Human Metabolome Database: Showing metabocard for Phosphoadenosine phosphosulfate (HMDB0001134)

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Identification Taxonomy Ontology Physical properties Spectra Biological properties Concentrations Links References enzymes (42) Show 42 proteins XML

enzymes (42) Show 42 proteins

Record Information

Version

4.0

Status

Expected but not Quantified

Creation Date

2005-11-16 15:48:42 UTC

Update Date

2020-06-25 20:15:15 UTC

HMDB ID

HMDB0001134

Secondary Accession Numbers

HMDB01134

Metabolite Identification

Common Name

Phosphoadenosine phosphosulfate

Description

Phosphoadenosine phosphosulfate, also known as 3'-phospho-5'-adenylyl sulfate or PAPS, belongs to the class of organic compounds known as purine ribonucleoside 3',5'-bisphosphates. These are purine ribobucleotides with one phosphate group attached to 3' and 5' hydroxyl groups of the ribose moiety. Phosphoadenosine phosphosulfate is a strong basic compound (based on its pKa). Phosphoadenosine phosphosulfate exists in all living species, ranging from bacteria to humans. Within humans, phosphoadenosine phosphosulfate participates in a number of enzymatic reactions. In particular, galactosylceramide (D18:1/18:0) and phosphoadenosine phosphosulfate can be converted into 3-O-sulfogalactosylceramide (D18:1/18:0) and adenosine 3',5'-diphosphate through its interaction with the enzyme galactosylceramide sulfotransferase. In addition, galabiosylceramide (D18:1/18:0) and phosphoadenosine phosphosulfate can be converted into adenosine 3',5'-diphosphate and galabiosylceramide sulfate (D18:1/18:0) through its interaction with the enzyme galactosylceramide sulfotransferase. An adenosine bisphosphate having monophosphate groups at the 3'- and 5'-positions and a sulfo group attached to the phosphate at position 5'. In humans, phosphoadenosine phosphosulfate is involved in globoid cell leukodystrophy.

Structure

MOL SDF PDB SMILES InChI

Synonyms

Value	Source
3'-Phosphoadenosine 5'-phosphosulfate	ChEBI
3'-Phosphoadenylyl sulfate	ChEBI
PAPS	ChEBI
3'-Phospho-5'-adenylyl sulfate	Kegg
3'-Phosphoadenosine 5'-phosphosulfuric acid	Generator
3'-Phosphoadenosine 5'-phosphosulphate	Generator
3'-Phosphoadenosine 5'-phosphosulphuric acid	Generator
3'-Phosphoadenylyl sulfuric acid	Generator
3'-Phosphoadenylyl sulphate	Generator
3'-Phosphoadenylyl sulphuric acid	Generator
3'-Phospho-5'-adenylyl sulfuric acid	Generator
3'-Phospho-5'-adenylyl sulphate	Generator
3'-Phospho-5'-adenylyl sulphuric acid	Generator
Phosphoadenosine phosphosulfuric acid	Generator
Phosphoadenosine phosphosulphate	Generator
Phosphoadenosine phosphosulphuric acid	Generator
3'-Phosphoadenosine-5'-phosphosulfate	HMDB
3'-Phosphoadenosine-5'-phosphosulphate	HMDB
3'-Phosphoadenylyl-sulfate	HMDB
3'-Phosphoadenylyl-sulphate	HMDB
5-Phosphoadenosine 3-phosphosulfate	HMDB
5-Phosphoadenosine 3-phosphosulphate	HMDB
Adenosine 3' phosphate 5' phosphosulfate	HMDB
Adenosine-3'-phosphate-5'-phosphosulfate	HMDB
Phosphosulfate, phosphoadenosine	HMDB
3’-Phosphoadenosine 5’-phosphosulfate	HMDB
3’-Phosphoadenosine 5’-phosphosulphate	HMDB
3’-Phosphoadenylyl sulfate	HMDB
3’-Phosphoadenylyl sulphate	HMDB
5'-Adenylyl sulfate 3'-phosphate	HMDB
5'-Adenylyl sulphate 3'-phosphate	HMDB
5’-Adenylyl sulfate 3’-phosphate	HMDB
5’-Adenylyl sulphate 3’-phosphate	HMDB
Adenosine 3'-phosphate 5'-phosphosulfate	HMDB
Adenosine 3'-phosphate 5'-phosphosulphate	HMDB
Adenosine 3'-phosphate 5'-sulfatophosphate	HMDB
Adenosine 3’-phosphate 5’-phosphosulfate	HMDB
Adenosine 3’-phosphate 5’-phosphosulphate	HMDB
Adenosine 3’-phosphate 5’-sulfatophosphate	HMDB
Adenosine 5'-phosphosulfate 3'-phosphate	HMDB
Adenosine 5'-phosphosulphate 3'-phosphate	HMDB
Adenosine 5’-phosphosulfate 3’-phosphate	HMDB
Adenosine 5’-phosphosulphate 3’-phosphate	HMDB

