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Literature summary for 2.7.1.25 extracted from

  • Schwenn, J.D.; Jender, H.G.
    A kinetic investigation of the APS-kinase from chlamydomonas reinhardii CW 15 (1981), Phytochemistry, 20, 601-604.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
adenosine 5'-phosphosulfate substrate inhibition above 0.03-0.04 mM Chlamydomonas reinhardtii
ATP in the absence of ATP regenerating system, substrate inhibition above 0.6 mM, in the presence of ATP regenerating system, substrate inhibition above 0.2 mM Chlamydomonas reinhardtii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.006
-
adenosine 5'-phosphosulfate pH 8.0 Chlamydomonas reinhardtii
0.05 0.06 ATP pH 8.0 Chlamydomonas reinhardtii

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activation Chlamydomonas reinhardtii

Organism

Organism UniProt Comment Textmining
Chlamydomonas reinhardtii
-
CW15, cell wall mutant
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate, Sephacryl S-200, partially purified Chlamydomonas reinhardtii

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.002 0.006
-
Chlamydomonas reinhardtii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + adenosine 5-phosphosulfate i.e. adenylylsulfate or APS Chlamydomonas reinhardtii ADP + 3'-phosphoadenosine 5'-phosphosulfate i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate r