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Literature summary extracted from

  • Kyriakis, E.; Stravodimos, G.A.; Kantsadi, A.L.; Chatzileontiadou, D.S.; Skamnaki, V.T.; Leonidas, D.D.
    Natural flavonoids as antidiabetic agents. The binding of gallic and ellagic acids to glycogen phosphorylase b (2015), FEBS Lett., 589, 1787-1794.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.4.1.1 AMP allosteric activator Oryctolagus cuniculus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.1.1 determination of crystal structures of the glycogen phosphorylase b-gallic acid and glycogen phosphorylase b-ellagic acid complexes, overview Oryctolagus cuniculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.1 Caffeine
-
 Oryctolagus cuniculus
2.4.1.1 chrysin
-
 Oryctolagus cuniculus
2.4.1.1 ellagic acid competitive inhibitor with respect to the substrate, glucose-1-phoshate, and non-competitive to the allosteric activator, AMP. Ellagic acid functions with glucose in a strongly synergistic mode. Determination of crystal structures of the GPb-gallic acid and GPb-ellagic acid complexes, overview Oryctolagus cuniculus
2.4.1.1 flavopiridol
-
 Oryctolagus cuniculus
2.4.1.1 gallic acid competitive inhibitor with respect to the substrate, glucose-1-phoshate, and non-competitive to the allosteric activator, AMP Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.1 [(1->4)-alpha-D-glucosyl]n + phosphate Oryctolagus cuniculus
-
 [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.1 Oryctolagus cuniculus P00489
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.4.1.1 phosphoprotein glycogen phosphorylase a is prepared from glycogen phosphorylase b by phosphorylation through a truncated form of the catalytic subunit of rabbit skeletal muscle phosphorylase kinase Oryctolagus cuniculus

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.1 native glycogen phosphorylase b from skeletal muscle, glycogen phosphorylase a is prepared from glycogen phosphorylase b by phosphorylation Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.1.1 skeletal muscle
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.1 [(1->4)-alpha-D-glucosyl]n + phosphate
-
 Oryctolagus cuniculus [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
 r

Synonyms

EC Number Synonyms Comment Organism
2.4.1.1 glycogen phosphorylase b
-
 Oryctolagus cuniculus
2.4.1.1 GPA
-
 Oryctolagus cuniculus
2.4.1.1 GPb
-
 Oryctolagus cuniculus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.1 30
-
 assay at, glycogen synthesis Oryctolagus cuniculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.1 6.8
-
 assay at, glycogen synthesis Oryctolagus cuniculus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.4.1.1 1.73
-
 ellagic acid pH 6.8, 30°C Oryctolagus cuniculus
2.4.1.1 13.4
-
 gallic acid pH 6.8, 30°C Oryctolagus cuniculus