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Literature summary 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)

EC Number Cloned (Comment) Organism
2.7.1.25 expresssion in Escherichia coli Mus musculus
2.7.7.4 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

EC Number Organism UniProt Comment Textmining
2.7.1.25 Mus musculus
-
 bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase
-
2.7.7.4 Mus musculus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.4 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

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 0.00016
-
 recombinant enzyme Mus musculus

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 Mus musculus ADP + 3'-phosphoadenosine 5'-phosphosulfate i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate ?
2.7.7.4 ATP + sulfate
-
 Mus musculus diphosphate + adenylylsulfate
-
 r

Subunits

EC Number Subunits Comment Organism
2.7.7.4 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]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.1.25 37
-
 no loss of activity after 2 h, recombinant enzyme Mus musculus
2.7.7.4 25
-
 2 h, wild-type enzyme and individually expressed ATP sulfurylase domain of the bifunctional are stable Mus musculus
2.7.7.4 37
-
 2 h, wild-type enzyme is stable, individually expressed ATP sulfurylase domain of the bifunctional enzyme loses 98% of its activity Mus musculus