<?xml version="1.0" encoding="UTF-8"?>
<compound>
  <version>2.0</version>
  <creation_date>2012-05-31 09:57:49 -0600</creation_date>
  <update_date>2015-09-13 12:56:06 -0600</update_date>
  <accession>ECMDB00123</accession>
  <m2m_id>M2MDB000046</m2m_id>
  <name>Glycine</name>
  <description>Glycine is a simple amino acid. The glycine cleavage enzyme system comprises four proteins: P-, T-, H- and L-proteins (EC 1.4.4.2, EC 2.1.2.10 and EC 1.8.1.4 for P-, T- and L-proteins). The glycine cleavage system catalyses the oxidative conversion of glycine into carbon dioxide and ammonia, with the remaining one-carbon unit transferred to folate as methylenetetrahydrofolate. It is the main catabolic pathway for glycine and it also contributes to one-carbon metabolism.</description>
  <synonyms>
    <synonym>2-Aminoacetate</synonym>
    <synonym>2-Aminoacetic acid</synonym>
    <synonym>Aciport</synonym>
    <synonym>Amino-Acetate</synonym>
    <synonym>Amino-Acetic acid</synonym>
    <synonym>Aminoacetate</synonym>
    <synonym>Aminoacetic acid</synonym>
    <synonym>Aminoethanoate</synonym>
    <synonym>Aminoethanoic acid</synonym>
    <synonym>G</synonym>
    <synonym>Glicoamin</synonym>
    <synonym>Gly</synonym>
    <synonym>Glycocoll</synonym>
    <synonym>Glycolixir</synonym>
    <synonym>Glycosthene</synonym>
    <synonym>Gyn-Hydralin</synonym>
    <synonym>Padil</synonym>
  </synonyms>
  <chemical_formula>C2H5NO2</chemical_formula>
  <average_molecular_weight>75.0666</average_molecular_weight>
  <monisotopic_moleculate_weight>75.032028409</monisotopic_moleculate_weight>
  <iupac_name>2-aminoacetic acid</iupac_name>
  <traditional_iupac>glycine</traditional_iupac>
  <cas_registry_number>56-40-6</cas_registry_number>
  <smiles>NCC(O)=O</smiles>
  <inchi>InChI=1S/C2H5NO2/c3-1-2(4)5/h1,3H2,(H,4,5)</inchi>
  <inchikey>DHMQDGOQFOQNFH-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>
    <property>
      <kind>logp</kind>
      <value>-3.34</value>
      <source>ALOGPS</source>
    </property>
    <property>
      <kind>logs</kind>
      <value>0.87</value>
      <source>ALOGPS</source>
    </property>
    <property>
      <kind>solubility</kind>
      <value>5.52e+02 g/l</value>
      <source>ALOGPS</source>
    </property>
  </predicted_properties>
  <experimental_properties>
    <property>
      <kind>melting_point</kind>
      <value>504 deg F</value>
    </property>
  </experimental_properties>
  <property>
    <kind>logp</kind>
    <value>-3.4</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>pka_strongest_acidic</kind>
    <value>2.31</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>pka_strongest_basic</kind>
    <value>9.24</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>iupac</kind>
    <value>2-aminoacetic acid</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>average_mass</kind>
    <value>75.0666</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>mono_mass</kind>
    <value>75.032028409</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>smiles</kind>
    <value>NCC(O)=O</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>formula</kind>
    <value>C2H5NO2</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>inchi</kind>
    <value>InChI=1S/C2H5NO2/c3-1-2(4)5/h1,3H2,(H,4,5)</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>inchikey</kind>
    <value>DHMQDGOQFOQNFH-UHFFFAOYSA-N</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>polar_surface_area</kind>
    <value>63.32</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>refractivity</kind>
    <value>16</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>polarizability</kind>
    <value>6.65</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>rotatable_bond_count</kind>
    <value>1</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>acceptor_count</kind>
    <value>3</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>donor_count</kind>
    <value>2</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>physiological_charge</kind>
    <value>0</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>Nitrogen metabolism</name>
      <description>
The biological process of the nitrogen cycle is a complex interplay among many microorganisms catalyzing different reactions, where nitrogen is found in various oxidation states ranging from +5 in nitrate to -3 in ammonia. 
 The ability of fixing atmospheric nitrogen by the nitrogenase enzyme complex is present in restricted prokaryotes (diazotrophs). The other reduction pathways are assimilatory nitrate reduction  and dissimilatory nitrate reduction  both for conversion to ammonia, and denitrification. Denitrification is a respiration in which nitrate or nitrite is reduced as a terminal electron acceptor under low oxygen or anoxic conditions, producing gaseous nitrogen compounds (N2, NO and N2O) to the atmosphere.
