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Literature summary for 2.7.11.19 extracted from

  • King, M.M.; Carslon, G.M.
    Synergistic activation by Ca2+ and Mg2+ as the primary cause for hysteresis in the phosphorylase kinase reactions (1981), J. Biol. Chem., 256, 11058-11064.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
EGTA
-
Oryctolagus cuniculus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ synergism with Mg2+ Oryctolagus cuniculus
Mg2+ requirement Oryctolagus cuniculus
Mg2+ synergism with Ca2+ Oryctolagus cuniculus
Mg2+ major role of Mg2+: cosubstrate in Mg2+-ATP complex Oryctolagus cuniculus
Mg2+ required for activity phosphorylation by (cAMP-dependent protein kinase) 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
-

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
-
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