanine react in an ATP-mediated ligation through a UDP-N-acetylmuramate-alanine ligase releasing an ADP, hydrogen ion, a phosphate and a UDP-N-acetylmuramoyl-L-alanine. This compound interacts with D-glutamic acid and ATP through UDP-N-acetylmuramoylalanine-D-glutamate ligase releasing ADP, A phosphate and UDP-N-acetylmuramoyl-L-alanyl-D-glutamate. The latter compound then interacts with meso-diaminopimelate in an ATP mediated ligation through a UDP-N-acetylmuramoylalanine-D-glutamate-2,6-diaminopimelate ligase resulting in ADP, phosphate, hydrogen ion and UDP-N-Acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diaminopimelate. This compound in turn with D-alanyl-D-alanine react in an ATP-mediated ligation through UDP-N-Acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase to produce UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gama-D-glutamyl-meso-2,6-diaminopimeloyl-Dalanyl-D-alanine and hydrogen ion, ADP, phosphate. UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gama-D-glutamyl-meso-2,6-diaminopimeloyl-Dalanyl-D-alanine interacts with di-trans,octa-cis-undecaprenyl phosphate through a phospho-N-acetylmuramoyl-pentapeptide-transferase, resulting in UMP and N-Acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol which in turn reacts with a UDP-N-acetylglucosamine through a N-acetylglucosaminyl transferase to produce a hydrogen, UDP and Undecaprenyl-diphospho-N-acetylmuramoyl-(N-acetylglucosamine)-L-alanyl-D-glutaminyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine. This compound ends the cytoplasmic part of the pathway. Undecaprenyl-diphospho-N-acetylmuramoyl-(N-acetylglucosamine)-L-alanyl-D-glutaminyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine is transported through a lipi II flippase. Once in the periplasmic space, the compound reacts with a penicillin binding protein 1A prodducing a peptidoglycan dimer, a hydrogen ion, and UDP. The peptidoglycan dimer then reacts with a penicillin binding protein 1B producing a peptidoglycan with D,D, cross-links and a D-alanine.</description>
      <pathwhiz_id>PW002062</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
  </pathways>
  <spectra>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>24779</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>24780</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>24781</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>31337</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>31338</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>31339</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2911922</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2911923</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2911924</spectrum_id>
    </spectrum>
  </spectra>
  <hmdb_id>HMDB00588</hmdb_id>
  <pubchem_compound_id>923</pubchem_compound_id>
  <chemspider_id>899</chemspider_id>
  <kegg_id>C01330</kegg_id>
  <chebi_id>26708</chebi_id>
  <biocyc_id>NA+</biocyc_id>
  <het_id>NA</het_id>
  <wikipidia>Sodium</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>Fox CS, Larson MG, Hwang SJ, Leip EP, Rifai N, Levy D, Benjamin EJ, Murabito JM, Meigs JB, Vasan RS: Cross-sectional relations of serum aldosterone and urine sodium excretion to urinary albumin excretion in a community-based sample. Kidney Int. 2006 Jun;69(11):2064-9.</reference_text>
      <pubmed_id>16572107</pubmed_id>
    </reference>
    <reference>
      <reference_text>Felder RA, Jose PA: Mechanisms of disease: the role of GRK4 in the etiology of essential hypertension and salt sensitivity. Nat Clin Pract Nephrol. 2006 Nov;2(11):637-50.</reference_text>
      <pubmed_id>17066056</pubmed_id>
    </reference>
    <reference>
      <reference_text>Achard JM, Hadchouel J, Faure S, Jeunemaitre X: Inherited sodium avid states.  Adv Chronic Kidney Dis. 2006 Apr;13(2):118-23.</reference_text>
      <pubmed_id>16580612</pubmed_id>
    </reference>
  </general_references>
  <synthesis_reference/>
  <msds_url>http://hmdb.ca/system/metabolites/msds/000/000/507/original/HMDB00588.pdf?1358895667</msds_url>
  <enzymes>
  </enzymes>
  <transporters>
    <enzyme>
      <name>Melibiose carrier protein</name>
      <uniprot_id>P02921</uniprot_id>
      <uniprot_name>MELB_ECOLI</uniprot_name>
