<?xml version="1.0" encoding="UTF-8"?>
<compound>
  <version>2.0</version>
  <creation_date>2012-05-31 13:50:04 -0600</creation_date>
  <update_date>2015-09-17 16:24:07 -0600</update_date>
  <accession>ECMDB01333</accession>
  <m2m_id>M2MDB000341</m2m_id>
  <name>Manganese</name>
  <description>Manganese is an essential trace nutrient in all forms of life.[18] The classes of enzymes that have manganese cofactors are very broad and include oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases, lectins, and integrins. The best known manganese-containing polypeptides may be arginase, the diphtheria toxin, and Mn-containing superoxide dismutase (Mn-SOD). The Mn-SOD enzyme is probably one of the most ancient, for nearly all organisms living in the presence of oxygen use it to deal with the toxic effects of superoxide, formed from the 1-electron reduction of dioxygen. (Wikipedia)</description>
  <synonyms>
    <synonym>Manganese</synonym>
    <synonym>Manganese (II) ion</synonym>
    <synonym>Manganese ion</synonym>
    <synonym>Mn(II)</synonym>
    <synonym>MN++</synonym>
    <synonym>MN+2</synonym>
    <synonym>Mn&lt;SUP&gt;++&lt;/SUP&gt;</synonym>
    <synonym>Mn&lt;SUP&gt;+2&lt;/SUP&gt;</synonym>
  </synonyms>
  <chemical_formula>Mn</chemical_formula>
  <average_molecular_weight>54.938</average_molecular_weight>
  <monisotopic_moleculate_weight>54.938049636</monisotopic_moleculate_weight>
  <iupac_name>manganese(2+) ion</iupac_name>
  <traditional_iupac>manganese(2+) ion</traditional_iupac>
  <cas_registry_number>7439-96-5</cas_registry_number>
  <smiles>[Mn++]</smiles>
  <inchi>InChI=1S/Mn/q+2</inchi>
  <inchikey>WAEMQWOKJMHJLA-UHFFFAOYSA-N</inchikey>
  <state>Solid</state>
  <cellular_locations>
    <cellular_location>Cytosol</cellular_location>
    <cellular_location>Extra-organism</cellular_location>
    <cellular_location>Periplasm</cellular_location>
  </cellular_locations>
  <predicted_properties>
  </predicted_properties>
  <experimental_properties>
    <property>
      <kind>melting_point</kind>
      <value>1244 oC</value>
    </property>
  </experimental_properties>
  <property>
    <kind>logp</kind>
    <value>-0.16</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>pka_strongest_acidic</kind>
    <value>3.09</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>iupac</kind>
    <value>manganese(2+) ion</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>average_mass</kind>
    <value>54.938</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>mono_mass</kind>
    <value>54.938049636</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>smiles</kind>
    <value>[Mn++]</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>formula</kind>
    <value>Mn</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>inchi</kind>
    <value>InChI=1S/Mn/q+2</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>inchikey</kind>
    <value>WAEMQWOKJMHJLA-UHFFFAOYSA-N</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>polar_surface_area</kind>
    <value>0</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>refractivity</kind>
    <value>0</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>polarizability</kind>
    <value>1.78</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>rotatable_bond_count</kind>
    <value>0</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>acceptor_count</kind>
    <value>0</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>donor_count</kind>
    <value>0</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>physiological_charge</kind>
    <value>2</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>formal_charge</kind>
    <value>2</value>
    <source>ChemAxon</source>
  </property>
  <pathways>
    <pathway>
      <name>ABC transporters</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec02010</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>Two-component system</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec02020</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>Porphyrin metabolism</name>
      <description>The metabolism of porphyrin begins with with glutamic acid being processed by an ATP-driven glutamyl-tRNA synthetase by interacting with hydrogen ion and tRNA(Glu), resulting in amo, pyrophosphate and L-glutamyl-tRNA(Glu) Glutamic acid. Glutamic acid can be obtained as a result of L-glutamate metabolism pathway, glutamate / aspartate : H+ symporter GltP, glutamate:sodium symporter or a glutamate / aspartate ABC transporter .
L-glutamyl-tRNA(Glu) Glutamic acid interacts with a NADPH glutamyl-tRNA reductase resulting in a NADP, a tRNA(Glu) and a (S)-4-amino-5-oxopentanoate. 
