<?xml version="1.0" encoding="UTF-8"?>
<compound>
  <version>2.0</version>
  <creation_date>2012-05-31 10:23:49 -0600</creation_date>
  <update_date>2015-09-13 12:56:07 -0600</update_date>
  <accession>ECMDB00214</accession>
  <m2m_id>M2MDB000087</m2m_id>
  <name>Ornithine</name>
  <description>Ornithine is an amino acid produced in the urea cycle by the splitting off of urea from arginine.  It is a central part of the urea cycle, which allows for the disposal of excess nitrogen.  L-Ornithine is also a precursor of citrulline and arginine.</description>
  <synonyms>
    <synonym>&amp;alpha;,&amp;delta;-diaminovalerate</synonym>
    <synonym>&amp;alpha;,&amp;delta;-diaminovaleric acid</synonym>
    <synonym>(+)-S-Ornithine</synonym>
    <synonym>(S)-2,5-Diaminopentanoate</synonym>
    <synonym>(S)-2,5-Diaminopentanoic acid</synonym>
    <synonym>(S)-a,D-Diaminovalerate</synonym>
    <synonym>(S)-a,D-Diaminovaleric acid</synonym>
    <synonym>(S)-Ornithine</synonym>
    <synonym>2, 5-Diaminopentanoate</synonym>
    <synonym>2, 5-Diaminopentanoic acid</synonym>
    <synonym>2, 5-Diaminovalerate</synonym>
    <synonym>2, 5-Diaminovaleric acid</synonym>
    <synonym>5-Amino-L-Norvaline</synonym>
    <synonym>a,delta-Diaminovalerate</synonym>
    <synonym>a,delta-Diaminovaleric acid</synonym>
    <synonym>a,δ-Diaminovalerate</synonym>
    <synonym>a,δ-Diaminovaleric acid</synonym>
    <synonym>Alpha,delta-Diaminovalerate</synonym>
    <synonym>Alpha,delta-Diaminovaleric acid</synonym>
    <synonym>L-(-)-Ornithine</synonym>
    <synonym>L-Ornithine</synonym>
    <synonym>Ornithine</synonym>
    <synonym>α,δ-Diaminovalerate</synonym>
    <synonym>α,δ-Diaminovaleric acid</synonym>
  </synonyms>
  <chemical_formula>C5H12N2O2</chemical_formula>
  <average_molecular_weight>132.161</average_molecular_weight>
  <monisotopic_moleculate_weight>132.089877638</monisotopic_moleculate_weight>
  <iupac_name>(2S)-2,5-diaminopentanoic acid</iupac_name>
  <traditional_iupac>ornithine</traditional_iupac>
  <cas_registry_number>70-26-8</cas_registry_number>
  <smiles>NCCC[C@H](N)C(O)=O</smiles>
  <inchi>InChI=1S/C5H12N2O2/c6-3-1-2-4(7)5(8)9/h4H,1-3,6-7H2,(H,8,9)/t4-/m0/s1</inchi>
  <inchikey>AHLPHDHHMVZTML-BYPYZUCNSA-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>-3.64</value>
      <source>ALOGPS</source>
    </property>
    <property>
      <kind>logs</kind>
      <value>0.11</value>
      <source>ALOGPS</source>
    </property>
    <property>
      <kind>solubility</kind>
      <value>1.72e+02 g/l</value>
      <source>ALOGPS</source>
    </property>
  </predicted_properties>
  <experimental_properties>
    <property>
      <kind>melting_point</kind>
      <value>140 oC</value>
    </property>
  </experimental_properties>
  <property>
    <kind>logp</kind>
    <value>-3.7</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>pka_strongest_acidic</kind>
    <value>2.67</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>pka_strongest_basic</kind>
    <value>10.29</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>iupac</kind>
    <value>(2S)-2,5-diaminopentanoic acid</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>average_mass</kind>
    <value>132.161</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>mono_mass</kind>
    <value>132.089877638</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>smiles</kind>
    <value>NCCC[C@H](N)C(O)=O</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>formula</kind>
    <value>C5H12N2O2</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>inchi</kind>
    <value>InChI=1S/C5H12N2O2/c6-3-1-2-4(7)5(8)9/h4H,1-3,6-7H2,(H,8,9)/t4-/m0/s1</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>inchikey</kind>
    <value>AHLPHDHHMVZTML-BYPYZUCNSA-N</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>polar_surface_area</kind>
    <value>89.34</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>refractivity</kind>
    <value>33.21</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>polarizability</kind>
    <value>13.85</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>rotatable_bond_count</kind>
    <value>4</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>acceptor_count</kind>
    <value>4</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>donor_count</kind>
    <value>3</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>physiological_charge</kind>
    <value>1</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>formal_charge</kind>
    <value>0</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>Arginine and proline metabolism</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec00330</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>ABC transporters</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec02010</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>arginine metabolism</name>
      <description>The metabolism of L-arginine starts with the acetylation of L-glutamic acid resulting in a N-acetylglutamic acid while releasing a coenzyme A and a hydrogen ion. N-acetylglutamic acid is then phosphorylated via an ATP driven acetylglutamate kinase which yields a N-acetyl-L-glutamyl 5-phosphate. This compound undergoes a NDPH dependent reduction resulting in N-acetyl-L-glutamate 5-semialdehyde. This compound reacts with L-glutamic acid through a acetylornithine aminotransferase / N-succinyldiaminopimelate aminotransferase to produce  a N-acetylornithine which is then deacetylated through a acetylornithine deacetylase which yield an ornithine.