Chemical Formula

C₁₀H₁₅N₅O₁₃P₂S

Average Molecular Weight

507.264

Monoisotopic Molecular Weight

506.986229305

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

Traditional Name

3'-phosphoadenylyl sulfate

CAS Registry Number

482-67-7

SMILES

NC1=C2N=CN([C@@H]3O[C@H](COP(O)(=O)OS(O)(=O)=O)[C@@H](OP(O)(O)=O)[C@H]3O)C2=NC=N1

InChI Identifier

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 Key

GACDQMDRPRGCTN-KQYNXXCUSA-N

Chemical Taxonomy

Description

belongs to the class of organic compounds known as purine ribonucleoside 3',5'-bisphosphates. These are purine ribobucleotides with one phosphate group attached to 3' and 5' hydroxyl groups of the ribose moiety.

Kingdom

Organic compounds

Super Class

Nucleosides, nucleotides, and analogues

Class

Purine nucleotides

Sub Class

Purine ribonucleotides

Direct Parent

Purine ribonucleoside 3',5'-bisphosphates

Alternative Parents

Substituents

Purine ribonucleoside 3',5'-bisphosphate
Purine ribonucleoside monophosphate
Ribonucleoside 3'-phosphate
Pentose phosphate
Pentose-5-phosphate
Glycosyl compound
N-glycosyl compound
6-aminopurine
Monosaccharide phosphate
Pentose monosaccharide
Imidazopyrimidine
Purine
Aminopyrimidine
Monoalkyl phosphate
Monosaccharide
N-substituted imidazole
Organic phosphoric acid derivative
Phosphoric acid ester
Imidolactam
Alkyl phosphate
Pyrimidine
Tetrahydrofuran
Organic sulfuric acid or derivatives
Azole
Imidazole
Heteroaromatic compound
Secondary alcohol
Organoheterocyclic compound
Azacycle
Oxacycle
Organooxygen compound
Organic nitrogen compound
Hydrocarbon derivative
Alcohol
Organic oxide
Organic oxygen compound
Primary amine
Amine
Organonitrogen compound
Organopnictogen compound
Aromatic heteropolycyclic compound

Molecular Framework

Aromatic heteropolycyclic compounds

External Descriptors

acyl sulfate (CHEBI:17980 )
adenosine bisphosphate (CHEBI:17980 )
purine ribonucleoside bisphosphate (CHEBI:17980 )
Coenzymes (C00053 )

Ontology

Disposition

Source:

Endogenous

Biological location:

Organ and components:

Cell and elements:

Element:

Platelet

Subcellular:

Golgi

Process

Naturally occurring process:

Biological process:

Biochemical pathway:

Role

Industrial application:

Pharmaceutical industry:

Pharmaceutical

Physical Properties

State

Solid

Experimental Properties

Property	Value	Reference
Melting Point	Not Available	Not Available
Boiling Point	Not Available	Not Available
Water Solubility	Not Available	Not Available
LogP	Not Available	Not Available