This compound interacts with a glutamate-1-semialdehyde aminotransferase resulting a 5-aminolevulinic acid. This compound interacts with a porphobilinogen synthase resulting in a hydrogen ion, water and porphobilinogen. The latter compound interacts with water resulting in hydroxymethylbilane synthase resulting in ammonium, and hydroxymethylbilane. 
 Hydroxymethylbilane can either be dehydrated to produce uroporphyrinogen I or interact with a uroporphyrinogen III synthase resulting in a water molecule and a uroporphyrinogen III.
Uroporphyrinogen I interacts with hydrogen ion through a uroporphyrinogen decarboxylase resulting in a carbon dioxide and a coproporphyrinogen I
Uroporphyrinogen III can be metabolized into precorrin by interacting with a S-adenosylmethionine through a siroheme synthase resulting in hydrogen ion, an s-adenosylhomocysteine and a precorrin-1. On the other hand, Uroporphyrinogen III interacts with hydrogen ion through a uroporphyrinogen decarboxylase resulting in a carbon dioxide and a Coproporphyrinogen III.
Precorrin-1 reacts with a S-adenosylmethionine through a siroheme synthase resulting in a S-adenosylhomocysteine and a Precorrin-2. The latter compound is processed by a NAD dependent uroporphyrin III C-methyltransferase [multifunctional] resulting in a NADH and a sirohydrochlorin. This compound then interacts with Fe 2+ 
uroporphyrin III C-methyltransferase [multifunctional] resulting in a hydrogen ion and a siroheme. The siroheme is then processed in sulfur metabolism pathway.
Uroporphyrinogen III can be processed in anaerobic or aerobic condition. 
Anaerobic:
Uroporphyrinogen III interacts with an oxygen molecule, a hydrogen ion through a coproporphyrinogen III oxidase resulting in water, carbon dioxide and protoporphyrinogen IX. The latter compound then interacts with an 3 oxygen molecule through a protoporphyrinogen oxidase resulting in 3 hydrogen peroxide and a Protoporphyrin IX
Aerobic:
Uroporphyrinogen III reacts with S-adenosylmethionine through a coproporphyrinogen III dehydrogenase resulting in carbon dioxide, 5-deoxyadenosine, L-methionine and protoporphyrinogen IX. The latter compound interacts with a meanquinone through a protoporphyrinogen oxidase resulting in protoporphyrin IX.

The protoporphyrin IX interacts with Fe 2+ through a ferrochelatase resulting in a hydrogen ion and a ferroheme b. The ferroheme b can either be incorporated into the oxidative phosphorylation as a cofactor of the enzymes involved in that pathway or it can interact with hydrogen peroxide through a catalase HPII resulting in a heme D. Heme D can then be incorporated into the oxidative phosphyrlation pathway as a cofactor of the enzymes involved in that pathway. Ferroheme b can also interact with water and a farnesyl pyrophosphate through a heme O synthase resulting in a release of pyrophosphate and heme O. Heme O is then incorporated into the Oxidative phosphorylation pathway.
</description>
      <pathwhiz_id>PW000936</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>Secondary Metabolites: Ubiquinol biosynthesis</name>
      <description>The biosynthesis of ubiquinol starts the interaction of 4-hydroxybenzoic acid interacting with an octaprenyl diphosphate. The former compound comes from the chorismate interacting with a chorismate lyase resulting in the release of a pyruvic acid and a 4-hydroxybenzoic acid. On the other hand, the latter compound, octaprenyl diphosphate is the result of a farnesyl pyrophosphate interacting with an isopentenyl pyrophosphate through an octaprenyl diphosphate synthase resulting in the release of a pyrophosphate and an octaprenyl diphosphate.
The 4-hydroxybenzoic acid interacts with octaprenyl diphosphate through a 4-hydroxybenzoate octaprenyltransferase resulting in the release of a pyrophosphate and a 3-octaprenyl-4-hydroxybenzoate. The latter compound then interacts with a hydrogen ion through a 3-octaprenyl-4-hydroxybenzoate carboxy-lyase resulting in the release of a carbon dioxide and a 2-octaprenylphenol. The latter compound interacts with an oxygen molecule and a hydrogen ion through a NADPH driven 2-octaprenylphenol hydroxylase resulting in a NADP, a water molecule and  a 2-octaprenyl-6-hydroxyphenol.