L-glutamine is used to synthesize carbamoyl phosphate through the interaction of L-glutamine, water, ATP, and hydrogen carbonate. This reaction yields ADP, L-glutamic acid, phosphate, and hydrogen ion. 
Carbamoyl phosphate and ornithine are used to catalyze the production of citrulline through an ornithine carbamoyltransferase. Citrulline reacts with L-aspartic acid through an ATP dependent enzyme, argininosuccinate synthase to produce pyrophosphate, AMP and argininosuccinic acid. Argininosussinic acid is then lyase to produce L-arginine and fumaric acid.
L-arginine can be metabolized into succinic acid by two different sets of reactions:
1. Arginine reacts with succinyl-CoA through a arginine N-succinyltransferase resulting in N2-succinyl-L-arginine while releasing CoA and Hydrogen Ion. N2-succinyl-L-arginine is then dihydrolase to produce a N2-succinyl-L-ornithine through a N-succinylarginine dihydrolase. This compound in turn reacts with oxoglutaric acid through succinylornithine transaminase resulting in L-glutamic acid and N2-succinyl-L-glutamic acid 5-semialdehyde. This compoud in turn reacts with a NAD dependent dehydrogenase resulting in N2-succinylglutamate while releasing NADH and hydrogen ion. N2-succinylglutamate reacts with water through a succinylglutamate desuccinylase resulting in  L-glutamic acid and 
a succinic acid. The succinic acid is then incorporated in the TCA cycle
2.Argine reacts with carbon dioxide and a hydrogen ion through a biodegradative arginine decarboxylase, resulting in Agmatine. This compound is then transformed into putrescine by reacting with water and an agmatinase, and releasing urea. Putrescine can be metabolized by reaction with either l-glutamic acid or oxoglutaric acid. If putrescine reacts with L-glutamic acid, it reacts through an ATP mediated gamma-glutamylputrescine producing a hydrogen ion, ADP, phosphate and gamma-glutamyl-L-putrescine. This compound is reduced by interacting with oxygen, water and a gamma-glutamylputrescine oxidoreductase resulting in ammonium, hydrogen peroxide and 4-gamma-glutamylamino butanal. This compound is dehydrogenated through a NADP mediated reaction  lead by gamma-glutamyl-gamma-aminobutaryaldehyde dehydrogenase resulting in  hydrogen ion, NADPH and 4-glutamylamino butanoate. In turn, the latter compound reacts with water through a gamma-glutamyl-gamma-aminobutyrate hydrolase resulting in L-glutamic acid and Gamma aminobutyric acid. On the other hand, if putrescine reacts with oxoglutaric acid through a putrescine aminotransferase, it results in L-glutamic acid, and a 4-aminobutyraldehyde. This compound reacts with water through a NAD dependent gamma aminobutyraldehyde dehydrogenase resulting in hydrogen ion, NADH and gamma-aminobutyric acid.
Gamma Aaminobutyric acid reacts with oxoglutaric acid through 4-aminobutyrate aminotransferase resulting in L-glutamic acid and succinic acid semialdehyde. This compound in turn can react with with either NADP  or NAD to result in the production of succinic acid through succinate-semialdehyde dehydrogenase or aldehyde dehydrogenase-like protein yneI respectively. Succinic acid can then be integrated in the TCA cycle. 
