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Literature summary 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)

EC Number Cloned (Comment) Organism
2.7.1.25
-
Homo sapiens

Crystallization (Commentary)

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.1.25 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)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.25 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

EC Number Organism UniProt Comment Textmining
2.7.1.25 Homo sapiens O43252
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.25
-
Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.25 ATP + adenosine 5'-phosphosulfate
-
Homo sapiens ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
?
2.7.1.25 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

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

Synonyms

EC Number Synonyms Comment Organism
2.7.1.25 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