The 2-octaprenyl-6-hydroxyphenol interacts with an S-adenosylmethionine through a bifunctional 3-demethylubiquinone-8 3-O-methyltransferase and 2-octaprenyl-6-hydroxyphenol methylase resulting in the release of a hydrogen ion, an s-adenosylhomocysteine and a 2-methoxy-6-(all-trans-octaprenyl)phenol. The latter compound then interacts with an oxygen molecule and a hydrogen ion through a NADPH driven 2-octaprenyl-6-methoxyphenol hydroxylase resulting in a NADP, a water molecule and a 2-methoxy-6-all trans-octaprenyl-2-methoxy-1,4-benzoquinol.
The latter compound interacts with a S-adenosylmethionine through a bifunctional 2-octaprenyl-6-methoxy-1,4-benzoquinone methylase and S-adenosylmethionine:2-DMK methyltransferase resulting in a s-adenosylhomocysteine, a hydrogen ion and a 6-methoxy-3-methyl-2-all-trans-octaprenyl-1,4-benzoquinol. The 6-methoxy-3-methyl-2-all-trans-octaprenyl-1,4-benzoquinol. interacts with a reduced acceptor, an oxygen molecule through a 2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinone hydroxylase resulting in the release of a water molecule, an oxidized electron acceptor and a 3-demethylubiquinol-8. The latter compound then interacts with a S-adenosylmethionine through a bifunctional 3-demethylubiquinone-8 3-O-methyltransferase and 2-octaprenyl-6-hydroxyphenol methylase resulting in a hydrogen ion, a S-adenosylhomocysteine and a ubiquinol 8.
</description>
      <pathwhiz_id>PW000981</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>Secondary metabolites: isoprenoid biosynthesis (nonmevalonate pathway)</name>
      <description>The biosynthesis of isoprenoids starts with a D-glyceraldehyde 3-phosphate interacting with a hydrogen ion through a 1-deoxyxylulose-5-phosphate synthase resulting in a carbon dioxide and 1-Deoxy-D-xylulose. The latter compound then interacts with a hydrogen ion through a NADPH driven 1-deoxy-D-xylulose 5-phosphate reductoisomerase resulting in a NADP and a 2-C-methyl-D-erythritol 4-phosphate. The latter compound then interacts with a cytidine triphosphate and a hydrogen ion through a 4-diphosphocytidyl-2C-methyl-D-erythritol synthase resulting in a pyrophosphate and a 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. The latter compound is then phosphorylated through an ATP driven 
4-diphosphocytidyl-2-C-methylerythritol kinase resulting in a release of an ADP, a hydrogen ion and a 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. The latter compound then interacts with a 
2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase  resulting in the release of a 2-C-methyl-D-erythritol-2,4-cyclodiphosphate resulting in the release of a cytidine monophosphate and 2-C-methyl-D-erythritol-2,4-cyclodiphosphate. The latter compound then interacts with a reduced flavodoxin through a 
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase  resulting in the release of a water molecule, a hydrogen ion, an oxidized flavodoxin and a 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. 
The compound 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate can interact with an NADPH,a hydrogen ion through a 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase  resulting in a NADP, a water molecule and either a Dimethylallylpyrophosphate or a Isopentenyl pyrophosphate. These two last compounds can be are isomers that can be produced through a isopentenyl diphosphate isomerase.and then get incorporated into the methylerythritol phosphate and polyisoprenoid biosynthesis pathway</description>
      <pathwhiz_id>PW000975</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>Secondary metabolites: methylerythritol phosphate and polyisoprenoid biosynthesis</name>
      <description>The biosynthesis of isoprenoids starts with a D-glyceraldehyde 3-phosphate interacting with a hydrogen ion through a 1-deoxyxylulose-5-phosphate synthase resulting in a carbon dioxide and 1-Deoxy-D-xylulose. The latter compound then interacts with a hydrogen ion through a NADPH driven 1-deoxy-D-xylulose 5-phosphate reductoisomerase resulting in a NADP and a 2-C-methyl-D-erythritol 4-phosphate. The latter compound then interacts with a cytidine triphosphate and a hydrogen ion through a 4-diphosphocytidyl-2C-methyl-D-erythritol synthase resulting in a pyrophosphate and a 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. The latter compound is then phosphorylated through an ATP driven 
4-diphosphocytidyl-2-C-methylerythritol kinase resulting in a release of an ADP, a hydrogen ion and a 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. The latter compound then interacts with a 
2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase  resulting in the release of a 2-C-methyl-D-erythritol-2,4-cyclodiphosphate resulting in the release of a cytidine monophosphate and 2-C-methyl-D-erythritol-2,4-cyclodiphosphate. The latter compound then interacts with a reduced flavodoxin through a 
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase  resulting in the release of a water molecule, a hydrogen ion, an oxidized flavodoxin and a 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. 