L-arginine is eventua lly metabolized into succinic acid which then goes to the TCA cycle</description>
      <pathwhiz_id>PW000790</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>ornithine metabolism</name>
      <description>
In the ornithine biosynthesis pathway of E. coli, L-glutamate is acetylated to N-acetylglutamate by the enzyme N-acetylglutamate synthase, encoded by the argA gene. The acetyl donor for this reaction is acetyl-CoA. N-acetylglutamic acid is then phosphorylated via an ATP driven acetylglutamate kinase which yields a N-acetyl-L-glutamyl 5-phosphate. This compound undergoes a NADPH dependent reduction resulting in N-acetyl-L-glutamate 5-semialdehyde. This compound reacts with L-glutamic acid through a acetylornithine aminotransferase / N-succinyldiaminopimelate aminotransferase to produce  a N-acetylornithine which is then deacetylated through a acetylornithine deacetylase which yield an ornithine. Ornithine interacts with hydrogen ion  through a Ornithine decarboxylase resulting in a carbon dioxide release and  a putrescine
Putrescine can be metabolized by reaction with either l-glutamic acid or oxoglutaric acid. If putrescine reacts with L-glutamic acid, it reacts through an ATP mediated gamma-glutamylputrescine producing a hydrogen ion, ADP, phosphate and gamma-glutamyl-L-putrescine. This compound is reduced by interacting with oxygen, water and a gamma-glutamylputrescine oxidoreductase resulting in ammonium, hydrogen peroxide and 4-gamma-glutamylamino butanal. This compound is dehydrogenated through a NADP mediated reaction  lead by gamma-glutamyl-gamma-aminobutaryaldehyde dehydrogenase resulting in  hydrogen ion, NADPH and 4-glutamylamino butanoate. In turn, the latter compound reacts with water through a gamma-glutamyl-gamma-aminobutyrate hydrolase resulting in L-glutamic acid and Gamma aminobutyric acid. On the other hand, if putrescine reacts with oxoglutaric acid through a putrescine aminotransferase, it results in L-glutamic acid, and a 4-aminobutyraldehyde. This compound reacts with water through a NAD dependent gamma aminobutyraldehyde dehydrogenase resulting in hydrogen ion, NADH and gamma-aminobutyric acid.
Gamma Aaminobutyric acid reacts with oxoglutaric acid through 4-aminobutyrate aminotransferase resulting in L-glutamic acid and succinic acid semialdehyde. This compound in turn can react with with either NADP  or NAD to result in the production of succinic acid through succinate-semialdehyde dehydrogenase or aldehyde dehydrogenase-like protein yneI respectively. Succinic acid can then be integrated in the TCA cycle. 

</description>
      <pathwhiz_id>PW000791</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>ornithine biosynthesis</name>
      <ecocyc_pathway_id>GLUTORN-PWY</ecocyc_pathway_id>
    </pathway>
    <pathway>
      <name>arginine biosynthesis I</name>
      <ecocyc_pathway_id>ARGSYN-PWY</ecocyc_pathway_id>
    </pathway>
    <pathway>
      <name>putrescine biosynthesis III</name>
      <ecocyc_pathway_id>PWY-46</ecocyc_pathway_id>
    </pathway>
    <pathway>
      <name>superpathway of ornithine degradation</name>
      <ecocyc_pathway_id>ORNDEG-PWY</ecocyc_pathway_id>
    </pathway>
  </pathways>
  <spectra>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>472</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>473</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>474</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1291</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1415</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1484</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1750</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>2994</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>30085</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>30379</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>30606</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>30798</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>31079</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>31080</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>31081</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>31082</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>31791</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>32270</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>32271</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>32273</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>37363</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>130647</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>138381</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1054761</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1054763</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>1206</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>1207</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>4859</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6152</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6153</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6154</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6155</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6156</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6157</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6158</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6159</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6160</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6161</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6162</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