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Literature summary for 3.1.3.42 extracted from

  • Kato, K.; Bishop, J.S.
    Glycogen synthetase-D phosphatase. I. Some new properties of the partially purified enzyme from rabbit skeletal muscle (1972), J. Biol. Chem., 247, 7420-7429.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
galactose 6-phosphate 0.1 mM, stimulates activity Oryctolagus cuniculus
glucosamine 6-phosphate 0.1 mM, stimulates activity Oryctolagus cuniculus
glucose 6-phosphate 0.1 mM, about 2fold increase in activity Oryctolagus cuniculus

General Stability

General Stability Organism
dithiothreitol, 1.7 mM, and bovine serum albumin, 0.07%, stabilize the enzyme during assay Oryctolagus cuniculus
enzyme dialyzed against EDTA is stable to freezing and thawing in absence of Mn2+ Oryctolagus cuniculus
Mn2+, 5 mM, stabilizes Oryctolagus cuniculus

Inhibitors

Inhibitors Comment Organism Structure
diphosphate 0.2 mM Oryctolagus cuniculus
F- 10 mM Oryctolagus cuniculus
Na2SO3 1 mM, 27% inhibition Oryctolagus cuniculus
phosphate 0.2 mM Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycogen synthase D + H2O
-
Oryctolagus cuniculus glycogen synthase I + phosphate
-
?
histone phosphate + H2O
-
Oryctolagus cuniculus ?
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
57
-
4 min, 80% loss of activity Oryctolagus cuniculus