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Literature summary for 2.7.11.19 extracted from

  • Paudel, H.K.; Xu, Y.H.; Jarrett, H.W.; Carlson, G.M.
    The model calmodulin-binding peptide melittin inhibits phosphorylase kinase by interacting with its catalytic center (1993), Biochemistry, 32, 11865-11872.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Melittin model calmodulin-binding peptide, mechanism, kinetic, phosphorylase b as substrate Oryctolagus cuniculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0098
-
Melittin
-
Oryctolagus cuniculus
0.0276
-
phosphorylase b holoenzyme Oryctolagus cuniculus
0.07
-
MgATP2- ATP (+ melittin) Oryctolagus cuniculus
0.08
-
MgATP2- ATP (+ tetrapeptide) Oryctolagus cuniculus
0.0824
-
phosphorylase b gamma subunit Oryctolagus cuniculus
0.3085
-
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
-
new Zealand white
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + melittin
-
Oryctolagus cuniculus ADP + phosphomelittin
-
?
ATP + phosphorylase b cosubstrate: Mg-ATP complex Oryctolagus cuniculus ADP + phosphorylase a
-
?
ATP + tetradecapeptide
-
Oryctolagus cuniculus ADP + phosphorylated tetradecapeptide
-
?

Temperature Optimum [°C]

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0983
-
Melittin
-
Oryctolagus cuniculus
23.6
-
tetradecapeptide
-
Oryctolagus cuniculus
57.1
-
phosphorylase b
-
Oryctolagus cuniculus