<?xml version="1.0" encoding="UTF-8"?>
<compound>
  <version>2.0</version>
  <creation_date>2012-05-31 10:25:02 -0600</creation_date>
  <update_date>2015-09-17 15:41:02 -0600</update_date>
  <accession>ECMDB00257</accession>
  <m2m_id>M2MDB000108</m2m_id>
  <name>Thiosulfate</name>
  <description>Thiosulfate occurs naturally in hot springs and geysers, and is produced by certain biochemical processes.  Thiosulfate is an intermediate in several biochemical pathways, including the synthesis of L-cysteine. Thiosulfate is manufactured by some cells by oxidation of elemental sulfur and by degradation of L-cysteine.  </description>
  <synonyms>
    <synonym>Hyposulfite</synonym>
    <synonym>Hyposulphite</synonym>
    <synonym>S-Hydril</synonym>
    <synonym>S2O3</synonym>
    <synonym>S2O3-2</synonym>
    <synonym>S2O32-</synonym>
    <synonym>S&lt;SUB&gt;2&lt;/SUB&gt;O&lt;SUB&gt;3&lt;/SUB&gt;</synonym>
    <synonym>S&lt;SUB&gt;2&lt;/SUB&gt;O&lt;SUB&gt;3&lt;/SUB&gt;&lt;SUP&gt;-2&lt;/SUP&gt;</synonym>
    <synonym>S&lt;SUB&gt;2&lt;/SUB&gt;O&lt;SUB&gt;3&lt;/SUB&gt;&lt;SUP&gt;2-&lt;/SUP&gt;</synonym>
    <synonym>Sodium hyposulfite</synonym>
    <synonym>Sodium hyposulphite</synonym>
    <synonym>Sodium oxide sulfide (Na2S2O3)</synonym>
    <synonym>Sodium oxide sulphide (Na2S2O3)</synonym>
    <synonym>Sodium thiosulfate</synonym>
    <synonym>Sodium thiosulfate (Na2S2O3)</synonym>
    <synonym>Sodium thiosulfate anhydrous</synonym>
    <synonym>Sodium thiosulfuric acid</synonym>
    <synonym>Sodium thiosulfuric acid (na2S2O3)</synonym>
    <synonym>Sodium thiosulfuric acid anhydrous</synonym>
    <synonym>Sodium thiosulphate</synonym>
    <synonym>Sodium thiosulphate (Na2S2O3)</synonym>
    <synonym>Sodium thiosulphate anhydrous</synonym>
    <synonym>Sodium thiosulphuric acid</synonym>
    <synonym>Sodium thiosulphuric acid (na2S2O3)</synonym>
    <synonym>Sodium thiosulphuric acid anhydrous</synonym>
    <synonym>Sulfactol</synonym>
    <synonym>Sulphactol</synonym>
    <synonym>Thiosulfate</synonym>
    <synonym>Thiosulfate (H2S2O3)</synonym>
    <synonym>Thiosulfate ion</synonym>
    <synonym>Thiosulfurate</synonym>
    <synonym>Thiosulfurate (H2S2O3)</synonym>
    <synonym>Thiosulfuric acid</synonym>
    <synonym>Thiosulfuric acid (H2S2O3)</synonym>
    <synonym>Thiosulfuric acid ion</synonym>
    <synonym>Thiosulphate</synonym>
    <synonym>Thiosulphate (H2S2O3)</synonym>
    <synonym>Thiosulphate ion</synonym>
    <synonym>Thiosulphurate</synonym>
    <synonym>Thiosulphurate (H2S2O3)</synonym>
    <synonym>Thiosulphuric acid</synonym>
    <synonym>Thiosulphuric acid (H2S2O3)</synonym>
    <synonym>Thiosulphuric acid ion</synonym>
  </synonyms>
  <chemical_formula>O3S2</chemical_formula>
  <average_molecular_weight>112.128</average_molecular_weight>
  <monisotopic_moleculate_weight>111.928885246</monisotopic_moleculate_weight>
  <iupac_name>sulfanesulfonic acid</iupac_name>
  <traditional_iupac>sulfurothioic S-acid</traditional_iupac>
  <cas_registry_number>14383-50-7</cas_registry_number>
  <smiles>[O-]S([S-])(=O)=O</smiles>
  <inchi>InChI=1S/H2O3S2/c1-5(2,3)4/h(H2,1,2,3,4)/p-2</inchi>
  <inchikey>DHCDFWKWKRSZHF-UHFFFAOYSA-L</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>48 oC</value>
    </property>
  </experimental_properties>
  <property>
    <kind>logp</kind>
    <value>-0.096</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>pka_strongest_acidic</kind>
    <value>-2.3</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>iupac</kind>
    <value>sulfanesulfonic acid</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>average_mass</kind>
    <value>112.128</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>mono_mass</kind>
    <value>111.928885246</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>smiles</kind>
    <value>[O-]S([S-])(=O)=O</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>formula</kind>
    <value>O3S2</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>inchi</kind>
    <value>InChI=1S/H2O3S2/c1-5(2,3)4/h(H2,1,2,3,4)/p-2</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>inchikey</kind>
    <value>DHCDFWKWKRSZHF-UHFFFAOYSA-L</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>polar_surface_area</kind>
    <value>54.37</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>refractivity</kind>
    <value>17.76</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>polarizability</kind>
    <value>8.29</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>rotatable_bond_count</kind>
    <value>0</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>-1</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>formal_charge</kind>
    <value>0</value>
    <source>ChemAxon</source>
  </property>
  <pathways>
    <pathway>
      <name>Cysteine and methionine metabolism</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec00270</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>Sulfur metabolism</name>
      <description>The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and  adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate,  which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. 
