Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.11.19 extracted from

  • Crabb, J.W.; Harris, W.R.; Johnson, C.M.; Sotiroudis, T.G.; Kuhn, C.C.; Heilmeyer, L.M.G.
    Electrophoretic purification of the alpha and beta subunits of phosphorylase kinase and evidence in support of the deduced amino acid sequences (1990), Electrophoresis, 11, 133-140.
    View publication on PubMed
Search for more literature for 2.7.11.19

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
-
-
-

Purification (Commentary)

Purification (Comment) Organism
alpha, alpha' and beta subunits by preparative SDS-PAGE 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 cosubstrate: Mg-ATP complex Oryctolagus cuniculus ADP + phosphorylase a
-
 ?

Subunits

Subunits Comment Organism
More alpha' Oryctolagus cuniculus
More amino acid sequence of alpha, beta Oryctolagus cuniculus