The compound 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate can interact with an NADPH,a hydrogen ion through a 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase  resulting in a NADP, a water molecule and either a Dimethylallylpyrophosphate or a Isopentenyl pyrophosphate. These two last compounds can be are isomers that can be produced through a isopentenyl diphosphate isomerase.
Dimethylallylpyrophosphate interacts with the isopentenyl pyrophosphate through a geranyl diphosphate synthase / farnesyl diphosphate synthase resulting in a pyrophosphate and a geranyl--PP. The latter compound interacts with a Isopentenyl pyrophosphate through a geranyl diphosphate synthase / farnesyl diphosphate synthase resulting in the release of a pyrophosphate and a farnesyl pyrophosphate. The latter compound interacts with isopentenyl pyrophosphate either through a undecaprenyl diphosphate synthase resulting in a release of a pyrophosphate and a di-trans,octa-cis-undecaprenyl diphosphate or through a octaprenyl diphosphate synthase resulting in a pyrophosphate and an octaprenyl diphosphate</description>
      <pathwhiz_id>PW000958</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>peptidoglycan biosynthesis I</name>
      <description>Peptidoglycan is a net-like polymer which surrounds the cytoplasmic membrane of most bacteria and functions to maintain cell shape and prevent rupture due to the internal turgor.In E. coli K-12, the peptidoglycan consists of glycan strands of alternating subunits of N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid (MurNAc) which are cross-linked by short peptides. The pathway for constructing this net involves two cell compartments: cytoplasm and periplasmic space. 
The pathway starts with a beta-D-fructofuranose going through a mannose  PTS permease, phosphorylating the compund and producing a beta-D-fructofuranose 6 phosphate. This compound can be obtained from the glycolysis and pyruvate dehydrogenase or from an isomerization reaction of Beta-D-glucose 6-phosphate through a glucose-6-phosphate isomerase.The compound Beta-D-fructofuranose 6 phosphate and L-Glutamine react with a glucosamine fructose-6-phosphate aminotransferase, thus producing a glucosamine 6-phosphate  and a l-glutamic acid. The glucosamine 6-phosphate interacts with phosphoglucosamine mutase in a reversible reaction producing glucosamine-1P. Glucosamine-1p and acetyl coa undergo acetylation throuhg a bifunctional protein glmU releasing Coa and a hydrogen ion and producing a N-acetyl-glucosamine 1-phosphate. Glmu, being a bifunctional protein, follows catalyze the interaction of N-acetyl-glucosamine 1-phosphate, hydrogen ion and UTP into UDP-N-acetylglucosamine and pyrophosphate. UDP-N-acetylglucosamine then interacts with phosphoenolpyruvic acid and a UDP-N acetylglucosamine 1- carboxyvinyltransferase realeasing a phosphate and the compound UDP-N-acetyl-alpha-D-glucosamine-enolpyruvate. This compound undergoes a NADPH dependent reduction producing a UDP-N-acetyl-alpha-D-muramate through a UDP-N-acetylenolpyruvoylglucosamine reductase. UDP-N-acetyl-alpha-D-muramate and L-alanine react in an ATP-mediated ligation through a UDP-N-acetylmuramate-alanine ligase releasing an ADP, hydrogen ion, a phosphate and a UDP-N-acetylmuramoyl-L-alanine. This compound interacts with D-glutamic acid and ATP through  UDP-N-acetylmuramoylalanine-D-glutamate ligase releasing ADP, A phosphate and UDP-N-acetylmuramoyl-L-alanyl-D-glutamate. The latter compound then interacts with meso-diaminopimelate in an ATP mediated ligation through a UDP-N-acetylmuramoylalanine-D-glutamate-2,6-diaminopimelate ligase resulting in ADP, phosphate, hydrogen ion and UDP-N-Acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diaminopimelate. This compound in turn with D-alanyl-D-alanine react in an ATP-mediated ligation through UDP-N-Acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase to produce UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gama-D-glutamyl-meso-2,6-diaminopimeloyl-Dalanyl-D-alanine and hydrogen ion, ADP, phosphate. UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gama-D-glutamyl-meso-2,6-diaminopimeloyl-Dalanyl-D-alanine interacts with di-trans,octa-cis-undecaprenyl phosphate through a phospho-N-acetylmuramoyl-pentapeptide-transferase, resulting in UMP and Undecaprenyl-diphospho-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine which in turn reacts with a UDP-N-acetylglucosamine through a N-acetylglucosaminyl transferase to produce a hydrogen, UDP and ditrans,octacis-undecaprenyldiphospho-N-acetyl-(N-acetylglucosaminyl)muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine. This compound ends the cytoplasmic part of the pathway. ditrans,octacis-undecaprenyldiphospho-N-acetyl-(N-acetylglucosaminyl)muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine is transported through a lipi II flippase. Once in the periplasmic space, the compound reacts with a penicillin binding protein 1A prodducing a peptidoglycan dimer, a hydrogen ion, and UDP. The peptidoglycan dimer then reacts with a penicillin binding protein 1B  producing a peptidoglycan with D,D, cross-links and a D-alanine. 
