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Literature summary for 2.7.11.19 extracted from

  • Xu, Y.H.; Wilkinson, D.A.; Carlson, G.M.
    Divalent cations but not other activators enhance phosphorylase kinases affinity for glycogen phosphorylase (1996), Biochemistry, 35, 5014-5021.
    View publication on PubMed
Search for more literature for 2.7.11.19

Activating Compound

Activating Compound Comment Organism Structure
glycogen activation Oryctolagus cuniculus
glycogen increases apparent affinity for phosphorylase b Oryctolagus cuniculus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ stimulates phosphorylase b binding to enzyme, but to a considerable lesser extent than Mg2+ Oryctolagus cuniculus
Mg2+ requirement Oryctolagus cuniculus
Mg2+ greatly enhances affinity for phosphorylase b Oryctolagus cuniculus
Mg2+ major role of Mg2+: cosubstrate in Mg2+-ATP complex Oryctolagus cuniculus
Mn2+ requirement Oryctolagus cuniculus
Mn2+ enhances enzyme/phosphorylase b interaction more effectively Oryctolagus cuniculus
phosphate requirement, phosphate containing enzyme Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
 new Zealand white
-

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 + phosphorylase b binding studies with immobilized substrate Oryctolagus cuniculus ADP + phosphorylase a
-
 ?
ATP + phosphorylase b rabbit skeletal muscle Oryctolagus cuniculus ADP + phosphorylase a
-
 ?