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Literature summary for 2.7.11.19 extracted from

  • Yeoman, S.J.; Cohen, P.
    The hormonal control of activity of skeletal muscle phosphorylase kinase. Phosphorylation of the enzyme at two sites in vivo in response to adrenalin (1975), Eur. J. Biochem., 51, 93-104.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+
-
Oryctolagus cuniculus
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
-
-
-

Purification (Commentary)

Purification (Comment) Organism
as in vivo activated phosphorylase sa 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 r Oryctolagus cuniculus ADP + phosphorylase a
-
?
ATP + phosphorylase b cosubstrate: Mg-ATP complex Oryctolagus cuniculus ADP + phosphorylase a
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
activity ratios at pH 6.8/8.2: 0.01-0.02 (phosphorylase kinase a), 0.36 (phosphorylase kinase sa), 0.67 (phosphorylase kinase a') Oryctolagus cuniculus