</description>
      <pathwhiz_id>PW000906</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>Secondary Metabolites: Ubiquinol biosynthesis 2</name>
      <description>The biosynthesis of ubiquinol starts the interaction of 4-hydroxybenzoic acid interacting with an octaprenyl diphosphate. The former compound comes from the chorismate interacting with a chorismate lyase resulting in the release of a pyruvic acid and a 4-hydroxybenzoic acid. On the other hand, the latter compound, octaprenyl diphosphate is the result of a farnesyl pyrophosphate interacting with an isopentenyl pyrophosphate through an octaprenyl diphosphate synthase resulting in the release of a pyrophosphate and an octaprenyl diphosphate. The 4-hydroxybenzoic acid interacts with octaprenyl diphosphate through a 4-hydroxybenzoate octaprenyltransferase resulting in the release of a pyrophosphate and a 3-octaprenyl-4-hydroxybenzoate. The latter compound then interacts with a hydrogen ion through a 3-octaprenyl-4-hydroxybenzoate carboxy-lyase resulting in the release of a carbon dioxide and a 2-octaprenylphenol. The latter compound interacts with an oxygen molecule and a hydrogen ion through a NADPH driven 2-octaprenylphenol hydroxylase resulting in a NADP, a water molecule and a 2-octaprenyl-6-hydroxyphenol. The 2-octaprenyl-6-hydroxyphenol interacts with an S-adenosylmethionine through a bifunctional 3-demethylubiquinone-8 3-O-methyltransferase and 2-octaprenyl-6-hydroxyphenol methylase resulting in the release of a hydrogen ion, an s-adenosylhomocysteine and a 2-methoxy-6-(all-trans-octaprenyl)phenol. The latter compound then interacts with an oxygen molecule and a hydrogen ion through a NADPH driven 2-octaprenyl-6-methoxyphenol hydroxylase resulting in a NADP, a water molecule and a 2-methoxy-6-all trans-octaprenyl-2-methoxy-1,4-benzoquinol. The latter compound interacts with a S-adenosylmethionine through a bifunctional 2-octaprenyl-6-methoxy-1,4-benzoquinone methylase and S-adenosylmethionine:2-DMK methyltransferase resulting in a s-adenosylhomocysteine, a hydrogen ion and a 6-methoxy-3-methyl-2-all-trans-octaprenyl-1,4-benzoquinol. The 6-methoxy-3-methyl-2-all-trans-octaprenyl-1,4-benzoquinol. interacts with a reduced acceptor, an oxygen molecule through a 2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinone hydroxylase resulting in the release of a water molecule, an oxidized electron acceptor and a 3-demethylubiquinol-8. The latter compound then interacts with a S-adenosylmethionine through a bifunctional 3-demethylubiquinone-8 3-O-methyltransferase and 2-octaprenyl-6-hydroxyphenol methylase resulting in a hydrogen ion, a S-adenosylhomocysteine and a ubiquinol 8.</description>
      <pathwhiz_id>PW002036</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>peptidoglycan biosynthesis I 2</name>
      <description>Peptidoglycan is a net-like polymer which surrounds the cytoplasmic membrane of most bacteria and functions to maintain cell shape and prevent rupture due to the internal turgor.In E. coli K-12, the peptidoglycan consists of glycan strands of alternating subunits of N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid (MurNAc) which are cross-linked by short peptides. The pathway for constructing this net involves two cell compartments: cytoplasm and periplasmic space. The pathway starts with a beta-D-fructofuranose going through a mannose PTS permease, phosphorylating the compund and producing a beta-D-fructofuranose 6 phosphate. This compound can be obtained from the glycolysis and pyruvate dehydrogenase or from an isomerization reaction of Beta-D-glucose 6-phosphate through a glucose-6-phosphate isomerase.The compound Beta-D-fructofuranose 6 phosphate and L-Glutamine react with a glucosamine fructose-6-phosphate aminotransferase, thus producing a glucosamine 6-phosphate and a l-glutamic acid. The