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Literature summary 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

EC Number Activating Compound Comment Organism Structure
2.7.11.19 cAMP dependent on Oryctolagus cuniculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.11.19 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

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

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.1 Oryctolagus cuniculus
-
 glycogen phosphorylase b
-
2.7.11.19 Oryctolagus cuniculus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.11.19 DEAE Toyopearl 650M column chromatography Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.1.1 skeletal muscle
-
 Oryctolagus cuniculus
-
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 + glycogen phosphorylase b PhK catalyzes the Ca2+- and cAMP-dependent glycogen phosphorylase b phosphorylation and activation Oryctolagus cuniculus ADP + phosphorylated glycogen phosphorylase b
-
 ?

Synonyms

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

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.11.19 ATP
-
 Oryctolagus cuniculus

General Information

EC Number General Information Comment Organism
2.4.1.1 physiological function molecular crowding by 1 M trimethylamine N-oxide stimulates phosphorylase b and phosphorylase kinase combined binding on glycogen particles. Phosphorylase kinase binding to glycogen particles containing adsorbed phosphorylase shows a two-stage character. At the initial stage, limited size particles with hydrodynamic radius of about 220 nm are formed, whereas the second stage is accompanied by linear growth of hydrodynamic radius. Flavin adenine dinucleotide selectively inhibits phosphorylase kinase binding at the second stage, while its binding in the second stage does not involve phosphorylase b Oryctolagus cuniculus