Nitrate can be introduced into the cytoplasm through a nitrate:nitrite antiporter NarK or a nitrate / nitrite transporter NarU. Nitrate is then reduced by a Nitrate Reductase resulting in the release of water, an acceptor and a Nitrite. Nitrite can also be introduced into the cytoplasm through a nitrate:nitrite antiporter NarK
Nitrite can be reduced a NADPH dependent nitrite reductase resulting in water and NAD and Ammonia.
Nitrite can interact with hydrogen ion, ferrocytochrome c through a cytochrome c-552 ferricytochrome resulting in the release of ferricytochrome c, water and ammonia
Another process by which ammonia is produced is by a reversible reaction of hydroxylamine with a reduced acceptor through a hydroxylamine reductase resulting in an acceptor, water and ammonia.
Water and carbon dioxide react through a carbonate dehydratase resulting in carbamic acid. This compound reacts spontaneously with hydrogen ion resulting in the release of carbon dioxide and ammonia. Carbon dioxide can interact with water through a carbonic anhydrase resulting in hydrogen carbonate. This compound interacts with cyanate and hydrogen ion through a cyanate hydratase resulting in a carbamic acid. 
Ammonia can be metabolized by reacting with L-glutamine and ATP driven glutamine synthetase resulting in ADP, phosphate and L-glutamine. The latter compound reacts with oxoglutaric acid and hydrogen ion through a NADPH dependent glutamate synthase resulting in the release of NADP and L-glutamic acid. L-glutamic acid reacts with water through a NADP-specific glutamate dehydrogenase resulting in the release of oxoglutaric acid, NADPH, hydrogen ion and ammonia.

</description>
      <pathwhiz_id>PW000755</pathwhiz_id>
      <kegg_map_id>ec00910</kegg_map_id>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>Purine metabolism</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec00230</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>Glycine, serine and threonine metabolism</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec00260</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>Cyanoamino acid metabolism</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec00460</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>Methane metabolism</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec00680</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>Aminoacyl-tRNA biosynthesis</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec00970</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>Porphyrin and chlorophyll metabolism</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec00860</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>Glyoxylate and dicarboxylate metabolism</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec00630</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>One carbon pool by folate</name>
      <description>Dihydrofolic acid, a product of the folate biosynthesis pathway, can be metabolized by multiple enzymes. 
Dihydrofolic acid can be reduced by a NADP-driven dihydrofolate reductase resulting in a NADPH, hydrogen ion and folic acid. 
Dihydrofolic acid can also be reduced by an NADPH-driven dihydrofolate reductase resulting in a NADP and a tetrahydrofolic acid. Folic acid can also produce a tetrahydrofolic acid through a NADPH-driven dihydrofolate reductase. 
Dihydrofolic acid also interacts with 5-thymidylic acid through a thymidylate synthase resulting in the release of dUMP and 5,10-methylene-THF
Tetrahydrofolic acid can be converted into 5,10-methylene-THF through two different reversible reactions.
Tetrahydrofolic acid interacts with a S-Aminomethyldihydrolipoylprotein through a aminomethyltransferase resulting in the release of ammonia, a dihydrolipoylprotein and 5,10-Methylene-THF
Tetrahydrofolic acid interacts with L-serine through a glycine hydroxymethyltransferase resulting in a glycine, water and 5,10-Methylene-THF.
The compound 5,10-methylene-THF reacts with an NADPH dependent methylenetetrahydrofolate reductase [NAD(P)H] resulting in NADP and 5-Methyltetrahydrofolic acid. This compound interacts with homocysteine through a methionine synthase resulting in L-methionine and tetrahydrofolic acid.
Tetrahydrofolic acid can be metabolized into 10-formyltetrahydrofolate through 4 different enzymes:

1.- Tetrahydrofolic acid interacts with FAICAR through a phosphoribosylaminoimidazolecarboxamide formyltransferase resulting in a 1-(5'-Phosphoribosyl)-5-amino-4-imidazolecarboxamide and a 10-formyltetrahydrofolate
2.-Tetrahydrofolic acid interacts with 5'-Phosphoribosyl-N-formylglycinamide through a phosphoribosylglycinamide formyltransferase 2 resulting in a Glycineamideribotide and a 10-formyltetrahydrofolate
3.-Tetrahydrofolic acid interacts with Formic acid through a formyltetrahydrofolate hydrolase resulting in water and a 10-formyltetrahydrofolate
4.-Tetrahydrofolic acid interacts with  N-formylmethionyl-tRNA(fMet) through a 10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-formyltransferase resulting in a L-methionyl-tRNA(Met) and a 10-formyltetrahydrofolate

10-formyltetrahydrofolate can interact with a hydrogen ion through a bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase resulting in water and 
5,10-methenyltetrahydrofolic acid.