glucosamine 6-phosphate interacts with phosphoglucosamine mutase in a reversible reaction producing glucosamine-1P. Glucosamine-1p and acetyl coa undergo acetylation throuhg a bifunctional protein glmU releasing Coa and a hydrogen ion and producing a N-acetyl-glucosamine 1-phosphate. Glmu, being a bifunctional protein, follows catalyze the interaction of N-acetyl-glucosamine 1-phosphate, hydrogen ion and UTP into UDP-N-acetylglucosamine and pyrophosphate. UDP-N-acetylglucosamine then interacts with phosphoenolpyruvic acid and a UDP-N acetylglucosamine 1- carboxyvinyltransferase realeasing a phosphate and the compound UDP-N-acetyl-alpha-D-glucosamine-enolpyruvate. This compound undergoes a NADPH dependent reduction producing a UDP-N-acetyl-alpha-D-muramate through a UDP-N-acetylenolpyruvoylglucosamine reductase. UDP-N-acetyl-alpha-D-muramate and L-alanine react in an ATP-mediated ligation through a UDP-N-acetylmuramate-alanine ligase releasing an ADP, hydrogen ion, a phosphate and a UDP-N-acetylmuramoyl-L-alanine. This compound interacts with D-glutamic acid and ATP through UDP-N-acetylmuramoylalanine-D-glutamate ligase releasing ADP, A phosphate and UDP-N-acetylmuramoyl-L-alanyl-D-glutamate. The latter compound then interacts with meso-diaminopimelate in an ATP mediated ligation through a UDP-N-acetylmuramoylalanine-D-glutamate-2,6-diaminopimelate ligase resulting in ADP, phosphate, hydrogen ion and UDP-N-Acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diaminopimelate. This compound in turn with D-alanyl-D-alanine react in an ATP-mediated ligation through UDP-N-Acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase to produce UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gama-D-glutamyl-meso-2,6-diaminopimeloyl-Dalanyl-D-alanine and hydrogen ion, ADP, phosphate. UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gama-D-glutamyl-meso-2,6-diaminopimeloyl-Dalanyl-D-alanine interacts with di-trans,octa-cis-undecaprenyl phosphate through a phospho-N-acetylmuramoyl-pentapeptide-transferase, resulting in UMP and N-Acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol which in turn reacts with a UDP-N-acetylglucosamine through a N-acetylglucosaminyl transferase to produce a hydrogen, UDP and Undecaprenyl-diphospho-N-acetylmuramoyl-(N-acetylglucosamine)-L-alanyl-D-glutaminyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine. This compound ends the cytoplasmic part of the pathway. Undecaprenyl-diphospho-N-acetylmuramoyl-(N-acetylglucosamine)-L-alanyl-D-glutaminyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine is transported through a lipi II flippase. Once in the periplasmic space, the compound reacts with a penicillin binding protein 1A prodducing a peptidoglycan dimer, a hydrogen ion, and UDP. The peptidoglycan dimer then reacts with a penicillin binding protein 1B producing a peptidoglycan with D,D, cross-links and a D-alanine.</description>
      <pathwhiz_id>PW002062</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
  </pathways>
  <spectra>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>23459</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>23460</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>23461</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>30257</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>30258</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>30259</spectrum_id>
    </spectrum>
  </spectra>
  <hmdb_id>HMDB01333</hmdb_id>
  <pubchem_compound_id>23930</pubchem_compound_id>
  <chemspider_id>25916</chemspider_id>
  <kegg_id>C00034</kegg_id>
  <chebi_id>18291</chebi_id>
  <biocyc_id>MN+2</biocyc_id>
  <het_id>MN</het_id>
  <wikipidia>Manganese</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>Ikeda S, Sera Y, Yoshida M, Ohshiro H, Uchino S, Oka Y, Lee KJ, Kotera A: Manganese deposits in patients with biliary atresia after hepatic porto-enterostomy. J Pediatr Surg. 2000 Mar;35(3):450-3.</reference_text>
