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Literature summary 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

Activating Compound

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

Inhibitors

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

Metals/Ions

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

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.19 Oryctolagus cuniculus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.11.19 skeletal muscle
-
Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.11.19 1.1 1.3
-
Oryctolagus cuniculus

Substrates and Products (Substrate)

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.11.19 30
-
assay at Oryctolagus cuniculus