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Literature summary for 2.7.7.4 extracted from

  • Mueller, J.W.; Shafqat, N.
    Adenosine-5-phosphosulfate - a multifaceted modulator of bifunctional 3-phospho-adenosine-5-phosphosulfate synthases and related enzymes (2013), FEBS J., 280, 3050-3057.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
PAPSS1 crystal structures analysis, PDB IDs 2GIF, 2OFW, 1XNJ, and 2PEY Homo sapiens

General Stability

General Stability Organism
adenylyl sulfate, APS, is a highly specific stabilizer of bifunctional PAPS synthases. APS most likely stabilizes the APS kinase part of these proteins by forming a dead-end enzyme-ADP-APS complex at APS concentrations between 0.0005 and 0.005 mM. At higher concentrations, APS may bind to the catalytic centers of ATP sulfurylase Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
adenylyl sulfate APS, binding mode, overview. On the ATP sulfurylase domain that initially produces APS from sulfate and ATP, APS acts as a potent product inhibitor, being competitive with both ATP and sulfate. For the APS kinase domain that phosphorylates APS to PAPS, APS is an uncompetitive substrate inhibitor that can bind both at the ATP/ADP-binding site and the PAPS/APS-binding site; APS, binding mode, overview. On the ATP sulfurylase domain that initially produces APS from sulfate and ATP, APS acts as a potent product inhibitor, being competitive with both ATP and sulfate. For the APS kinase domain that phosphorylates APS to PAPS, APS is an uncompetitive substrate inhibitor that can bind both at the ATP/ADP-binding site and the PAPS/APS-binding site Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + sulfate Homo sapiens
-
diphosphate + adenylyl sulfate
-
?
diphosphate + adenylyl sulfate Homo sapiens
-
ATP + sulfate
-
r
additional information Homo sapiens for human PAPS synthase 1, the steady-state concentration of APS is modelled to be 0.0016 mM, but this may increase up to 0.060 mM under conditions of sulfate excess. The APS concentration for maximal APS kinase activity is 0.015 mM ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens O43252 PAPS synthase 1
-
Homo sapiens O95340 PAPS synthase 2
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + sulfate
-
Homo sapiens diphosphate + adenylyl sulfate
-
?
diphosphate + adenylyl sulfate
-
Homo sapiens ATP + sulfate
-
r
additional information substrate binding structure analysis, overview Homo sapiens ?
-
?
additional information for human PAPS synthase 1, the steady-state concentration of APS is modelled to be 0.0016 mM, but this may increase up to 0.060 mM under conditions of sulfate excess. The APS concentration for maximal APS kinase activity is 0.015 mM Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
dimer the bifunctional PAPS synthase comprises a C-terminal ATP sulfurylase domain and an N-terminal APS kinase domain connected by a short irregular linker Homo sapiens

Synonyms

Synonyms Comment Organism
ATP sulfurylase
-
Homo sapiens
PAPS synthase 1
-
Homo sapiens
PAPS synthase 2
-
Homo sapiens
PAPSS1
-
Homo sapiens

General Information

General Information Comment Organism
metabolism all sulfation reactions rely on active sulfate in the form of 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Sulfate is converted to the sulfonucleotide adenylyl sulfate, APS, by the ubiquitous ATP sulfurylase. APS represents a metabolic branchpoint in bacteria and plants, where it is reduced by APS reductase to sulfite, and finally incorporated into primary metabolites after further reduction. Alternatively, APS is phosphorylated by APS kinase to the universal sulfate donor PAPS. In metazoans and humans, ATP sulfurylase and APS kinase reside on one polypeptide, the bifunctional PAPS synthase. All eukaryotic sulfotransferases depend on the provision of active sulfate inthe form of 3'-phospho-adenosine-5'-phosphosulfate (PAPS) for their proper action. The importance of PAPS for sulfation can rival that of ATP for phosphorylation processes. Various regulatory roles of APS in the overall process of PAPS biosynthesis Homo sapiens
metabolism all sulfation reactions rely on active sulfate in the form of 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Sulfate is converted to the sulfonucleotide adenylyl sulfate, APS, by the ubiquitous ATP sulfurylase. APS represents a metabolic branchpoint in bacteria and plants, where it is reduced by APS reductase to sulfite, and finally incorporated into primary metabolites after further reduction. Alternatively, APS is phosphorylated by APS kinase to the universal sulfate donor PAPS. In metazoans and humans, ATP sulfurylase and APS kinase reside on one polypeptide, the bifunctional PAPS synthase. All eukaryotic sulfotransferases depend on the provision of active sulfate inthe form of 3?-phospho-adenosine-5'-phosphosulfate (PAPS) for their proper action. The importance of PAPS for sulfation can rival that of ATP for phosphorylation processes. Various regulatory roles of APS in the overall process of PAPS biosynthesis Homo sapiens
additional information the bifunctional PAPS synthase comprises a C-terminal ATP sulfurylase domain and an N-terminal APS kinase domain connected by a short irregular linker, no intermediate channeling by the human enzyme. The human PAPS synthases, PAPS synthase 1 (PAPSS1) and PAPS synthase 2 (PAPSS2) are bifunctional enzymes that consist of ATP sulfurylase and APS kinase domains connected by a flexible linker. Adenylyl sulfate, APS, is a highly specific stabilizer of bifunctional PAPS synthases. APS most likely stabilizes the APS kinase part of these proteins by forming a dead-end enzyme-ADP-APS complex at APS concentrations between 0.0005 and 0.005 mM. At higher concentrations, APS may bind to the catalytic centers of ATP sulfurylase Homo sapiens