<?xml version="1.0" encoding="UTF-8"?>
<compound>
  <version>2.0</version>
  <creation_date>2012-05-31 13:46:04 -0600</creation_date>
  <update_date>2015-06-03 15:53:46 -0600</update_date>
  <accession>ECMDB01134</accession>
  <m2m_id>M2MDB000269</m2m_id>
  <name>Phosphoadenosine phosphosulfate</name>
  <description>3'-Phosphoadenosine-5'-phosphosulfate is a key intermediate in the formation by living cells of sulfate esters of phenols, alcohols, sulfated polysaccharides, and simple esters, such as choline sulfate. It is formed from a sulfate ion and ATP in a two-step process. This compound also is an important intermediate in the process of sulfur fixation in plants and microorganisms.</description>
  <synonyms>
    <synonym>3'-Phospho-5'-adenylyl sulfate</synonym>
    <synonym>3'-phospho-5'-Adenylyl sulfuric acid</synonym>
    <synonym>3'-Phospho-5'-adenylyl sulphate</synonym>
    <synonym>3'-phospho-5'-Adenylyl sulphuric acid</synonym>
    <synonym>3'-Phosphoadenosine 5'-phosphosulfate</synonym>
    <synonym>3'-Phosphoadenosine 5'-phosphosulfuric acid</synonym>
    <synonym>3'-Phosphoadenosine 5'-phosphosulphate</synonym>
    <synonym>3'-Phosphoadenosine 5'-phosphosulphuric acid</synonym>
    <synonym>3'-Phosphoadenosine-5'-phosphosulfate</synonym>
    <synonym>3'-Phosphoadenosine-5'-phosphosulfuric acid</synonym>
    <synonym>3'-Phosphoadenosine-5'-phosphosulphate</synonym>
    <synonym>3'-Phosphoadenosine-5'-phosphosulphuric acid</synonym>
    <synonym>3'-Phosphoadenylyl sulfate</synonym>
    <synonym>3'-Phosphoadenylyl sulfuric acid</synonym>
    <synonym>3'-Phosphoadenylyl sulphate</synonym>
    <synonym>3'-Phosphoadenylyl sulphuric acid</synonym>
    <synonym>3'-Phosphoadenylyl-sulfate</synonym>
    <synonym>3'-Phosphoadenylyl-sulfuric acid</synonym>
    <synonym>3'-Phosphoadenylyl-sulphate</synonym>
    <synonym>3'-Phosphoadenylyl-sulphuric acid</synonym>
    <synonym>5-Phosphoadenosine 3-phosphosulfate</synonym>
    <synonym>5-Phosphoadenosine 3-phosphosulfuric acid</synonym>
    <synonym>5-Phosphoadenosine 3-phosphosulphate</synonym>
    <synonym>5-Phosphoadenosine 3-phosphosulphuric acid</synonym>
    <synonym>PAPS</synonym>
    <synonym>Phosphoadenosine Phosphosulfate</synonym>
    <synonym>Phosphoadenosine phosphosulfuric acid</synonym>
    <synonym>Phosphoadenosine Phosphosulphate</synonym>
    <synonym>Phosphoadenosine phosphosulphuric acid</synonym>
  </synonyms>
  <chemical_formula>C10H15N5O13P2S</chemical_formula>
  <average_molecular_weight>507.264</average_molecular_weight>
  <monisotopic_moleculate_weight>506.986229305</monisotopic_moleculate_weight>
  <iupac_name>[({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy]sulfonic acid</iupac_name>
  <traditional_iupac>3'-phosphoadenylyl sulfate</traditional_iupac>
  <cas_registry_number>482-67-7</cas_registry_number>
  <smiles>NC1=NC=NC2=C1N=CN2[C@@H]1O[C@H](COP(O)(=O)OS(O)(=O)=O)[C@@H](OP(O)(O)=O)[C@H]1O</smiles>
  <inchi>InChI=1S/C10H15N5O13P2S/c11-8-5-9(13-2-12-8)15(3-14-5)10-6(16)7(27-29(17,18)19)4(26-10)1-25-30(20,21)28-31(22,23)24/h2-4,6-7,10,16H,1H2,(H,20,21)(H2,11,12,13)(H2,17,18,19)(H,22,23,24)/t4-,6-,7-,10-/m1/s1</inchi>
  <inchikey>GACDQMDRPRGCTN-KQYNXXCUSA-N</inchikey>
  <state>Solid</state>
  <cellular_locations>
    <cellular_location>Cytosol</cellular_location>
  </cellular_locations>
  <predicted_properties>
    <property>
      <kind>logp</kind>
      <value>-0.65</value>
      <source>ALOGPS</source>
    </property>
    <property>
      <kind>logs</kind>
      <value>-2.00</value>
      <source>ALOGPS</source>
    </property>
    <property>
      <kind>solubility</kind>
      <value>5.05e+00 g/l</value>
      <source>ALOGPS</source>
    </property>
  </predicted_properties>
  <experimental_properties>
  </experimental_properties>
  <property>
    <kind>logp</kind>
    <value>-5.7</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>pka_strongest_acidic</kind>
    <value>-2.4</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>pka_strongest_basic</kind>
    <value>3.94</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>iupac</kind>
    <value>[({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy]sulfonic acid</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>average_mass</kind>
    <value>507.264</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>mono_mass</kind>
    <value>506.986229305</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>smiles</kind>
    <value>NC1=NC=NC2=C1N=CN2[C@@H]1O[C@H](COP(O)(=O)OS(O)(=O)=O)[C@@H](OP(O)(O)=O)[C@H]1O</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>formula</kind>
    <value>C10H15N5O13P2S</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>inchi</kind>