The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described.
The third variant of sulfur metabolism starts with the import of an alkyl sulfate into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. The alkyl sulfate is dehydrogenated and along with oxygen is converted to sulfite and an aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described.</description>
      <pathwhiz_id>PW000922</pathwhiz_id>
      <kegg_map_id>ec00920</kegg_map_id>
      <subject>Metabolic</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>cysteine biosynthesis</name>
      <description>The pathway of cysteine biosynthesis is a two-step conversion starting from L-serine and yielding L-cysteine. L-serine biosynthesis is shown for context.
L-cysteine can also be synthesized from sulfate derivatives.
The process through L-serine involves a serine acetyltransferase that produces a O-acetylserine which reacts together with hydrogen sulfide through a cysteine synthase complex in order to produce L-cysteine and acetic acid.
Hydrogen sulfide is produced from a sulfate. Sulfate reacts with sulfate adenylyltransferase to produce adenosine phosphosulfate. This compound in turn is phosphorylated through a adenylyl-sulfate kinase into a phosphoadenosine phosphosulfate which in turn reacts with a phosphoadenosine phosphosulfate reductase to produce a sulfite. The sulfite reacts with a sulfite reductase to produce the hydrogen sulfide.
This pathway is regulated at the genetic level in its second step, wtih both cysteine synthase isozymes being under the positive control of the cysteine-responsive transcription factor CysB. It is also subject to very strong feedback inhibition of its first step by the final pathway product, cysteine.

Although two cysteine synthase isozymes exist, only cysteine synthase A (CysK) forms a complex with serine acetyltransferase. CysK is also the only one of the two cysteine synthases that is required for cell viability on cysteine-free medium.

Both steps in this pathway are reversible. Based on genetic and proteomic data, it appears that the cysteine synthases may actually act as a sulfur scavenging system during sulfur starvation, stripping sulfur off of L-cysteine, generating any number of variant amino acids in the process.</description>
      <pathwhiz_id>PW000800</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>sulfur metabolism (butanesulfonate)</name>
      <description>The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate, in this case 1-butanesulfonate, into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. 1-butanesulfonate is dehydrogenated and along with oxygen is converted to sulfite and betaine aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described.</description>
      <pathwhiz_id>PW000923</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>sulfur metabolism (ethanesulfonate)</name>
      <description>The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate, in this case ethanesulfonate, into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. Ethanesulfonate is dehydrogenated and along with oxygen is converted to sulfite and betaine aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described.</description>
      <pathwhiz_id>PW000925</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>sulfur metabolism (isethionate)</name>
      <description>The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate, in this case isethionate, into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. Isethionate is dehydrogenated and along with oxygen is converted to sulfite and betaine aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described.</description>
      <pathwhiz_id>PW000926</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>sulfur metabolism (methanesulfonate)</name>
      <description>The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate, in this case methanesulfonate, into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. Methanesulfonate is dehydrogenated and along with oxygen is converted to sulfite and an aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described.</description>
      <pathwhiz_id>PW000927</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>sulfur metabolism (propanesulfonate)</name>
      <description>The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate, in this case 3-(N-morpholino)propanesulfonate, into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. 3-(N-morpholino)propanesulfonate is dehydrogenated and along with oxygen is converted to sulfite and betaine aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described.</description>
      <pathwhiz_id>PW000924</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>Thiosulfate Disproportionation III</name>
      <description>Thiosulfate sulfurtransferase is more often referred to by the name rhodanese, from the German word for thiocyanate, "rhodanid". The enzyme catalyzes the transfer of a sulfur atom from suitable sulfur donors to nucleophilic sulfur acceptors. The original description of rhodanese, purified from bovine mitochondria, used thiosulfate and cyanide for this purpose. Rhodanese is a widespread enzyme, and has been detected in many major phyla, both prokaryotic and eukaryotic. Despite its ubiquity, the physiological role of rhodanese has not yet been established unambiguously. It has been suggested that rhodanese is involved in detoxification of cyanide in both mammals and bacteria. It has also been proposed that rhodanese, using the dithiol dihydrolipoate as the sulfur acceptor, may act as a sulfur insertase involved in the formation of prosthetic groups in iron-sulfur proteins, such as ferredoxin. (EcoCyc)</description>
