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Literature summary for 2.7.11.19 extracted from

  • Ashida, M.; Wyatt, G.R.
    Properties and activation of phosphorylase kinase from silkmoth fat body (1979), Insect Biochem., 9, 403-409.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
EGTA partial Hyalophora cecropia

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Hyalophora cecropia

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ requirement Hyalophora cecropia
Mg2+ requirement Hyalophora cecropia
Mg2+ major role of Mg2+: cosubstrate in Mg2+-ATP complex Hyalophora cecropia
phosphate requirement, phosphate containing enzyme Hyalophora cecropia

Organism

Organism UniProt Comment Textmining
Hyalophora cecropia
-
silk moth
-

Source Tissue

Source Tissue Comment Organism Textmining
fat body pupae Hyalophora cecropia
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + nonactivated phosphorylase kinase in the presence of Mg2+ and Ca2+ Hyalophora cecropia ADP + activated phosphorylase kinase
-
?
ATP + phosphorylase b cosubstrate: Mg-ATP complex Hyalophora cecropia ADP + phosphorylase a
-
?
ATP + phosphorylase b rabbit skeletal muscle Hyalophora cecropia ADP + phosphorylase a
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Hyalophora cecropia