    <value>InChI=1S/C10H15N5O13P2S/c11-8-5-9(13-2-12-8)15(3-14-5)10-6(16)7(27-29(17,18)19)4(26-10)1-25-30(20,21)28-31(22,23)24/h2-4,6-7,10,16H,1H2,(H,20,21)(H2,11,12,13)(H2,17,18,19)(H,22,23,24)/t4-,6-,7-,10-/m1/s1</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>inchikey</kind>
    <value>GACDQMDRPRGCTN-KQYNXXCUSA-N</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>polar_surface_area</kind>
    <value>275.97</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>refractivity</kind>
    <value>94.93</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>polarizability</kind>
    <value>39.26</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>rotatable_bond_count</kind>
    <value>8</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>acceptor_count</kind>
    <value>14</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>donor_count</kind>
    <value>6</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>physiological_charge</kind>
    <value>-4</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>formal_charge</kind>
    <value>0</value>
    <source>ChemAxon</source>
  </property>
  <pathways>
    <pathway>
      <name>Purine metabolism</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec00230</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>Selenoamino acid metabolism</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec00450</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>Metabolic pathways</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>eco01100</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>sulfate reduction I (assimilatory)</name>
      <ecocyc_pathway_id>SO4ASSIM-PWY</ecocyc_pathway_id>
    </pathway>
    <pathway>
      <name>sulfate activation for sulfonation</name>
      <ecocyc_pathway_id>PWY-5340</ecocyc_pathway_id>
    </pathway>
  </pathways>
  <spectra>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>26365</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>37942</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>146570</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>146571</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>146572</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>146573</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>146574</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>146575</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>146576</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>146577</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>146578</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>146579</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>146580</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>146581</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>146582</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>146583</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>146584</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>146585</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>146586</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>146587</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>146588</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::NmrOneD</type>
      <spectrum_id>146589</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>27410</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>27411</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>27412</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>33968</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>33969</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>33970</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2700499</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2700500</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2700501</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>3004902</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>3004903</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>3004904</spectrum_id>
    </spectrum>
  </spectra>
  <hmdb_id>HMDB01134</hmdb_id>
  <pubchem_compound_id>990</pubchem_compound_id>
  <chemspider_id>9799</chemspider_id>
  <kegg_id>C00053</kegg_id>
  <chebi_id>17980</chebi_id>
  <biocyc_id>PAPS</biocyc_id>
  <het_id>PPS</het_id>
  <wikipidia>Phosphoadenosine phosphosulfate</wikipidia>
  <foodb_id/>
  <general_references>
    <reference>
      <reference_text>Keseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590.</reference_text>
      <pubmed_id>21097882</pubmed_id>
    </reference>
    <reference>
      <reference_text>Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114.</reference_text>
      <pubmed_id>22080510</pubmed_id>
    </reference>
    <reference>
      <reference_text>van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25.</reference_text>
      <pubmed_id>17765195</pubmed_id>
    </reference>
    <reference>