      <pathwhiz_id>PW002060</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>thiosulfate disproportionation III (rhodanese)</name>
      <ecocyc_pathway_id>PWY-5350</ecocyc_pathway_id>
    </pathway>
  </pathways>
  <spectra>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>33194</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>159400</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>169131</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6292</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6293</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6294</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6295</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6296</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6297</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6298</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6299</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6300</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>6301</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>27059</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>27060</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>27061</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>33617</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>33618</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>33619</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>1218079</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>1218080</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>1218081</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2315777</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2315778</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2315779</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2622833</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2622834</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2622835</spectrum_id>
    </spectrum>
  </spectra>
  <hmdb_id>HMDB00257</hmdb_id>
  <pubchem_compound_id>439208</pubchem_compound_id>
  <chemspider_id>1054</chemspider_id>
  <kegg_id>C00320</kegg_id>
  <chebi_id>16094</chebi_id>
  <biocyc_id>S2O3</biocyc_id>
  <het_id>THJ</het_id>
  <wikipidia>Thiosulfate</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>Thiele I, Swainston N, Fleming RM, Hoppe A, Sahoo S, Aurich MK, Haraldsdottir H, Mo ML, Rolfsson O, Stobbe MD, Thorleifsson SG, Agren R, Bolling C, Bordel S, Chavali AK, Dobson P, Dunn WB, Endler L, Hala D, Hucka M, Hull D, Jameson D, Jamshidi N, Jonsson JJ, Juty N, Keating S, Nookaew I, Le Novere N, Malys N, Mazein A, Papin JA, Price ND, Selkov E Sr, Sigurdsson MI, Simeonidis E, Sonnenschein N, Smallbone K, Sorokin A, van Beek JH, Weichart D, Goryanin I, Nielsen J, Westerhoff HV, Kell DB, Mendes P, Palsson BO: A community-driven global reconstruction of human metabolism. Nat Biotechnol. 2013 Mar 3. doi: 10.1038/nbt.2488.</reference_text>
      <pubmed_id>23455439</pubmed_id>
    </reference>
  </general_references>
  <synthesis_reference>Serikova, E. A.; Racheva, I. V. Method for producing sodium thiosulfate.  U.S.S.R.  (1986), CODEN: URXXAF  SU  1279954  A1  19861230  Patent  written in Russian.  </synthesis_reference>
  <msds_url>http://hmdb.ca/system/metabolites/msds/000/000/189/original/HMDB00257.pdf?1358462823</msds_url>
  <enzymes>
    <enzyme>
      <name>Cystathionine gamma-synthase</name>
      <uniprot_id>P00935</uniprot_id>
      <uniprot_name>METB_ECOLI</uniprot_name>
      <gene_name>metB</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P00935.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Thiosulfate sulfurtransferase glpE</name>
      <uniprot_id>P0A6V5</uniprot_id>
      <uniprot_name>GLPE_ECOLI</uniprot_name>
      <gene_name>glpE</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0A6V5.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Cysteine synthase A</name>
      <uniprot_id>P0ABK5</uniprot_id>
      <uniprot_name>CYSK_ECOLI</uniprot_name>
      <gene_name>cysK</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0ABK5.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Sulfate/thiosulfate import ATP-binding protein cysA</name>
      <uniprot_id>P16676</uniprot_id>
      <uniprot_name>CYSA_ECOLI</uniprot_name>
      <gene_name>cysA</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P16676.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Cysteine synthase B</name>
      <uniprot_id>P16703</uniprot_id>
      <uniprot_name>CYSM_ECOLI</uniprot_name>
      <gene_name>cysM</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P16703.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>3-mercaptopyruvate sulfurtransferase</name>
      <uniprot_id>P31142</uniprot_id>
      <uniprot_name>THTM_ECOLI</uniprot_name>
      <gene_name>sseA</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P31142.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Thiosulfate sulfurtransferase YnjE</name>
      <uniprot_id>P78067</uniprot_id>
      <uniprot_name>YNJE_ECOLI</uniprot_name>
      <gene_name>ynjE</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P78067.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Sulfate transport system permease protein cysW</name>
      <uniprot_id>P0AEB0</uniprot_id>
      <uniprot_name>CYSW_ECOLI</uniprot_name>
