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Literature summary for 2.7.11.19 extracted from

  • Cox, D.E.; Meinke, M.H.; Edstrom, R.D.
    Mechanism of calmodulin inhibition of cAMP-dependent protein kinase activation of phosphorylation kinase (1987), Arch. Biochem. Biophys., 259, 350-362.
    View publication on PubMed
Search for more literature for 2.7.11.19

Activating Compound

Activating Compound Comment Organism Structure
Catalytic subunit of cAMP-dependent protein kinase activation of nonactivated enzyme Oryctolagus cuniculus
Catalytic subunit of cAMP-dependent protein kinase kinetics Oryctolagus cuniculus

Inhibitors

Inhibitors Comment Organism Structure
Calmodulin inhibits cAMP-dependent protein kinase mediated activation of phosphorylase kinase, kinetics Oryctolagus cuniculus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ requirement Oryctolagus cuniculus
Mg2+ major role of Mg2+: cosubstrate in Mg2+-ATP complex Oryctolagus cuniculus
phosphate requirement, phosphate containing enzyme Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
 Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1 1.3
-
 Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + phosphorylase b cosubstrate: Mg-ATP complex Oryctolagus cuniculus ADP + phosphorylase a
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Oryctolagus cuniculus