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Literature summary for 2.4.1.11 extracted from

  • Mitchell, J.W.; Thomas, J.A.
    Phosphorylation of bovine heart glycogen synthase by two protein kinases. Kinetic properties of phosphorylated forms of the enzyme (1981), J. Biol. Chem., 256, 6160-6169.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
glucose 6-phosphate synthase D, i.e. phosphorylated form, is glucose 6-phosphate dependent, synthase I, i.e. dephosphorylated form, is glucose 6-phosphate independent, interconversion of D and I forms and vice versa Bos taurus
SO42- stimulatory effect increases as the enzyme becomes more phosphorylated Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information values for phosphorylated enzyme forms Bos taurus
0.9
-
UDP-glucose
-
Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-glucose + glycogen Bos taurus
-
glycogen + UDP
-
?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein phosphorylation of glucose-6-phosphate independent enzyme, i.e. I enzyme, results in glucose-6-phosphate dependent enzyme, i.e. D enzyme Bos taurus
phosphoprotein phosphorylation leads to loss of activity Bos taurus
phosphoprotein incorporation of 1-3 phosphates per subunit Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
Bos taurus
-

Storage Stability

Storage Stability Organism
-70°C, stable for at least 3 months Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-glucose + glycogen
-
Bos taurus glycogen + UDP
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
assay at Bos taurus