      <pubmed_id>10726687</pubmed_id>
    </reference>
    <reference>
      <reference_text>Greger JL: Nutrition versus toxicology of manganese in humans: evaluation of potential biomarkers. Neurotoxicology. 1999 Apr-Jun;20(2-3):205-12.</reference_text>
      <pubmed_id>10385884</pubmed_id>
    </reference>
    <reference>
      <reference_text>Lander F, Kristiansen J, Lauritsen JM: Manganese exposure in foundry furnacemen and scrap recycling workers.  Int Arch Occup Environ Health. 1999 Nov;72(8):546-50.</reference_text>
      <pubmed_id>10592008</pubmed_id>
    </reference>
    <reference>
      <reference_text>Mizoguchi N, Nishimura Y, Ono H, Sakura N: Manganese elevations in blood of children with congenital portosystemic shunts. Eur J Pediatr. 2001 Apr;160(4):247-50.</reference_text>
      <pubmed_id>11317649</pubmed_id>
    </reference>
    <reference>
      <reference_text>Woolf A, Wright R, Amarasiriwardena C, Bellinger D: A child with chronic manganese exposure from drinking water.  Environ Health Perspect. 2002 Jun;110(6):613-6.</reference_text>
      <pubmed_id>12055054</pubmed_id>
    </reference>
    <reference>
      <reference_text>Ikeda S, Yamaguchi Y, Sera Y, Ohshiro H, Uchino S, Yamashita Y, Ogawa M: Manganese deposition in the globus pallidus in patients with biliary atresia. Transplantation. 2000 Jun 15;69(11):2339-43.</reference_text>
      <pubmed_id>10868637</pubmed_id>
    </reference>
    <reference>
      <reference_text>Wardle CA, Forbes A, Roberts NB, Jawhari AV, Shenkin A: Hypermanganesemia in long-term intravenous nutrition and chronic liver disease. JPEN J Parenter Enteral Nutr. 1999 Nov-Dec;23(6):350-5.</reference_text>
      <pubmed_id>10574484</pubmed_id>
    </reference>
    <reference>
      <reference_text>Mergler D, Baldwin M, Belanger S, Larribe F, Beuter A, Bowler R, Panisset M, Edwards R, de Geoffroy A, Sassine MP, Hudnell K: Manganese neurotoxicity, a continuum of dysfunction: results from a community based study. Neurotoxicology. 1999 Apr-Jun;20(2-3):327-42.</reference_text>
      <pubmed_id>10385894</pubmed_id>
    </reference>
    <reference>
      <reference_text>Butterworth RF: Hepatic encephalopathy.  Alcohol Res Health. 2003;27(3):240-6.</reference_text>
      <pubmed_id>15535452</pubmed_id>
    </reference>
    <reference>
      <reference_text>Herynek V, Babis M, Trunecka P, Filip K, Vymazal J, Dezortova M, Hajek M: Chronic liver disease: relaxometry in the brain after liver transplantation. MAGMA. 2001 Mar;12(1):10-5.</reference_text>
      <pubmed_id>11255087</pubmed_id>
    </reference>
    <reference>
      <reference_text>Miranda M, Caballero L: [Chronic hepatic encephalopathy: the role of high serum manganese levels and its relation with basal ganglia lesions in nuclear magnetic resonance of the brain. Clinical case] Rev Med Chil. 2001 Sep;129(9):1051-5.</reference_text>
      <pubmed_id>11725469</pubmed_id>
    </reference>
    <reference>
      <reference_text>Barceloux DG: Manganese.  J Toxicol Clin Toxicol. 1999;37(2):293-307.</reference_text>
      <pubmed_id>10382563</pubmed_id>
    </reference>
    <reference>
      <reference_text>Bader M, Dietz MC, Ihrig A, Triebig G: Biomonitoring of manganese in blood, urine and axillary hair following low-dose exposure during the manufacture of dry cell batteries. Int Arch Occup Environ Health. 1999 Nov;72(8):521-7.</reference_text>
      <pubmed_id>10592004</pubmed_id>
    </reference>
    <reference>
      <reference_text>Kao HJ, Chen WH, Liu JS: Rapid progression of parkinsonism associated with an increase of blood manganese. Kaohsiung J Med Sci. 1999 May;15(5):297-301.</reference_text>
      <pubmed_id>10375873</pubmed_id>
    </reference>
    <reference>
      <reference_text>Melo TM, Larsen C, White LR, Aasly J, Sjobakk TE, Flaten TP, Sonnewald U, Syversen T: Manganese, copper, and zinc in cerebrospinal fluid from patients with multiple sclerosis. Biol Trace Elem Res. 2003 Summer;93(1-3):1-8.</reference_text>
      <pubmed_id>12835484</pubmed_id>
    </reference>
    <reference>
      <reference_text>Lees-Haley PR, Rohling ML, Langhinrichsen-Rohling J: A meta-analysis of the neuropsychological effects of occupational exposure to manganese. Clin Neuropsychol. 2006 Feb;20(1):90-107.</reference_text>
      <pubmed_id>16393922</pubmed_id>
    </reference>
    <reference>
      <reference_text>Sadek AH, Rauch R, Schulz PE: Parkinsonism due to manganism in a welder.  Int J Toxicol. 2003 Sep-Oct;22(5):393-401.</reference_text>
      <pubmed_id>14555414</pubmed_id>
    </reference>
    <reference>
      <reference_text>Wang X, Li GJ, Zheng W: Upregulation of DMT1 expression in choroidal epithelia of the blood-CSF barrier following manganese exposure in vitro. Brain Res. 2006 Jun 30;1097(1):1-10. Epub 2006 May 26.</reference_text>
      <pubmed_id>16729984</pubmed_id>
    </reference>
    <reference>
      <reference_text>Takeda A: Manganese action in brain function.  Brain Res Brain Res Rev. 2003 Jan;41(1):79-87.</reference_text>
      <pubmed_id>12505649</pubmed_id>
    </reference>
    <reference>
      <reference_text>Baldwin M, Mergler D, Larribe F, Belanger S, Tardif R, Bilodeau L, Hudnell K: Bioindicator and exposure data for a population based study of manganese.  Neurotoxicology. 1999 Apr-Jun;20(2-3):343-53.</reference_text>
      <pubmed_id>10385895</pubmed_id>
    </reference>
  </general_references>
  <synthesis_reference/>
  <msds_url>http://hmdb.ca/system/metabolites/msds/000/001/195/original/HMDB01333.pdf?1358894826</msds_url>
  <enzymes>
    <enzyme>
      <name>Catalase-peroxidase</name>
      <uniprot_id>P13029</uniprot_id>
      <uniprot_name>KATG_ECOLI</uniprot_name>
      <gene_name>katG</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P13029.xml</protein_url>
    </enzyme>
  </enzymes>
  <transporters>
    <enzyme>
      <name>Zinc transporter zupT</name>
      <uniprot_id>P0A8H3</uniprot_id>
      <uniprot_name>ZUPT_ECOLI</uniprot_name>
      <gene_name>zupT</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0A8H3.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Zinc transporter zitB</name>
      <uniprot_id>P75757</uniprot_id>
      <uniprot_name>ZITB_ECOLI</uniprot_name>
      <gene_name>zitB</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P75757.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Manganese transport protein mntH</name>
      <uniprot_id>P0A769</uniprot_id>
      <uniprot_name>MNTH_ECOLI</uniprot_name>
      <gene_name>mntH</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0A769.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>Ferrous-iron efflux pump fieF</name>
      <uniprot_id>P69380</uniprot_id>
      <uniprot_name>FIEF_ECOLI</uniprot_name>
      <gene_name>fieF</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P69380.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>
  </reactions>
  <concentrations>
    <growth_media/>
    <growth_system/>
    <concentration>4000.0</concentration>
    <concentration_units>uM</concentration_units>
    <internal/>
    <error>0.0</error>
    <temperature/>
    <strain>K-12</strain>
    <growth_status/>
    <molecules>16000000</molecules>
    <molecules_error>0</molecules_error>
    <reference>
      <reference_text>1. Cybercell Database: &lt;a href='http://ccdb.wishartlab.com/CCDB/cgi-bin/STAT_NEW.cgi'&gt;http://ccdb.wishartlab.com/CCDB/cgi-bin/STAT_NEW.cgi&lt;/a&gt; &lt;br&gt;	2. Phillips R., Kondev, J., Theriot, J. (2008) “Physical Biology of the Cell” Garland Science, New York, NY.</reference_text>
      <pubmed_id/>
    </reference>
  </concentrations>
</compound>