6163</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6164</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6165</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6166</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6167</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6168</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6169</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6170</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6171</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>166442</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>349</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>350</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>351</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>3635</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>3636</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>3637</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>3638</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>3639</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>3640</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>3641</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>3642</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>3643</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>3644</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>3645</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>3646</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>3647</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>3648</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>3649</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>3650</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>3651</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>3652</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>3653</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>179271</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>179272</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>179273</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrTwoD</type>
      <spectrum_id>996</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrTwoD</type>
      <spectrum_id>1212</spectrum_id>
    </spectrum>
  </spectra>
  <hmdb_id>HMDB00214</hmdb_id>
  <pubchem_compound_id>6262</pubchem_compound_id>
  <chemspider_id>6026</chemspider_id>
  <kegg_id>C01602</kegg_id>
  <chebi_id/>
  <biocyc_id>L-ORNITHINE</biocyc_id>
  <het_id>ORN</het_id>
  <wikipidia>Ornithine</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>Sreekumar A, Poisson LM, Rajendiran TM, Khan AP, Cao Q, Yu J, Laxman B, Mehra R, Lonigro RJ, Li Y, Nyati MK, Ahsan A, Kalyana-Sundaram S, Han B, Cao X, Byun J, Omenn GS, Ghosh D, Pennathur S, Alexander DC, Berger A, Shuster JR, Wei JT, Varambally S, Beecher C, Chinnaiyan AM: Metabolomic profiles delineate potential role for sarcosine in prostate cancer progression. Nature. 2009 Feb 12;457(7231):910-4.</reference_text>
      <pubmed_id>19212411</pubmed_id>
    </reference>
    <reference>
      <reference_text>Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva.  J Dent Res. 2002 Jun;81(6):422-7.</reference_text>
      <pubmed_id>12097436</pubmed_id>
    </reference>
    <reference>
      <reference_text>Nicholson JK, O'Flynn MP, Sadler PJ, Macleod AF, Juul SM, Sonksen PH: Proton-nuclear-magnetic-resonance studies of serum, plasma and urine from fasting normal and diabetic subjects. Biochem J. 1984 Jan 15;217(2):365-75.</reference_text>
      <pubmed_id>6696735</pubmed_id>
    </reference>
    <reference>
      <reference_text>Engelborghs S, Marescau B, De Deyn PP: Amino acids and biogenic amines in cerebrospinal fluid of patients with Parkinson's disease. Neurochem Res. 2003 Aug;28(8):1145-50.</reference_text>
      <pubmed_id>12834252</pubmed_id>
    </reference>
    <reference>
      <reference_text>Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7.</reference_text>
      <pubmed_id>6198473</pubmed_id>
    </reference>
    <reference>
      <reference_text>Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14.</reference_text>
      <pubmed_id>15911239</pubmed_id>
    </reference>
    <reference>
      <reference_text>Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6.</reference_text>
      <pubmed_id>12297216</pubmed_id>
    </reference>
    <reference>
      <reference_text>Peters T, Thaete C, Wolf S, Popp A, Sedlmeier R, Grosse J, Nehls MC, Russ A, Schlueter V: A mouse model for cystinuria type I.  Hum Mol Genet. 2003 Sep 1;12(17):2109-20.</reference_text>
      <pubmed_id>12923163</pubmed_id>
    </reference>
    <reference>
      <reference_text>Mayer UM: [Hyperornithinaemia in patients with retinal dystrophy]  Ophthalmologe. 2003 Jan;100(1):55-61.</reference_text>
      <pubmed_id>12557027</pubmed_id>
    </reference>
    <reference>
      <reference_text>Gray RG, Green A, Hall S, McKeown C: Prenatal exclusion of the HHH syndrome.  Prenat Diagn. 1995 May;15(5):474-6.</reference_text>
      <pubmed_id>7644438</pubmed_id>
    </reference>
    <reference>
      <reference_text>Jensen TG, Sullivan DM, Morgan RA, Taichman LB, Nussenblatt RB, Blaese RM, Csaky KG: Retrovirus-mediated gene transfer of ornithine-delta-aminotransferase into keratinocytes from gyrate atrophy patients. Hum Gene Ther. 1997 Nov 20;8(17):2125-32.</reference_text>
      <pubmed_id>9414260</pubmed_id>
    </reference>
    <reference>
      <reference_text>Sell DR, Monnier VM: Ornithine is a novel amino acid and a marker of arginine damage by oxoaldehydes in senescent proteins. Ann N Y Acad Sci. 2005 Jun;1043:118-28.</reference_text>
