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Literature summary for 2.4.1.1 extracted from

  • Buchbinder, J.L.; Fletterick, R.J.
    Role of the active site gate of glycogen phosphorylase in allosteric inhibition and substrate binding (1996), J. Biol. Chem., 271, 22305-22309.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D238A 15fold decrease in Vmax, 10fold decrease in Km for glucose 1-phosphate, 10fold increase in Ka for AMP, 10-20fold increase in Ki for glucose Oryctolagus cuniculus
D238N 15fold decrease in Vmax, 10fold decrease in Km for glucose 1-phosphate, 10fold increase in Ka for AMP, 10-20fold increase in Ki for glucose Oryctolagus cuniculus
F285L 2fold decrease in Vmax, 10fold decrease in affinity for caffeine, 3fold increase in Ka for AMP Oryctolagus cuniculus
N284A 3fold decrease in Vmax, 2fold increase in Ki for glucose Oryctolagus cuniculus
N284D 10fold reduction of Vmax, 10fold increase in Ki for glucose Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
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-
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Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
Oryctolagus cuniculus
-