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Literature summary for 2.7.1.25 extracted from

  • Renosto, F.; Martin, R.L.; Segel, I.H.
    Sulfate-activating enzymes of Penicillium chrysogenum. The ATP sulfurylase.adenosine 5-phosphosulfate complex does not serve as a substrate for adenosine 5-phosphosulfate kinase (1989), J. Biol. Chem., 264, 9433-9437.
    View publication on PubMed
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0014
-
 adenosine 5'-phosphosulfate
-
 Penicillium chrysogenum

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activation Penicillium chrysogenum

Organism

Organism UniProt Comment Textmining
Penicillium chrysogenum
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate mechanism Penicillium chrysogenum
a

Source Tissue

Source Tissue Comment Organism Textmining
mycelium
-
 Penicillium chrysogenum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + adenosine 5-phosphosulfate no substrate-chanelling of adenosine 5'-phosphosulfate between ATP-sulfurylase, EC 2.7.7.4, and APS-kinase, i.e. ATP-sulfurylase-APS-complex is no substrate for the kinase Penicillium chrysogenum ADP + 3'-phosphoadenosine 5'-phosphosulfate i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate r
ATP + adenosine 5-phosphosulfate i.e. adenylylsulfate or APS Penicillium chrysogenum ADP + 3'-phosphoadenosine 5'-phosphosulfate i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate r