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Literature summary for 2.7.11.19 extracted from

  • Hayakawa, T.; Perkins, J.P.; Krebs, E.G.
    Studies of the subunit structure of rabbit skeletal muscle phosphorylase kinase (1973), Biochemistry, 12, 574-580.
    View publication on PubMed
Search for more literature for 2.7.11.19

Activating Compound

Activating Compound Comment Organism Structure
additional information autophosphorylation Oryctolagus cuniculus
additional information phosphorylation by protein kinases Oryctolagus cuniculus
additional information the nonactivated enzyme is activated either by limited proteolysis 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
-

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
-
 ?

Subunits

Subunits Comment Organism
More partial amino acid composition of subunits Oryctolagus cuniculus

Cofactor

Cofactor Comment Organism Structure
ATP activation of nonactivated enzyme by phosphorylation of subunits A and B, not C Oryctolagus cuniculus