 
Tetrahydrofolic acid can be metabolized into 5,10-methenyltetrahydrofolic acid  by reacting with a 
5'-phosphoribosyl-a-N-formylglycineamidine through a phosphoribosylglycinamide formyltransferase 2 resulting in water, glycineamideribotide and  5,10-methenyltetrahydrofolic acid. The latter compound can either interact with water through an aminomethyltransferase resulting in a N5-Formyl-THF, or it can interact with a NADPH driven bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase resulting in a NADP and 5,10-Methylene THF.



</description>
      <pathwhiz_id>PW000773</pathwhiz_id>
      <kegg_map_id>ec00670</kegg_map_id>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>Thiamine metabolism</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec00730</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>Lysine degradation</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec00310</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>Microbial metabolism in diverse environments</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec01120</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>ABC transporters</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec02010</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>Metabolic pathways</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>eco01100</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>One Carbon Pool by Folate I</name>
      <description>Dihydrofolic acid, a product of the folate biosynthesis pathway, can be metabolized by multiple enzymes. 
Dihydrofolic acid can be reduced by a NADP-driven dihydrofolate reductase resulting in a NADPH, hydrogen ion and folic acid. 
Dihydrofolic acid can also be reduced by an NADPH-driven dihydrofolate reductase resulting in a NADP and a tetrahydrofolic acid. Folic acid can also produce a tetrahydrofolic acid through a NADPH-driven dihydrofolate reductase. 
Dihydrofolic acid also interacts with 5-thymidylic acid through a thymidylate synthase resulting in the release of dUMP and 5,10-methylene-THF
Tetrahydrofolic acid can be converted into 5,10-methylene-THF through two different reversible reactions.
Tetrahydrofolic acid interacts with a S-Aminomethyldihydrolipoylprotein through a aminomethyltransferase resulting in the release of ammonia, a dihydrolipoylprotein and 5,10-Methylene-THF
Tetrahydrofolic acid interacts with L-serine through a glycine hydroxymethyltransferase resulting in a glycine, water and 5,10-Methylene-THF.
The compound 5,10-methylene-THF reacts with an NADPH dependent methylenetetrahydrofolate reductase [NAD(P)H] resulting in NADP and 5-Methyltetrahydrofolic acid. This compound interacts with homocysteine through a methionine synthase resulting in L-methionine and tetrahydrofolic acid.
Tetrahydrofolic acid can be metabolized into 10-formyltetrahydrofolate through 4 different enzymes:

1.- Tetrahydrofolic acid interacts with FAICAR through a phosphoribosylaminoimidazolecarboxamide formyltransferase resulting in a 1-(5'-Phosphoribosyl)-5-amino-4-imidazolecarboxamide and a 10-formyltetrahydrofolate
2.-Tetrahydrofolic acid interacts with 5'-Phosphoribosyl-N-formylglycinamide through a phosphoribosylglycinamide formyltransferase 2 resulting in a Glycineamideribotide and a 10-formyltetrahydrofolate
3.-Tetrahydrofolic acid interacts with Formic acid through a formyltetrahydrofolate hydrolase resulting in water and a 10-formyltetrahydrofolate
4.-Tetrahydrofolic acid interacts with  N-formylmethionyl-tRNA(fMet) through a 10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-formyltransferase resulting in a L-methionyl-tRNA(Met) and a 10-formyltetrahydrofolate

10-formyltetrahydrofolate can interact with a hydrogen ion through a bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase resulting in water and 
5,10-methenyltetrahydrofolic acid.
 
Tetrahydrofolic acid can be metabolized into 5,10-methenyltetrahydrofolic acid  by reacting with a 
5'-phosphoribosyl-a-N-formylglycineamidine through a phosphoribosylglycinamide formyltransferase 2 resulting in water, glycineamideribotide and  5,10-methenyltetrahydrofolic acid. The latter compound can either interact with water through an aminomethyltransferase resulting in a N5-Formyl-THF, or it can interact with a NADPH driven bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase resulting in a NADP and 5,10-Methylene THF.