      <reference_text>Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). "Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948.</reference_text>
      <pubmed_id>18331064</pubmed_id>
    </reference>
    <reference>
      <reference_text>Emmi L, Bergamini C, Spinelli A, Liotta F, Marchione T, Caldini A, Fanelli A, De Cristofaro MT, Dal Pozzo G: Possible pathogenetic role of activated platelets in the primary antiphospholipid syndrome involving the central nervous system. Ann N Y Acad Sci. 1997 Aug 14;823:188-200.</reference_text>
      <pubmed_id>9292045</pubmed_id>
    </reference>
    <reference>
      <reference_text>Fanelli A, Bergamini C, Rapi S, Caldini A, Spinelli A, Buggiani A, Emmi L: Flow cytometric detection of circulating activated platelets in primary antiphospholipid syndrome. Correlation with thrombocytopenia and anticardiolipin antibodies. Lupus. 1997;6(3):261-7.</reference_text>
      <pubmed_id>9104734</pubmed_id>
    </reference>
    <reference>
      <reference_text>Joseph JE, Harrison P, Mackie IJ, Isenberg DA, Machin SJ: Increased circulating platelet-leucocyte complexes and platelet activation in patients with antiphospholipid syndrome, systemic lupus erythematosus and rheumatoid arthritis. Br J Haematol. 2001 Nov;115(2):451-9.</reference_text>
      <pubmed_id>11703349</pubmed_id>
    </reference>
    <reference>
      <reference_text>Suarez IM, Diaz RA, Aguayo Canela D, Pujol de la Llave E: Correction of severe thrombocytopenia with chloroquine in the primary antiphospholipid syndrome. Lupus. 1996 Feb;5(1):81-3.</reference_text>
      <pubmed_id>8646233</pubmed_id>
    </reference>
    <reference>
      <reference_text>Khoo BY, Sit KH, Wong KP: Does PAPS generation determine the overall sulfate conjugation in human platelets? Life Sci. 1988;42(23):2389-95.</reference_text>
      <pubmed_id>3131608</pubmed_id>
    </reference>
    <reference>
      <reference_text>Wong KP, Khoo BY, Sit KH: Biosynthesis of PAPS in vitro by human liver. Measurement by two independent assay procedures. Biochem Pharmacol. 1991 Jan 1;41(1):63-9.</reference_text>
      <pubmed_id>1846073</pubmed_id>
    </reference>
    <reference>
      <reference_text>Cappiello M, Franchi M, Rane A, Pacifici GM: Sulphotransferase and its substrate: adenosine-3'-phosphate-5'-phosphosulphate in human fetal liver and placenta. Dev Pharmacol Ther. 1990;14(1):62-5.</reference_text>
      <pubmed_id>2311482</pubmed_id>
    </reference>
    <reference>
      <reference_text>Cappiello M, Franchi M, Giuliani L, Pacifici GM: Distribution of 2-naphthol sulphotransferase and its endogenous substrate adenosine 3'-phosphate 5'-phosphosulphate in human tissues. Eur J Clin Pharmacol. 1989;37(3):317-20.</reference_text>
      <pubmed_id>2612547</pubmed_id>
    </reference>
    <reference>
      <reference_text>Carlier M, Squifflet JP, Pirson Y, Gribomont B, Alexandre GP: Maximal hydration during anesthesia increases pulmonary arterial pressures and improves early function of human renal transplants. Transplantation. 1982 Oct;34(4):201-4.</reference_text>
      <pubmed_id>6755828</pubmed_id>
    </reference>
  </general_references>
  <synthesis_reference>Lin, Chun-Hung; Shen, Gwo-Jenn; Garcia-Junceda, Eduardo; Wong, Chi-Huey. Enzymic Synthesis and Regeneration of 3'-Phosphoadenosine 5'-Phosphosulfate (PAPS) for Regioselective Sulfation of Oligosaccharides. Journal of the American Chemical Society (1995), </synthesis_reference>
  <msds_url/>
  <enzymes>
    <enzyme>
      <name>Adenylyl-sulfate kinase</name>
      <uniprot_id>P0A6J1</uniprot_id>
      <uniprot_name>CYSC_ECOLI</uniprot_name>
      <gene_name>cysC</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0A6J1.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Thioredoxin-2</name>
      <uniprot_id>P0AGG4</uniprot_id>
      <uniprot_name>THIO2_ECOLI</uniprot_name>
      <gene_name>trxC</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AGG4.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Phosphoadenosine phosphosulfate reductase</name>
      <uniprot_id>P17854</uniprot_id>
      <uniprot_name>CYSH_ECOLI</uniprot_name>
      <gene_name>cysH</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P17854.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>3'(2'),5'-bisphosphate nucleotidase cysQ</name>
      <uniprot_id>P22255</uniprot_id>
      <uniprot_name>CYSQ_ECOLI</uniprot_name>
      <gene_name>cysQ</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P22255.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Putative aliphatic sulfonates transport permease protein ssuC</name>
      <uniprot_id>P75851</uniprot_id>
      <uniprot_name>SSUC_ECOLI</uniprot_name>
      <gene_name>ssuC</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P75851.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Glutaredoxin-4</name>
