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

BRENDA support

Literature summary for 2.7.11.19 extracted from

  • Kilimann, M.; Heilmeyer, L.M.G.
    The effect of Mg2+ on the Ca2+-binding properties of non-activated phosphorylase kinase (1977), Eur. J. Biochem., 73, 191-197.
    View publication on PubMed
Search for more literature for 2.7.11.19

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ binding studies Oryctolagus cuniculus
Ca2+ 12 mol Ca2+ per mol (alphabetagammadelta)4 Oryctolagus cuniculus
Mg2+ requirement Oryctolagus cuniculus
Mg2+ effect of Mg2+ on Ca2+-binding properties of nonactivated enzyme at pH 6.8 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
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
 Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4
-
 pH 8.2 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
-
 ?