</description>
      <pathwhiz_id>PW001735</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>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>tRNA Charging 2</name>
      <description>This pathway groups together all E. coli tRNA charging reactions.</description>
      <pathwhiz_id>PW000803</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>tRNA charging</name>
      <description>This pathway groups together all E. coli tRNA charging reactions.</description>
      <pathwhiz_id>PW000799</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>threonine biosynthesis</name>
      <description>The biosynthesis of threonine starts with oxalacetic acid interacting with an L-glutamic acid through an aspartate aminotransferase resulting in a oxoglutaric acid and an L-aspartic acid. The latter compound is then phosphorylated by an ATP driven Aspartate kinase resulting in an a release of an ADP and an L-aspartyl-4-phosphate. This compound interacts with a hydrogen ion through an NADPH driven aspartate semialdehyde dehydrogenase resulting in the release of a phosphate, an NADP and a L-aspartate-semialdehyde.The latter compound interacts with a hydrogen ion through a NADPH driven aspartate kinase / homoserine dehydrogenase resulting in the release of an NADP and a L-homoserine. L-homoserine is phosphorylated through an ATP driven homoserine kinase resulting in the release of an ADP, a hydrogen ion and a O-phosphohomoserine. The latter compound then interacts with a water molecule threonine synthase resulting in the release of a phosphate and an L-threonine. </description>
      <pathwhiz_id>PW000817</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>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>
    <pathway>
      <name>tRNA charging</name>
      <ecocyc_pathway_id>TRNA-CHARGING-PWY</ecocyc_pathway_id>
    </pathway>
    <pathway>
      <name>formylTHF biosynthesis I</name>
      <ecocyc_pathway_id>1CMET2-PWY</ecocyc_pathway_id>
    </pathway>
    <pathway>
      <name>glycine cleavage complex</name>
      <ecocyc_pathway_id>GLYCLEAV-PWY</ecocyc_pathway_id>
    </pathway>
    <pathway>
      <name>superpathway of serine and glycine biosynthesis I</name>
      <ecocyc_pathway_id>GLYSYN-PWY</ecocyc_pathway_id>
    </pathway>
    <pathway>
      <name>folate polyglutamylation</name>
      <ecocyc_pathway_id>PWY-2161</ecocyc_pathway_id>
    </pathway>
    <pathway>
      <name>threonine degradation II</name>
      <ecocyc_pathway_id>THREONINE-DEG2-PWY</ecocyc_pathway_id>
    </pathway>
    <pathway>
      <name>threonine degradation IV</name>
      <ecocyc_pathway_id>PWY-5436</ecocyc_pathway_id>
    </pathway>
    <pathway>
      <name>glutathione biosynthesis</name>
      <ecocyc_pathway_id>GLUTATHIONESYN-PWY</ecocyc_pathway_id>
    </pathway>
    <pathway>
      <name>superpathway of 5-aminoimidazole ribonucleotide biosynthesis</name>
      <ecocyc_pathway_id>PWY-6277</ecocyc_pathway_id>
    </pathway>
    <pathway>
      <name>5-aminoimidazole ribonucleotide biosynthesis I</name>
      <ecocyc_pathway_id>PWY-6121</ecocyc_pathway_id>
    </pathway>
    <pathway>
      <name>5-aminoimidazole ribonucleotide biosynthesis II</name>
      <ecocyc_pathway_id>PWY-6122</ecocyc_pathway_id>
    </pathway>
  </pathways>
  <spectra>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>338</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>339</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>340</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>926</spectrum_id>
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    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1034</spectrum_id>
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    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>2814</spectrum_id>
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    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>28766</spectrum_id>
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    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>30056</spectrum_id>
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    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>30058</spectrum_id>
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    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>30355</spectrum_id>
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    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>30559</spectrum_id>
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    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>30724</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>30755</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>31010</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>31011</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>31909</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>32265</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>32378</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>37305</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>151252</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1050550</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1050552</spectrum_id>
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    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>1050553</spectrum_id>
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    <spectrum>
      <type>Specdb::EiMs</type>
      <spectrum_id>629</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>1094</spectrum_id>
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    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>1153</spectrum_id>
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    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>2467</spectrum_id>
