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Literature summary extracted from

  • Farrar, Y.J.K.; Carlson, G.M.
    Kinetic characterization of the calmodulin-activated catalytic subunit of phosphorylase kinase (1991), Biochemistry, 30, 10274-10279.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.11.19 5'-adenylylimidodiphosphate substrate-directed dead end inhibitor Oryctolagus cuniculus
2.7.11.19 MgADP- product inhibition Oryctolagus cuniculus
2.7.11.19 Phosphotetradecapeptide product inhibition Oryctolagus cuniculus
2.7.11.19 Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Asp-Val-Arg-Gly-Leu substrate-directed dead end inhibitor Oryctolagus cuniculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.11.19 0.47
-
tetradecapeptide
-
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
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.11.19 2 ATP + phosphorylase b = 2 ADP + phosphorylase a mechanism Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.11.19 skeletal muscle
-
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
-
?
2.7.11.19 ATP + synthetic tetradecapeptide i.e. Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu Oryctolagus cuniculus ?
-
?
2.7.11.19 ATP + synthetic tetradecapeptide substrate for holoenzyme and for catalytic gamma subunit Oryctolagus cuniculus ?
-
?