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Literature summary extracted from

  • Nicholls, R.
    Purification and steady-state kinetics of adenosine 5-pyrophosphate sulphurylase from bakers yeast (1977), Biochem. J., 165, 149-155.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.5 phosphate competitive Saccharomyces cerevisiae
2.7.7.5 sulfate very poor inhibition in combination with increased ionic strength Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.5 1.2
-
adenosine 5'-phosphosulfate 30°C, pH 8 Saccharomyces cerevisiae
2.7.7.5 4.9
-
phosphate 30°C, pH 8 Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.5 phosphate + adenosine 5'-phosphosulfate Saccharomyces cerevisiae
-
ADP + SO42-
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.5 Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.5
-
Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.7.5 0.8
-
purified enzyme, 30°C, pH 8 Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.5 phosphate + adenosine 5'-phosphosulfate
-
Saccharomyces cerevisiae ADP + SO42-
-
?
2.7.7.5 phosphate + adenosine 5'-phosphosulfate ping pong reaction mechanism Saccharomyces cerevisiae ADP + SO42-
-
r

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.7.5 11.7
-
phosphate 30°C, pH 8 Saccharomyces cerevisiae
2.7.7.5 167
-
sulfate 4 mM adenosine 5'-phosphosulfate, 30°C, pH 8 Saccharomyces cerevisiae