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    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>3160</spectrum_id>
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    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>4726</spectrum_id>
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    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>142330</spectrum_id>
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    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>142331</spectrum_id>
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    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>142332</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>142333</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>142334</spectrum_id>
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    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>142335</spectrum_id>
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    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>142336</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>142337</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>142338</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>142339</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>142340</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>142341</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>142342</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>142343</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>142344</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>142345</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>142346</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>142347</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>142348</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>142349</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>180</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>181</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>182</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2922</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2923</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2924</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2925</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2926</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2927</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2928</spectrum_id>
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    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2929</spectrum_id>
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    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2930</spectrum_id>
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    <spectrum>
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      <spectrum_id>2934</spectrum_id>
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    <spectrum>
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    <spectrum>
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      <spectrum_id>437677</spectrum_id>
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      <spectrum_id>437678</spectrum_id>
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    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>437679</spectrum_id>
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    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>440029</spectrum_id>
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    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>446181</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrTwoD</type>
      <spectrum_id>959</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrTwoD</type>
      <spectrum_id>1152</spectrum_id>
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  </spectra>
  <hmdb_id>HMDB00123</hmdb_id>
  <pubchem_compound_id>750</pubchem_compound_id>
  <chemspider_id>730</chemspider_id>
  <kegg_id>C00037</kegg_id>
  <chebi_id>15428</chebi_id>
  <biocyc_id>GLY</biocyc_id>
  <het_id>GLY_LFZW</het_id>
  <wikipidia>Glycine</wikipidia>
  <foodb_id/>
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    </reference>
    <reference>
      <reference_text>Boneh A, Degani Y, Harari M: Prognostic clues and outcome of early treatment of nonketotic hyperglycinemia. Pediatr Neurol. 1996 Sep;15(2):137-41.</reference_text>
      <pubmed_id>8888048</pubmed_id>
    </reference>
    <reference>
      <reference_text>Dicke JM, Verges D, Kelley LK, Smith CH: Glycine uptake by microvillous and basal plasma membrane vesicles from term human placentae. Placenta. 1993 Jan-Feb;14(1):85-92.</reference_text>
      <pubmed_id>8456092</pubmed_id>
    </reference>
    <reference>
      <reference_text>Prescot AP, de B Frederick B, Wang L, Brown J, Jensen JE, Kaufman MJ, Renshaw PF: In vivo detection of brain glycine with echo-time-averaged (1)H magnetic resonance spectroscopy at 4.0 T. Magn Reson Med. 2006 Mar;55(3):681-6.</reference_text>
      <pubmed_id>16453318</pubmed_id>
    </reference>
    <reference>
      <reference_text>Byard RW, Harrison R, Wells R, Gilbert JD: Glycine toxicity and unexpected intra-operative death.  J Forensic Sci. 2001 Sep;46(5):1244-6.</reference_text>
      <pubmed_id>11569574</pubmed_id>
    </reference>
    <reference>
      <reference_text>Khan SA, Cox IJ, Hamilton G, Thomas HC, Taylor-Robinson SD: In vivo and in vitro nuclear magnetic resonance spectroscopy as a tool for investigating hepatobiliary disease: a review of H and P MRS applications. Liver Int. 2005 Apr;25(2):273-81.</reference_text>
      <pubmed_id>15780050</pubmed_id>
    </reference>
    <reference>
      <reference_text>Van Hove JL, Vande Kerckhove K, Hennermann JB, Mahieu V, Declercq P, Mertens S, De Becker M, Kishnani PS, Jaeken J: Benzoate treatment and the glycine index in nonketotic hyperglycinaemia.  J Inherit Metab Dis. 2005;28(5):651-63.</reference_text>