Predicted Properties

Property	Value	Source
Water Solubility	5.05 g/L	ALOGPS
logP	-0.65	ALOGPS
logP	-5.7	ChemAxon
logS	-2	ALOGPS
pKa (Strongest Acidic)	-2.4	ChemAxon
pKa (Strongest Basic)	3.94	ChemAxon
Physiological Charge	-4	ChemAxon
Hydrogen Acceptor Count	14	ChemAxon
Hydrogen Donor Count	6	ChemAxon
Polar Surface Area	275.97 Å²	ChemAxon
Rotatable Bond Count	8	ChemAxon
Refractivity	94.93 m³·mol⁻¹	ChemAxon
Polarizability	39.26 Å³	ChemAxon
Number of Rings	3	ChemAxon
Bioavailability	No	ChemAxon
Rule of Five	No	ChemAxon
Ghose Filter	No	ChemAxon
Veber's Rule	No	ChemAxon
MDDR-like Rule	Yes	ChemAxon

Spectra

Spectrum Type	Description	Splash Key	View
Predicted GC-MS	Predicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positive	splash10-0002-8930200000-a2821e129c20bee87c33	Spectrum
Predicted GC-MS	Predicted GC-MS Spectrum - GC-MS (1 TMS) - 70eV, Positive	splash10-0002-9441110000-619798b0c3242743c13a	Spectrum
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 10V, Positive	splash10-000i-2901410000-afa8a71104e69c842868	Spectrum
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 20V, Positive	splash10-000i-0900200000-8f9317ccb6340a4317c4	Spectrum
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 40V, Positive	splash10-000i-1900000000-e2c92e775605a11d728e	Spectrum
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 10V, Negative	splash10-0a7i-4900240000-500302d146b6d356a0b8	Spectrum
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 20V, Negative	splash10-0059-5900100000-07e0047589df3afabbbd	Spectrum
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 40V, Negative	splash10-004i-9500000000-517ff9b08c8f8999b922	Spectrum

Biological Properties

Cellular Locations

Golgi apparatus

Biospecimen Locations

Not Available

Tissue Locations

Kidney
Liver
Platelet

Pathways

Name	SMPDB/Pathwhiz	KEGG
Sulfate/Sulfite Metabolism
Sulfite oxidase deficiency		Not Available
Sphingolipid Metabolism
Gaucher Disease		Not Available
Globoid Cell Leukodystrophy		Not Available

Normal Concentrations

Not Available

Abnormal Concentrations

Not Available

Associated Disorders and Diseases

Disease References

None

Associated OMIM IDs

None

External Links

DrugBank ID

DB02902

Phenol Explorer Compound ID

Not Available

FooDB ID

KNApSAcK ID

Chemspider ID

KEGG Compound ID

BioCyc ID

BiGG ID

Wikipedia Link

3'-Phosphoadenosine-5'-phosphosulfate

METLIN ID

6028

PubChem Compound

10214

PDB ID

Not Available

ChEBI ID

17980

Food Biomarker Ontology

Not Available

VMH ID

PAPS

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. J. Am. Chem. Soc., 1995, 117 (30), pp 8031-8032

Material Safety Data Sheet (MSDS)

Not Available

General References

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. [PubMed:9292045 ]
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. [PubMed:9104734 ]
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. [PubMed:11703349 ]
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. [PubMed:8646233 ]
Khoo BY, Sit KH, Wong KP: Does PAPS generation determine the overall sulfate conjugation in human platelets? Life Sci. 1988;42(23):2389-95. [PubMed:3131608 ]
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. [PubMed:1846073 ]
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. [PubMed:2311482 ]
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. [PubMed:2612547 ]
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. [PubMed:6755828 ]

Only showing the first 10 proteins. There are 42 proteins in total.

