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Literature summary extracted from

  • Lin, K.; Hwang, P.K.; Fletterick, R.J.
    Mechanism of regulation in yeast glycogen phosphorylase (1995), J. Biol. Chem., 270, 26833-26839.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.4.1.1 Phosphorylase kinase 1000fold increase in activity after phosphorylation Saccharomyces cerevisiae

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.1 expression of wild-type and N-terminal deletion mutant glycogen phosphorylase in Escherichia coli Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.1 glucose 6-phosphate
-
 Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.1 0.86
-
 glucose 1-phosphate
-
 Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.1 Saccharomyces cerevisiae
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.4.1.1 side-chain modification
-
 Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
2.4.1.1 pyridoxal 5'-phosphate 1 pyridoxal 5'-phosphate/subunit Saccharomyces cerevisiae

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.4.1.1 0.29
-
 glucose 6-phosphate unphosphorylated glycogen phosphorylase Saccharomyces cerevisiae
2.4.1.1 4.8
-
 glucose 6-phosphate phosphorylated glycogen phosphorylase Saccharomyces cerevisiae