      <pubmed_id>16151895</pubmed_id>
    </reference>
  </general_references>
  <synthesis_reference> Anslow, Winston K.; King, Harold. Synthesis of glycine. Journal of the Chemical Society (1929), 2163-6.</synthesis_reference>
  <msds_url>http://hmdb.ca/system/metabolites/msds/000/000/084/original/HMDB00123.pdf?1358894433</msds_url>
  <enzymes>
    <enzyme>
      <name>Glycyl-tRNA synthetase alpha subunit</name>
      <uniprot_id>P00960</uniprot_id>
      <uniprot_name>SYGA_ECOLI</uniprot_name>
      <gene_name>glyQ</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P00960.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Glycyl-tRNA synthetase beta subunit</name>
      <uniprot_id>P00961</uniprot_id>
      <uniprot_name>SYGB_ECOLI</uniprot_name>
      <gene_name>glyS</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P00961.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Glutathione synthetase</name>
      <uniprot_id>P04425</uniprot_id>
      <uniprot_name>GSHB_ECOLI</uniprot_name>
      <gene_name>gshB</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P04425.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Aminopeptidase N</name>
      <uniprot_id>P04825</uniprot_id>
      <uniprot_name>AMPN_ECOLI</uniprot_name>
      <gene_name>pepN</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P04825.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Serine hydroxymethyltransferase</name>
      <uniprot_id>P0A825</uniprot_id>
      <uniprot_name>GLYA_ECOLI</uniprot_name>
      <gene_name>glyA</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0A825.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Dihydrolipoyl dehydrogenase</name>
      <uniprot_id>P0A9P0</uniprot_id>
      <uniprot_name>DLDH_ECOLI</uniprot_name>
      <gene_name>lpdA</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0A9P0.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>2-amino-3-ketobutyrate coenzyme A ligase</name>
      <uniprot_id>P0AB77</uniprot_id>
      <uniprot_name>KBL_ECOLI</uniprot_name>
      <gene_name>kbl</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AB77.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Aminoacyl-histidine dipeptidase</name>
      <uniprot_id>P15288</uniprot_id>
      <uniprot_name>PEPD_ECOLI</uniprot_name>
      <gene_name>pepD</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P15288.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Phosphoribosylamine--glycine ligase</name>
      <uniprot_id>P15640</uniprot_id>
      <uniprot_name>PUR2_ECOLI</uniprot_name>
      <gene_name>purD</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P15640.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Aminomethyltransferase</name>
      <uniprot_id>P27248</uniprot_id>
      <uniprot_name>GCST_ECOLI</uniprot_name>
      <gene_name>gcvT</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P27248.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Glycine dehydrogenase [decarboxylating]</name>
      <uniprot_id>P33195</uniprot_id>
      <uniprot_name>GCSP_ECOLI</uniprot_name>
      <gene_name>gcvP</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P33195.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Peptidase B</name>
      <uniprot_id>P37095</uniprot_id>
      <uniprot_name>PEPB_ECOLI</uniprot_name>
      <gene_name>pepB</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P37095.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Cytosol aminopeptidase</name>
      <uniprot_id>P68767</uniprot_id>
      <uniprot_name>AMPA_ECOLI</uniprot_name>
      <gene_name>pepA</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P68767.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Low specificity L-threonine aldolase</name>
      <uniprot_id>P75823</uniprot_id>
      <uniprot_name>LTAE_ECOLI</uniprot_name>
      <gene_name>ltaE</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P75823.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>N-methyl-L-tryptophan oxidase</name>
      <uniprot_id>P40874</uniprot_id>
      <uniprot_name>MTOX_ECOLI</uniprot_name>
      <gene_name>solA</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P40874.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Glycine cleavage system H protein</name>
      <uniprot_id>P0A6T9</uniprot_id>
      <uniprot_name>GCSH_ECOLI</uniprot_name>
      <gene_name>gcvH</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0A6T9.xml</protein_url>
    </enzyme>
  </enzymes>
  <transporters>
    <enzyme>
      <name>Aminopeptidase N</name>
      <uniprot_id>P04825</uniprot_id>
      <uniprot_name>AMPN_ECOLI</uniprot_name>
      <gene_name>pepN</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P04825.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>Uncharacterized amino-acid ABC transporter ATP-binding protein yecC</name>
      <uniprot_id>P37774</uniprot_id>
      <uniprot_name>YECC_ECOLI</uniprot_name>
      <gene_name>yecC</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P37774.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Inner membrane amino-acid ABC transporter permease protein yecS</name>
      <uniprot_id>P0AFT2</uniprot_id>
      <uniprot_name>YECS_ECOLI</uniprot_name>
      <gene_name>yecS</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AFT2.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>D-serine/D-alanine/glycine transporter</name>
      <uniprot_id>P0AAE0</uniprot_id>
      <uniprot_name>CYCA_ECOLI</uniprot_name>
      <gene_name>cycA</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AAE0.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Uncharacterized transporter YeaV</name>
      <uniprot_id>P0ABD1</uniprot_id>
      <uniprot_name>YEAV_ECOLI</uniprot_name>