      <pubmed_id>16037230</pubmed_id>
    </reference>
    <reference>
      <reference_text>Stadler S, Gempel K, Bieger I, Pontz BF, Gerbitz KD, Bauer MF, Hofmann S: Detection of neonatal argininosuccinate lyase deficiency by serum tandem mass spectrometry. J Inherit Metab Dis. 2001 Jun;24(3):370-8.</reference_text>
      <pubmed_id>11486903</pubmed_id>
    </reference>
    <reference>
      <reference_text>Gokmen SS, Aygit AC, Ayhan MS, Yorulmaz F, Gulen S: Significance of arginase and ornithine in malignant tumors of the human skin. J Lab Clin Med. 2001 May;137(5):340-4.</reference_text>
      <pubmed_id>11329531</pubmed_id>
    </reference>
    <reference>
      <reference_text>Morizono H, Woolston JE, Colombini M, Tuchman M: The use of yeast mitochondria to study the properties of wild-type and mutant human mitochondrial ornithine transporter. Mol Genet Metab. 2005 Dec;86(4):431-40. Epub 2005 Oct 26.</reference_text>
      <pubmed_id>16256388</pubmed_id>
    </reference>
  </general_references>
  <synthesis_reference>Zhang, Peng; Zhang, Shurong; Liu, Chunqiao; Yang, Yuhong.  Method for preparing L-ornithine by enzymatic conversion.    Faming Zhuanli Shenqing Gongkai Shuomingshu  (2007),     8pp.</synthesis_reference>
  <msds_url>http://hmdb.ca/system/metabolites/msds/000/000/152/original/HMDB00214.pdf?1358463180</msds_url>
  <enzymes>
    <enzyme>
      <name>Ornithine carbamoyltransferase chain I</name>
      <uniprot_id>P04391</uniprot_id>
      <uniprot_name>OTC1_ECOLI</uniprot_name>
      <gene_name>argI</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P04391.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Ornithine carbamoyltransferase chain F</name>
      <uniprot_id>P06960</uniprot_id>
      <uniprot_name>OTC2_ECOLI</uniprot_name>
      <gene_name>argF</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P06960.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Histidine transport ATP-binding protein hisP</name>
      <uniprot_id>P07109</uniprot_id>
      <uniprot_name>HISP_ECOLI</uniprot_name>
      <gene_name>hisP</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P07109.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Ornithine decarboxylase, constitutive</name>
      <uniprot_id>P21169</uniprot_id>
      <uniprot_name>DCOR_ECOLI</uniprot_name>
      <gene_name>speC</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P21169.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Acetylornithine deacetylase</name>
      <uniprot_id>P23908</uniprot_id>
      <uniprot_name>ARGE_ECOLI</uniprot_name>
      <gene_name>argE</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P23908.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Ornithine decarboxylase, inducible</name>
      <uniprot_id>P24169</uniprot_id>
      <uniprot_name>DCOS_ECOLI</uniprot_name>
      <gene_name>speF</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P24169.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Histidine transport system permease protein hisM</name>
      <uniprot_id>P0AEU3</uniprot_id>
      <uniprot_name>HISM_ECOLI</uniprot_name>
      <gene_name>hisM</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AEU3.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Histidine transport system permease protein hisQ</name>
      <uniprot_id>P52094</uniprot_id>
      <uniprot_name>HISQ_ECOLI</uniprot_name>
      <gene_name>hisQ</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P52094.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Lysine-arginine-ornithine-binding periplasmic protein</name>
      <uniprot_id>P09551</uniprot_id>
      <uniprot_name>ARGT_ECOLI</uniprot_name>
      <gene_name>argT</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P09551.xml</protein_url>
    </enzyme>
  </enzymes>
  <transporters>
    <enzyme>
      <name>Histidine transport ATP-binding protein hisP</name>
      <uniprot_id>P07109</uniprot_id>
      <uniprot_name>HISP_ECOLI</uniprot_name>
      <gene_name>hisP</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P07109.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Histidine transport system permease protein hisM</name>
      <uniprot_id>P0AEU3</uniprot_id>
      <uniprot_name>HISM_ECOLI</uniprot_name>
      <gene_name>hisM</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AEU3.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Histidine transport system permease protein hisQ</name>
      <uniprot_id>P52094</uniprot_id>
      <uniprot_name>HISQ_ECOLI</uniprot_name>
      <gene_name>hisQ</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P52094.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Lysine-arginine-ornithine-binding periplasmic protein</name>
      <uniprot_id>P09551</uniprot_id>
      <uniprot_name>ARGT_ECOLI</uniprot_name>
      <gene_name>argT</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P09551.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>Putative arginine/ornithine antiporter</name>
      <uniprot_id>P0AAE5</uniprot_id>
      <uniprot_name>ARCD_ECOLI</uniprot_name>
      <gene_name>ydgI</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AAE5.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>Putrescine-ornithine antiporter</name>
      <uniprot_id>P0AAF1</uniprot_id>
      <uniprot_name>POTE_ECOLI</uniprot_name>
