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Literature summary extracted from

  • Dairou, J.; Pluvinage, B.; Noiran, J.; Petit, E.; Vinh, J.; Haddad, I.; Mary, J.; Dupret, J.M.; Rodrigues-Lima, F.
    Nitration of a critical tyrosine residue in the allosteric inhibitor site of muscle glycogen phosphorylase impairs its catalytic activity (2007), J. Mol. Biol., 372, 1009-1021.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.1 peroxynitrite the peroxynitrite-dependent inactivation of the enzyme could be due to the nitration of Tyr613, a key amino acid of the allosteric inhibitor site of the enzyme. Glycogen phosphorylase functions may be regulated by tyrosine nitration Mus musculus
2.4.1.1 peroxynitrite the peroxynitrite-dependent inactivation of the enzyme could be due to the nitration of Tyr613, a key amino acid of the allosteric inhibitor site of the enzyme. Glycogen phosphorylase functions may be regulated by tyrosine nitration Oryctolagus cuniculus

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.1
-
 Mus musculus
2.4.1.1
-
 Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.1.1 C2C12 cell cultured Mus musculus
-
2.4.1.1 muscle
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.1 glycogen + phosphate
-
 Mus musculus glycogen + glucose 1-phosphate
-
 ?
2.4.1.1 glycogen + phosphate
-
 Oryctolagus cuniculus glycogen + glucose 1-phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.1 GPb
-
 Mus musculus
2.4.1.1 GPb
-
 Oryctolagus cuniculus