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Literature summary for 2.7.11.19 extracted from

  • Chebotareva, N.A.; Meremyanin, A.V.; Makeeva, V.F.; Eronina, T.B.; Kurganov, B.I.
    Glycogen phosphorylase b and phosphorylase kinase binding to glycogen under molecular crowding conditions. Inhibitory effect of FAD (2009), Biochemistry, 74, 562-568.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
cAMP dependent on Oryctolagus cuniculus

Inhibitors

Inhibitors Comment Organism Structure
FAD FAD at high concentrations completely inhibits the second stage of enzyme binding to glycogen particles containing glycogen phosphorylase b, the inhibitory effect of FAD is not complete and reaches a maximal value at FAD concentrations around 0.03 mM Oryctolagus cuniculus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required for activity Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
DEAE Toyopearl 650M column chromatography 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 + glycogen phosphorylase b PhK catalyzes the Ca2+- and cAMP-dependent glycogen phosphorylase b phosphorylation and activation Oryctolagus cuniculus ADP + phosphorylated glycogen phosphorylase b
-
?

Synonyms

Synonyms Comment Organism
EC 2.7.1.38 formerly Oryctolagus cuniculus
PhK
-
Oryctolagus cuniculus
phosphorylase kinase
-
Oryctolagus cuniculus

Cofactor

Cofactor Comment Organism Structure
ATP
-
Oryctolagus cuniculus