      <gene_name>potE</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AAF1.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>Adenosine triphosphate + Water + Ornithine &gt; ADP + Hydrogen ion + Ornithine + Phosphate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>ABC-37-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + Water + Ornithine &gt; ADP + Hydrogen ion + Ornithine + Phosphate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>ABC-37-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Hydrogen ion + Ornithine + L-Ornithine &lt;&gt; Carbon dioxide + Putrescine + Ethylenediamine</reaction_text>
    <kegg_reaction_id>R00670</kegg_reaction_id>
    <ecocyc_id>ORNDECARBOX-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Carbamoylphosphate + Ornithine + L-Ornithine &lt;&gt; Citrulline + Hydrogen ion + Phosphate</reaction_text>
    <kegg_reaction_id>R01398</kegg_reaction_id>
    <ecocyc_id>ORNCARBAMTRANSFER-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>N-Acetylornithine + Water &lt;&gt; Acetic acid + Ornithine + L-Ornithine</reaction_text>
    <kegg_reaction_id>R00669</kegg_reaction_id>
    <ecocyc_id>ACETYLORNDEACET-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>N-Acetylornithine + Water &lt;&gt; Acetic acid + Ornithine</reaction_text>
    <kegg_reaction_id>R00669</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Ornithine &lt;&gt; Putrescine + Carbon dioxide</reaction_text>
    <kegg_reaction_id>R00670</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Carbamoylphosphate + Ornithine &lt;&gt; Phosphate + Citrulline</reaction_text>
    <kegg_reaction_id>R01398</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + Ornithine + Water &gt; ADP + Phosphate + Ornithine + Hydrogen ion</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>ABC-37-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + Ornithine + Water &gt; ADP + Phosphate + Ornithine + Hydrogen ion</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>ABC-37-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>N-Acetylornithine + Water &gt; Ornithine + Acetic acid</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>ACETYLORNDEACET-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Ornithine + Carbamoylphosphate &lt;&gt; Hydrogen ion + Citrulline + Phosphate</reaction_text>
    <kegg_reaction_id>R01398</kegg_reaction_id>
    <ecocyc_id>ORNCARBAMTRANSFER-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Hydrogen ion + Ornithine &gt; Carbon dioxide + Putrescine</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>ORNDECARBOX-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Ornithine &gt; Putrescine + Carbon dioxide</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Carbamoylphosphate + Ornithine &gt; Inorganic phosphate + Citrulline</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>N-Acetylornithine + Water &gt; Ornithine + Acetic acid + Ornithine</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id>PW_R002694</pw_reaction_id>
    <reaction_text>Ornithine + Carbamoylphosphate + Ornithine &gt; Phosphate + Hydrogen ion + Citrulline</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id>PW_R002676</pw_reaction_id>
    <reaction_text>Ornithine + Hydrogen ion + Ornithine &gt; Putrescine + Carbon dioxide</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id>PW_R002695</pw_reaction_id>
    <reaction_text>Carbamoylphosphate + Ornithine + L-Ornithine &lt;&gt; Citrulline + Hydrogen ion + Phosphate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Hydrogen ion + Ornithine + L-Ornithine &lt;&gt; Carbon dioxide + Putrescine + Ethylenediamine</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Ornithine &lt;&gt; Putrescine + Carbon dioxide</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>N-Acetylornithine + Water &lt;&gt; Acetic acid + Ornithine + L-Ornithine</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>N-Acetylornithine + Water &lt;&gt; Acetic acid + Ornithine + L-Ornithine</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
  </reactions>
  <concentrations>
    <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>10.1</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>40400</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>
    <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 glycerol</growth_media>
    <growth_system>Shake flask and filter culture</growth_system>
    <concentration>30.3</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>121200</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>
    <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 acetate</growth_media>
    <growth_system>Shake flask and filter culture</growth_system>
    <concentration>27.5</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>110000</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>
    <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>120.0</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>480000</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>Luria-Bertani (LB) media</growth_media>
    <growth_system>Shake flask</growth_system>
    <concentration>267.33</concentration>
    <concentration_units>uM</concentration_units>
    <internal>true</internal>
    <error>10.21</error>
    <temperature>37 oC</temperature>
    <strain>BL21 DE3</strain>
    <growth_status>Stationary phase cultures (overnight culture)</growth_status>
    <molecules>1069333</molecules>
    <molecules_error>40857</molecules_error>
    <reference>
      <reference_text>Lin, Z., Johnson, L. C., Weissbach, H., Brot, N., Lively, M. O., Lowther, W. T. (2007). "Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function." Proc Natl Acad Sci U S A 104:9597-9602.</reference_text>
      <pubmed_id>17535911</pubmed_id>
    </reference>
  </concentrations>
</compound>