      <uniprot_id>P0AC69</uniprot_id>
      <uniprot_name>GLRX4_ECOLI</uniprot_name>
      <gene_name>grxD</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AC69.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Glutaredoxin-3</name>
      <uniprot_id>P0AC62</uniprot_id>
      <uniprot_name>GLRX3_ECOLI</uniprot_name>
      <gene_name>grxC</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AC62.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Glutaredoxin-2</name>
      <uniprot_id>P0AC59</uniprot_id>
      <uniprot_name>GLRX2_ECOLI</uniprot_name>
      <gene_name>grxB</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AC59.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Glutaredoxin-1</name>
      <uniprot_id>P68688</uniprot_id>
      <uniprot_name>GLRX1_ECOLI</uniprot_name>
      <gene_name>grxA</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P68688.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Thioredoxin-1</name>
      <uniprot_id>P0AA25</uniprot_id>
      <uniprot_name>THIO_ECOLI</uniprot_name>
      <gene_name>trxA</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AA25.xml</protein_url>
    </enzyme>
  </enzymes>
  <transporters>
    <enzyme>
      <name>Putative aliphatic sulfonates transport permease protein ssuC</name>
      <uniprot_id>P75851</uniprot_id>
      <uniprot_name>SSUC_ECOLI</uniprot_name>
      <gene_name>ssuC</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P75851.xml</protein_url>
    </enzyme>
  </transporters>
  <reactions>
    <reaction_text>glutaredoxin + Phosphoadenosine phosphosulfate &gt; glutaredoxin +2 Hydrogen ion + Adenosine 3',5'-diphosphate + Sulfite</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Phosphoadenosine phosphosulfate + Reduced Thioredoxin &gt;2 Hydrogen ion + Adenosine 3',5'-diphosphate + Sulfite + Oxidized Thioredoxin</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Adenosine phosphosulfate + Adenosine triphosphate &lt;&gt; ADP + Hydrogen ion + Phosphoadenosine phosphosulfate</reaction_text>
    <kegg_reaction_id>R00509</kegg_reaction_id>
    <ecocyc_id>ADENYLYLSULFKIN-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Phosphoadenosine phosphosulfate + Water &lt;&gt; Adenosine phosphosulfate + Phosphate</reaction_text>
    <kegg_reaction_id>R00508</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + Adenosine phosphosulfate &lt;&gt; ADP + Phosphoadenosine phosphosulfate</reaction_text>
    <kegg_reaction_id>R00509</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Thioredoxin + Phosphoadenosine phosphosulfate + Thioredoxin disulfide &lt;&gt; Thioredoxin disulfide + Sulfite + Adenosine 3',5'-diphosphate + Thioredoxin</reaction_text>
    <kegg_reaction_id>R02021</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Adenosine phosphosulfate + Adenosine triphosphate &gt; Hydrogen ion + Phosphoadenosine phosphosulfate + ADP</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>ADENYLYLSULFKIN-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + Adenosine phosphosulfate &gt; ADP + Phosphoadenosine phosphosulfate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Adenosine 3',5'-diphosphate + Sulfite + thioredoxin disulfide &gt; Phosphoadenosine phosphosulfate + thioredoxin</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Phosphoadenosine phosphosulfate + reduced thioredoxin &gt; Sulfite +2 Hydrogen ion + Adenosine 3',5'-diphosphate +2 oxidized thioredoxin  + Sulfite + Adenosine 3',5'-diphosphate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id>PW_R002850</pw_reaction_id>
    <reaction_text>Phosphoadenosine phosphosulfate + reduced thioredoxin &gt; Sulfite + oxidized thioredoxin  + Hydrogen ion + Adenosine 3',5'-diphosphate + Sulfite + Adenosine 3',5'-diphosphate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id>PW_R003460</pw_reaction_id>
    <reaction_text>Adenosine phosphosulfate + Adenosine triphosphate &gt; Phosphoadenosine phosphosulfate + Adenosine diphosphate + Hydrogen ion + ADP</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id>PW_R002851</pw_reaction_id>
    <reaction_text>Adenosine phosphosulfate + Adenosine triphosphate &lt;&gt; ADP + Hydrogen ion + Phosphoadenosine phosphosulfate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Thioredoxin + Phosphoadenosine phosphosulfate + Thioredoxin disulfide &lt;&gt; Sulfite + Adenosine 3',5'-diphosphate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Phosphoadenosine phosphosulfate + Water &lt;&gt; Adenosine phosphosulfate + Phosphate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Phosphoadenosine phosphosulfate + Water &lt;&gt; Adenosine phosphosulfate + Phosphate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
  </reactions>
  <concentrations>
  </concentrations>
</compound>
