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Literature summary for 2.7.7.4 extracted from

  • Deyrup, A.T.; Krishnan, S.; Singh, B.; Schwartz, N.B.
    Activity and stability of recombinant bifunctional rearranged and monofunctional domains of ATP-sulfurylase and adenosine 5'-phosphosulfate kinase (1999), J. Biol. Chem., 274, 10751-10757.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase. Full-length enzyme and its constituent adenosine 5'-phosphosulfate kinase and ATP sulfurylase domains are individually expressed and purified. Expressed protein generated from the ATP-sulfurylase domain alone is fully active in both the forward and the reverse assays. APS kinase-only recombinants exhibit no kinase activity Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase. Full-length enzyme and its constituent adenosine 5'-phosphosulfate kinase and ATP sulfurylase domains are individually expressed and purified Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + sulfate
-
Mus musculus diphosphate + adenylylsulfate
-
r

Subunits

Subunits Comment Organism
More the enzyme consists of a COOH-terminal ATP sulfurylase domain covalently linked through a nonhomologous intervening sequence to an NH2-terminal adenosine 5'-phosphosulfate kinase domain forming a bifunctional fused protein Mus musculus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25
-
2 h, wild-type enzyme and individually expressed ATP sulfurylase domain of the bifunctional are stable Mus musculus
37
-
2 h, wild-type enzyme is stable, individually expressed ATP sulfurylase domain of the bifunctional enzyme loses 98% of its activity Mus musculus