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Literature summary 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

EC Number Metals/Ions Comment Organism Structure
2.7.11.19 Ca2+
-
 Oryctolagus cuniculus
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
-
-
-

Purification (Commentary)

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.11.19 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