      <gene_name>cysW</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AEB0.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Sulfate transport system permease protein cysT</name>
      <uniprot_id>P16701</uniprot_id>
      <uniprot_name>CYST_ECOLI</uniprot_name>
      <gene_name>cysU</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P16701.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Sulfate-binding protein</name>
      <uniprot_id>P0AG78</uniprot_id>
      <uniprot_name>SUBI_ECOLI</uniprot_name>
      <gene_name>sbp</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AG78.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Thiosulfate-binding protein</name>
      <uniprot_id>P16700</uniprot_id>
      <uniprot_name>CYSP_ECOLI</uniprot_name>
      <gene_name>cysP</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P16700.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Thiosulfate sulfurtransferase PspE</name>
      <uniprot_id>P23857</uniprot_id>
      <uniprot_name>PSPE_ECOLI</uniprot_name>
      <gene_name>pspE</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P23857.xml</protein_url>
    </enzyme>
  </enzymes>
  <transporters>
    <enzyme>
      <name>Sulfate/thiosulfate import ATP-binding protein cysA</name>
      <uniprot_id>P16676</uniprot_id>
      <uniprot_name>CYSA_ECOLI</uniprot_name>
      <gene_name>cysA</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P16676.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Sulfate transport system permease protein cysW</name>
      <uniprot_id>P0AEB0</uniprot_id>
      <uniprot_name>CYSW_ECOLI</uniprot_name>
      <gene_name>cysW</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AEB0.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Sulfate transport system permease protein cysT</name>
      <uniprot_id>P16701</uniprot_id>
      <uniprot_name>CYST_ECOLI</uniprot_name>
      <gene_name>cysU</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P16701.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Sulfate-binding protein</name>
      <uniprot_id>P0AG78</uniprot_id>
      <uniprot_name>SUBI_ECOLI</uniprot_name>
      <gene_name>sbp</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AG78.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>Thiosulfate-binding protein</name>
      <uniprot_id>P16700</uniprot_id>
      <uniprot_name>CYSP_ECOLI</uniprot_name>
      <gene_name>cysP</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P16700.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>
    <enzyme>
      <name>Protein PhsC homolog</name>
      <uniprot_id>P77409</uniprot_id>
      <uniprot_name>PHSC_ECOLI</uniprot_name>
      <gene_name>ydhU</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P77409.xml</protein_url>
    </enzyme>
  </transporters>
  <reactions>
    <reaction_text>Adenosine triphosphate + Water + Thiosulfate &gt; ADP + Hydrogen ion + Phosphate + Thiosulfate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>ABC-7-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + Water + Thiosulfate &gt; ADP + Hydrogen ion + Phosphate + Thiosulfate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>ABC-7-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Hydrogen cyanide + Thiosulfate &gt; Hydrogen ion + Sulfite + Thiocyanate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Thiosulfate + Cyanide &lt;&gt; Sulfite + Thiocyanate</reaction_text>
    <kegg_reaction_id>R01931</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>3-Mercaptopyruvic acid + Sulfite &lt;&gt; Thiosulfate + Pyruvic acid</reaction_text>
    <kegg_reaction_id>R03105</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>O-Acetylserine + Thiosulfate &lt;&gt; Cysteine-S-sulfate + Acetic acid</reaction_text>
    <kegg_reaction_id>R03132</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>O-Acetylserine + Thiosulfate + Thioredoxin + Hydrogen ion &lt;&gt; L-Cysteine + Sulfite + Thioredoxin disulfide + Acetic acid</reaction_text>
    <kegg_reaction_id>R04859</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + Thiosulfate + Water &gt; ADP + Phosphate + Thiosulfate + Hydrogen ion</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>ABC-7-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + Thiosulfate + Water &gt; ADP + Phosphate + Thiosulfate + Hydrogen ion</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>ABC-7-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Thiosulfate + Hydrogen cyanide &gt; Sulfite + Thiocyanate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Cyanide + Thiosulfate + Cyanide + Thiosulfate &gt; Thiocyanate + Sulfite + Hydrogen ion + Thiocyanate + Sulfite</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id>PW_R003463</pw_reaction_id>
    <reaction_text>O-Acetylserine + Thiosulfate + Thiosulfate &gt; Cysteine-S-sulfate + Acetic acid</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id>PW_R005147</pw_reaction_id>
    <reaction_text>Hydrogen cyanide + Thiosulfate &gt; Thiocyanate + Sulfite +2 Hydrogen ion</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id>PW_R006013</pw_reaction_id>
    <reaction_text>Thiosulfate + Adenosine triphosphate + Water &gt; ADP + Phosphate + Hydrogen ion</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id>PW_RCT000185</pw_reaction_id>
    <reaction_text>Thiosulfate + Cyanide &lt;&gt; Sulfite + Thiocyanate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Thiosulfate + Cyanide &lt;&gt; Sulfite + Thiocyanate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
  </reactions>
  <concentrations>
  </concentrations>
</compound>
