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

BRENDA support

Literature summary for 2.4.1.1 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

Inhibitors Comment Organism Structure
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
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

Organism UniProt Comment Textmining
Mus musculus
-
-
-
Oryctolagus cuniculus P00489
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Mus musculus
-
Oryctolagus cuniculus

Source Tissue

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
GPb
-
Mus musculus
GPb
-
Oryctolagus cuniculus