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Literature summary for 2.7.11.19 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
Search for more literature for 2.7.11.19

Inhibitors

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

KM Value [mM]

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

Reaction

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

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
-
 ?
ATP + synthetic tetradecapeptide i.e. Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu Oryctolagus cuniculus ?
-
 ?
ATP + synthetic tetradecapeptide substrate for holoenzyme and for catalytic gamma subunit Oryctolagus cuniculus ?
-
 ?