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Literature summary for 2.7.1.25 extracted from

  • Harjes, S.; Bayer, P.; Scheidig, A.J.
    The crystal structure of human PAPS synthetase 1 reveals asymmetry in substrate binding (2005), J. Mol. Biol., 347, 623-635.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
71000
-
2 * 71000, asymmetric complex, only one monomer is occupied by a bound ATP or ADP, crystal structure analysis Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + adenosine 5'-phosphosulfate Homo sapiens synthesis of the important sulfate donor 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate, decreased activity leads to defects in skeleton ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens O43252
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + adenosine 5'-phosphosulfate
-
Homo sapiens ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
?
ATP + adenosine 5'-phosphosulfate synthesis of the important sulfate donor 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate, decreased activity leads to defects in skeleton Homo sapiens ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
?

Subunits

Subunits Comment Organism
dimer 2 * 71000, asymmetric complex, only one monomer is occupied by a bound ATP or ADP, crystal structure analysis Homo sapiens

Synonyms

Synonyms Comment Organism
More bifunctional enzyme with ATP sulfurylase activity and adenosine phosphosulfate kinase activity, catalyzes the formation of 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate Homo sapiens