      <gene_name>yeaV</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0ABD1.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>Outer membrane protein F</name>
      <uniprot_id>P02931</uniprot_id>
      <uniprot_name>OMPF_ECOLI</uniprot_name>
      <gene_name>ompF</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P02931.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Outer membrane protein C</name>
      <uniprot_id>P06996</uniprot_id>
      <uniprot_name>OMPC_ECOLI</uniprot_name>
      <gene_name>ompC</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P06996.xml</protein_url>
    </enzyme>
  </transporters>
  <reactions>
    <reaction_text>Cysteinylglycine + Water &gt; L-Cysteine + Glycine</reaction_text>
    <kegg_reaction_id>R00899</kegg_reaction_id>
    <ecocyc_id>RXN-6622</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>L-Threonine &lt;&gt; Acetaldehyde + Glycine</reaction_text>
    <kegg_reaction_id>R00751</kegg_reaction_id>
    <ecocyc_id>THREONINE-ALDOLASE-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>L-Allothreonine &gt; Acetaldehyde + Glycine</reaction_text>
    <kegg_reaction_id>R06171</kegg_reaction_id>
    <ecocyc_id>LTAA-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Glycine + NAD + Tetrahydrofolic acid &gt; Carbon dioxide + 5,10-Methylene-THF + NADH + Ammonium</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + Glycine + tRNA(Gly) + tRNA(Gly) &lt;&gt; Adenosine monophosphate + Glycyl-tRNA(Gly) + Pyrophosphate + Glycyl-tRNA(Gly)</reaction_text>
    <kegg_reaction_id>R03654</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Water + L-Prolinylglycine &gt; Glycine + L-Proline</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Water + Oxygen + Sarcosine &gt; Formaldehyde + Glycine + Hydrogen peroxide</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>L-Serine + Tetrahydrofolic acid &lt;&gt; Glycine + Water + 5,10-Methylene-THF</reaction_text>
    <kegg_reaction_id>R00945</kegg_reaction_id>
    <ecocyc_id>GLYOHMETRANS-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + gamma-Glutamylcysteine + Glycine &lt;&gt; ADP + Glutathione + Hydrogen ion + Phosphate</reaction_text>
    <kegg_reaction_id>R00497</kegg_reaction_id>
    <ecocyc_id>GLUTATHIONE-SYN-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Acetyl-CoA + Glycine &lt;&gt; L-2-Amino-3-oxobutanoic acid + Coenzyme A</reaction_text>
    <kegg_reaction_id>R00371</kegg_reaction_id>
    <ecocyc_id>AKBLIG-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + Glycine + 5-Phosphoribosylamine &lt;&gt; ADP + Glycineamideribotide + Hydrogen ion + Phosphate</reaction_text>
    <kegg_reaction_id>R04144</kegg_reaction_id>
    <ecocyc_id>GLYRIBONUCSYN-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + gamma-Glutamylcysteine + Glycine &lt;&gt; ADP + Phosphate + Glutathione</reaction_text>
    <kegg_reaction_id>R00497</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Cysteinylglycine + Water &lt;&gt; L-Cysteine + Glycine</reaction_text>
    <kegg_reaction_id>R00899</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>5,10-Methylene-THF + Glycine + Water &lt;&gt; Tetrahydrofolic acid + L-Serine</reaction_text>
    <kegg_reaction_id>R00945</kegg_reaction_id>
    <ecocyc_id>GLYOHMETRANS-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Glycine + Tetrahydrofolic acid + NAD &lt;&gt; 5,10-Methylene-THF + Ammonia + Carbon dioxide + NADH + Hydrogen ion</reaction_text>
    <kegg_reaction_id>R01221</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Glycine + Lipoylprotein &lt;&gt; S-Aminomethyldihydrolipoylprotein + Carbon dioxide</reaction_text>
    <kegg_reaction_id>R03425</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + Glycine + tRNA(Gly) &lt;&gt; Adenosine monophosphate + Pyrophosphate + Glycyl-tRNA(Gly)</reaction_text>
    <kegg_reaction_id>R03654</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + 5-Phosphoribosylamine + Glycine &lt;&gt; ADP + Phosphate + Glycineamideribotide</reaction_text>
    <kegg_reaction_id>R04144</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>R-S-Cysteinylglycine + Water &lt;&gt; S-Substituted L-cysteine + Glycine</reaction_text>
    <kegg_reaction_id>R04951</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>L-Allothreonine &lt;&gt; Glycine + Acetaldehyde</reaction_text>
    <kegg_reaction_id>R06171</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>L-Serine + 5,6,7,8-Tetrahydromethanopterin &lt;&gt; 5,10-Methylenetetrahydromethanopterin + Glycine + Water</reaction_text>
    <kegg_reaction_id>R09099</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>NAD + Glycine + Tetrahydrofolic acid &gt; Hydrogen ion + 5,10-Methylene-THF + Ammonia + Carbon dioxide + NADH</reaction_text>
    <kegg_reaction_id>R01221</kegg_reaction_id>
    <ecocyc_id>GCVMULTI-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Glycine + Acetyl-CoA &lt;&gt; Hydrogen ion + L-2-Amino-3-oxobutanoic acid + Coenzyme A</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>AKBLIG-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Glycine + gamma-Glutamylcysteine + Adenosine triphosphate &gt; Hydrogen ion + Glutathione + Phosphate + ADP</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>GLUTATHIONE-SYN-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>L-&lt;i&gt;threo&lt;/i&gt;-3-phenylserine  benzaldehyde + Glycine</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>PHENYLSERINE-ALDOLASE-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>DL-allothreonine &lt;&gt; Acetaldehyde + Glycine</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>RXN0-5234</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>4-Hydroxy-L-threonine &lt;&gt; Glycolaldehyde + Glycine</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>RXN0-6563</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>gly-met + Water &gt; Glycine + L-Methionine</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>RXN0-6974</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>ala-gly + Water &gt; L-Alanine + Glycine</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>RXN0-6977</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>gly-asn + Water &gt; Glycine + L-Asparagine</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>RXN0-6982</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>gly-gln + Water &gt; Glycine + L-Glutamine</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>RXN0-6983</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>glycyl-L-glutamate + Water &gt; Glycine + L-Glutamate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>RXN0-6984</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>gly-asp + Water &gt; Glycine + L-Aspartic acid</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>RXN0-6987</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>glycylproline + Water &gt; Glycine + L-Proline</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>RXN0-6988</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>L-Threonine &gt; Acetaldehyde + Glycine</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>THREONINE-ALDOLASE-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Glycine + H-protein-lipoyllysine &gt; H-protein-S-aminomethyldihydrolipoyllysine + Carbon dioxide</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>5,10-Methylene-THF + Glycine + Water &gt; Tetrahydrofolic acid + L-Serine</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + gamma-Glutamylcysteine + Glycine &gt; ADP + Inorganic phosphate + Glutathione</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Acetyl-CoA + Glycine &gt; CoA + L-2-Amino-3-oxobutanoic acid</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + 5-Phosphoribosylamine + Glycine &gt; ADP + Inorganic phosphate + 5'-Phospho-ribosylglycinamide</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + Glycine + tRNA(Gly) &gt; Adenosine monophosphate + Pyrophosphate + glycyl-tRNA(Gly)</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Tetrahydrofolic acid + L-Serine + Tetrahydrofolic acid + L-Serine &lt;&gt; 5,10-Methylene-THF + Glycine + Water + 5,10-Methylene-THF</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id>PW_R002544</pw_reaction_id>
    <reaction_text>L-Alanine + Glyoxylic acid + L-Alanine &lt;&gt; Glycine + Pyruvic acid</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id>PW_R002587</pw_reaction_id>
    <reaction_text>Glycine + Adenosine triphosphate + Hydrogen ion + tRNA(gly) &gt; Adenosine monophosphate + Pyrophosphate + Glycyl-tRNA(Gly)</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id>PW_R002827</pw_reaction_id>
    <reaction_text>gamma-Glutamylcysteine + Glycine + Adenosine triphosphate &gt; Hydrogen ion + Phosphate + Adenosine diphosphate + Glutathione + ADP</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id>PW_R003053</pw_reaction_id>
    <reaction_text>5-Phosphoribosylamine + Glycine + Adenosine triphosphate + 5-Phosphoribosylamine &gt; N1-(5-phospho-β-D-ribosyl)glycinamide + Phosphate + Adenosine diphosphate + Hydrogen ion + ADP</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id>PW_R003411</pw_reaction_id>
    <reaction_text>L-2-Amino-3-oxobutanoic acid + Coenzyme A &gt; Acetyl-CoA + Glycine</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id>PW_R005169</pw_reaction_id>
    <reaction_text>Adenosine triphosphate + Glycine + tRNA(Gly) &lt;&gt; Adenosine monophosphate + Glycyl-tRNA(Gly) + Pyrophosphate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + gamma-Glutamylcysteine + Glycine &lt;&gt; ADP + Glutathione + Hydrogen ion + Phosphate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>L-Threonine &lt;&gt; Acetaldehyde + Glycine</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>L-Allothreonine &gt; Acetaldehyde + Glycine</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Cysteinylglycine + Water &gt; L-Cysteine + Glycine</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + Glycine + 5 5-Phosphoribosylamine &lt;&gt; ADP + Glycineamideribotide + Hydrogen ion + Phosphate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Glycine + Lipoylprotein &lt;&gt; S-Aminomethyldihydrolipoylprotein + Carbon dioxide</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Glycine + Tetrahydrofolic acid + NAD &lt;&gt;5 5,10-Methylene-THF + Ammonia + Carbon dioxide + NADH + Hydrogen ion</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + Glycine + tRNA(Gly) &lt;&gt; Adenosine monophosphate + Glycyl-tRNA(Gly) + Pyrophosphate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>L-Allothreonine &gt; Acetaldehyde + Glycine</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Glycine + Tetrahydrofolic acid + NAD &lt;&gt;5 5,10-Methylene-THF + Ammonia + Carbon dioxide + NADH + Hydrogen ion</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
  </reactions>
  <concentrations>
    <growth_media>48 mM Na2HPO4, 22 mM KH2PO4, 10 mM NaCl, 45 mM (NH4)2SO4, supplemented with 1 mM MgSO4, 1 mg/l thiamine·HCl, 5.6 mg/l CaCl2, 8 mg/l FeCl3, 1 mg/l MnCl2·4H2O, 1.7 mg/l ZnCl2, 0.43 mg/l CuCl2·2H2O, 0.6 mg/l CoCl2·2H2O and 0.6 mg/l Na2MoO4·2H2O.  4 g/L Gluco</growth_media>
    <growth_system>Bioreactor, pH controlled, O2 and CO2 controlled, dilution rate: 0.2/h</growth_system>
    <concentration>318.0</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>1272000</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>235.33</concentration>
    <concentration_units>uM</concentration_units>
    <internal>true</internal>
    <error>14.15</error>
    <temperature>37 oC</temperature>
    <strain>BL21 DE3</strain>
    <growth_status>Stationary phase cultures (overnight culture)</growth_status>
    <molecules>941333</molecules>
    <molecules_error>56616</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>
