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Literature summary extracted from

  • Robbins, P.W.; Lipmann, F.
    The enzymatic sequence in the biosynthesis of active sulfate (1956), J. Am. Chem. Soc., 78, 6409-6410.
No PubMed abstract available

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.25 Mg2+ activation Saccharomyces cerevisiae
2.7.1.25 additional information a divalent cation is required for activity Saccharomyces cerevisiae
2.7.7.4 Mg2+ or an other divalent cation required Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.25 Saccharomyces cerevisiae
-
-
-
2.7.7.4 Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.25 partial Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.1.25 0.208
-
-
Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.25 ATP + adenosine 5-phosphosulfate i.e. adenylylsulfate or APS Saccharomyces cerevisiae ADP + 3'-phosphoadenosine 5'-phosphosulfate i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate ?
2.7.7.4 ATP + sulfate
-
Saccharomyces cerevisiae diphosphate + adenylylsulfate
-
r