      <gene_name>melB</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P02921.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Sodium/proline symporter</name>
      <uniprot_id>P07117</uniprot_id>
      <uniprot_name>PUTP_ECOLI</uniprot_name>
      <gene_name>putP</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P07117.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Uncharacterized transporter yaaJ</name>
      <uniprot_id>P30143</uniprot_id>
      <uniprot_name>YAAJ_ECOLI</uniprot_name>
      <gene_name>yaaJ</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P30143.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Sodium/glutamate symport carrier protein</name>
      <uniprot_id>P0AER8</uniprot_id>
      <uniprot_name>GLTS_ECOLI</uniprot_name>
      <gene_name>gltS</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AER8.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>Serine/threonine transporter sstT</name>
      <uniprot_id>P0AGE4</uniprot_id>
      <uniprot_name>SSTT_ECOLI</uniprot_name>
      <gene_name>sstT</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AGE4.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Sodium/pantothenate symporter</name>
      <uniprot_id>P16256</uniprot_id>
      <uniprot_name>PANF_ECOLI</uniprot_name>
      <gene_name>panF</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P16256.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Cation/acetate symporter ActP</name>
      <uniprot_id>P32705</uniprot_id>
      <uniprot_name>ACTP_ECOLI</uniprot_name>
      <gene_name>actP</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P32705.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Multidrug resistance protein mdtK</name>
      <uniprot_id>P37340</uniprot_id>
      <uniprot_name>MDTK_ECOLI</uniprot_name>
      <gene_name>mdtK</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P37340.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>Na(+)/H(+) antiporter nhaA</name>
      <uniprot_id>P13738</uniprot_id>
      <uniprot_name>NHAA_ECOLI</uniprot_name>
      <gene_name>nhaA</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P13738.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>Uncharacterized symporter yidK</name>
      <uniprot_id>P31448</uniprot_id>
      <uniprot_name>YIDK_ECOLI</uniprot_name>
      <gene_name>yidK</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P31448.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>Inner membrane protein yrbG</name>
      <uniprot_id>P45394</uniprot_id>
      <uniprot_name>YRBG_ECOLI</uniprot_name>
      <gene_name>yrbG</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P45394.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Na(+)/H(+) antiporter nhaB</name>
      <uniprot_id>P0AFA7</uniprot_id>
      <uniprot_name>NHAB_ECOLI</uniprot_name>
      <gene_name>nhaB</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AFA7.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Branched-chain amino acid transport system 2 carrier protein</name>
      <uniprot_id>P0AD99</uniprot_id>
      <uniprot_name>BRNQ_ECOLI</uniprot_name>
      <gene_name>brnQ</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AD99.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>
  </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>188000.0</concentration>
    <concentration_units>uM</concentration_units>
    <internal/>
    <error>3000.0</error>
    <temperature>37 oC</temperature>
    <strain>K12</strain>
    <growth_status>Stationary Phase (50 mM chloride in media)</growth_status>
    <molecules>752000000</molecules>
    <molecules_error>12000000</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>70000.0</concentration>
    <concentration_units>uM</concentration_units>
    <internal/>
    <error>2000.0</error>
    <temperature>37 oC</temperature>
    <strain>K12</strain>
    <growth_status>Mid-Log Phase (50 mM chloride in media)</growth_status>
    <molecules>280000000</molecules>
    <molecules_error>8000000</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>5000.0</concentration>
    <concentration_units>uM</concentration_units>
    <internal/>
    <error>0.0</error>
    <temperature/>
    <strain>K-12</strain>
    <growth_status/>
    <molecules>20000000</molecules>
    <molecules_error>0</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>