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Enzymes

Enzyme Details

1. Ectonucleotide pyrophosphatase/phosphodiesterase family member 1

General function:: Involved in catalytic activity
Specific function:: Involved primarily in ATP hydrolysis at the plasma membrane. Plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. In vitro, has a broad specificity, hydrolyzing other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity.
Gene Name:: ENPP1
Uniprot ID:: P22413
Molecular weight:: 104923.58

Reactions

Phosphoadenosine phosphosulfate + Water → Oat gum + Adenosine 3',5'-diphosphate	details

Enzyme Details

2. Ectonucleotide pyrophosphatase/phosphodiesterase family member 3

General function:: Involved in catalytic activity
Specific function:: Cleaves a variety of phosphodiester and phosphosulfate bonds including deoxynucleotides, nucleotide sugars, and NAD (By similarity).
Gene Name:: ENPP3
Uniprot ID:: O14638
Molecular weight:: 100123.54

Reactions

Phosphoadenosine phosphosulfate + Water → Oat gum + Adenosine 3',5'-diphosphate	details

Enzyme Details

3. Carbohydrate sulfotransferase 11

General function:: Involved in sulfotransferase activity
Specific function:: Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Can also sulfate Gal residues in desulfated dermatan sulfate. Preferentially sulfates in GlcA->GalNAc unit than in IdoA->GalNAc unit. Does not form 4, 6-di-O-sulfated GalNAc when chondroitin sulfate C is used as an acceptor.
Gene Name:: CHST11
Uniprot ID:: Q9NPF2
Molecular weight:: 41002.97

Reactions

Phosphoadenosine phosphosulfate + Chondroitin → Adenosine 3',5'-diphosphate + chondroitin 4'-sulfate	details
Phosphoadenosine phosphosulfate + Chondroitin → Adenosine 3',5'-diphosphate + Chondroitin 4-sulfate	details

Enzyme Details

4. Carbohydrate sulfotransferase 3

General function:: Involved in sulfotransferase activity
Specific function:: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Can also sulfate Gal residues of keratan sulfate, another glycosaminoglycan, and the Gal residues in sialyl N-acetyllactosamine (sialyl LacNAc) oligosaccharides. May play a role in the maintenance of naive T-lymphocytes in the spleen.
Gene Name:: CHST3
Uniprot ID:: Q7LGC8
Molecular weight:: 54705.5

Reactions

Phosphoadenosine phosphosulfate + Chondroitin → Adenosine 3',5'-diphosphate + Chondroitin 6-sulfate	details

Enzyme Details

5. Carbohydrate sulfotransferase 13

General function:: Involved in sulfotransferase activity
Specific function:: Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Transfers sulfate to the C4 hydroxyl of beta1,4-linked GalNAc that is substituted with a beta-linked glucuronic acid at the C-3 hydroxyl. No activity toward dermatan.
Gene Name:: CHST13
Uniprot ID:: Q8NET6
Molecular weight:: 38919.34

Reactions

Phosphoadenosine phosphosulfate + Chondroitin → Adenosine 3',5'-diphosphate + chondroitin 4'-sulfate	details
Phosphoadenosine phosphosulfate + Chondroitin → Adenosine 3',5'-diphosphate + Chondroitin 4-sulfate	details

Enzyme Details

6. Carbohydrate sulfotransferase 12

General function:: Involved in sulfotransferase activity
Specific function:: Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin and desulfated dermatan sulfate. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Activity toward partially desulfated dermatan sulfate is however lower. Does not form 4, 6-di-O-sulfated GalNAc when chondroitin sulfate C is used as an acceptor.
Gene Name:: CHST12
Uniprot ID:: Q9NRB3
Molecular weight:: 48413.945

Reactions

Phosphoadenosine phosphosulfate + Chondroitin → Adenosine 3',5'-diphosphate + chondroitin 4'-sulfate	details
Phosphoadenosine phosphosulfate + Chondroitin → Adenosine 3',5'-diphosphate + Chondroitin 4-sulfate	details

Enzyme Details

7. Galactosylceramide sulfotransferase

General function:: Involved in galactosylceramide sulfotransferase activity
Specific function:: Catalyzes the sulfation of membrane glycolipids. Seems to prefer beta-glycosides at the non-reducing termini of sugar chains attached to a lipid moiety. Catalyzes the synthesis of galactosylceramide sulfate (sulfatide), a major lipid component of the myelin sheath and of monogalactosylalkylacylglycerol sulfate (seminolipid), present in spermatocytes (By similarity). Also acts on lactosylceramide, galactosyl 1-alkyl-2-sn-glycerol and galactosyl diacylglycerol (in vitro).
Gene Name:: GAL3ST1
Uniprot ID:: Q99999
Molecular weight:: 48763.63

Reactions

Phosphoadenosine phosphosulfate + a galactosylceramide → Adenosine 3',5'-diphosphate + a galactosylceramidesulfate	details
Phosphoadenosine phosphosulfate + monogalactosylalkylacylglycerol → Adenosine 3',5'-diphosphate + monogalactosylalkylacylglycerol sulfate	details
Phosphoadenosine phosphosulfate + Galactosylceramide → Adenosine 3',5'-diphosphate + Sulfatide	details
Phosphoadenosine phosphosulfate + Digalactosylceramide → Adenosine 3',5'-diphosphate + Digalactosylceramidesulfate	details

Enzyme Details

8. Heparan sulfate glucosamine 3-O-sulfotransferase 3B1

General function:: Involved in sulfotransferase activity
Specific function:: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to an N-unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate. Catalyzes the O-sulfation of glucosamine in IdoUA2S-GlcNS and also in IdoUA2S-GlcNH2. The substrate-specific O-sulfation generates an enzyme-modified heparan sulfate which acts as a binding receptor to Herpes simplex virus-1 (HSV-1) and permits its entry. Unlike 3-OST-1, does not convert non-anticoagulant heparan sulfate to anticoagulant heparan sulfate.
Gene Name:: HS3ST3B1
Uniprot ID:: Q9Y662
Molecular weight:: 43323.605

Reactions

Phosphoadenosine phosphosulfate + [heparan sulfate]-glucosamine → Adenosine 3',5'-diphosphate + [heparan sulfate]-glucosamine 3-sulfate	details

Enzyme Details

9. Heparan sulfate glucosamine 3-O-sulfotransferase 3A1

General function:: Involved in sulfotransferase activity
Specific function:: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to an N-unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate. Catalyzes the O-sulfation of glucosamine in IdoUA2S-GlcNS and also in IdoUA2S-GlcNH2. The substrate-specific O-sulfation generates an enzyme-modified heparan sulfate which acts as a binding receptor to Herpes simplex virus-1 (HSV-1) and permits its entry. Unlike 3-OST-1, does not convert non-anticoagulant heparan sulfate to anticoagulant heparan sulfate.
Gene Name:: HS3ST3A1
Uniprot ID:: Q9Y663
Molecular weight:: 44899.155

Reactions

Phosphoadenosine phosphosulfate + [heparan sulfate]-glucosamine → Adenosine 3',5'-diphosphate + [heparan sulfate]-glucosamine 3-sulfate	details

Enzyme Details

10. Sulfotransferase 1A1

General function:: Involved in sulfotransferase activity
Specific function:: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. Has also estrogen sulfotransferase activity. responsible for the sulfonation and activation of minoxidil. Is Mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and could so participate as modulating factor of cancer risk.
Gene Name:: SULT1A1
Uniprot ID:: P50225
Molecular weight:: 34165.13

Reactions

Phosphoadenosine phosphosulfate + a phenol → Adenosine 3',5'-diphosphate + an aryl sulfate	details
Phosphoadenosine phosphosulfate + Phenol → Adenosine 3',5'-diphosphate + Phenol sulphate	details

Only showing the first 10 proteins. There are 42 proteins in total.

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Showing metabocard for Phosphoadenosine phosphosulfate (HMDB0001134)

Structure for HMDB0001134 (Phosphoadenosine phosphosulfate)

Enzymes

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