Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | no inhibition by phosphorylation of catalytic subunit of the glycogen synthase complex; not inhibitory: UDP-pyridoxal, LiBr | Oryctolagus cuniculus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.002 | - |
UDP-glucose | - |
Oryctolagus cuniculus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | less effective than Mn2+ | Oryctolagus cuniculus | |
Mn2+ | absolutely dependent on divalent cations, Mn2+ can be replaced by Mg2+ with less effectivity | Oryctolagus cuniculus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
38000 | - |
gel filtration, SDS-PAGE, glycogenin glucosyltransferase represents the smaller subunit of glycogen synthase | Oryctolagus cuniculus |
124000 | - |
gel filtration, heterodimeric glycogen synthase complex | Oryctolagus cuniculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-glucose + glycogenin | Oryctolagus cuniculus | the glycogenin subunit of glycogen synthase, EC 2.4.1.11, catalyzes this reaction, i.e. the enzyme catalyzes its own glucosylation | UDP + glucosylated glycogenin | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | autoglycosylation | Oryctolagus cuniculus |
glycoprotein | five molecules of glucose can be transferred to one molecule of glycogenin, which contains already 1 glucose molecule prior to autoglycosylation | Oryctolagus cuniculus |
Purification (Comment) | Organism |
---|---|
separation from glycogen synthase, EC 2.4.1.11, by LiBr | Oryctolagus cuniculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
skeletal muscle | - |
Oryctolagus cuniculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-glucose + glycogenin | autoglycosylation reaction | Oryctolagus cuniculus | UDP + glucosylated glycogenin | glucosylation reaches a plateau, when 5 additional glucose residues have been added to glycogenin | ? | |
UDP-glucose + glycogenin | autoglycosylation reaction | Oryctolagus cuniculus | UDP + glucosylated glycogenin | i.e. primed glycogenin | ? | |
UDP-glucose + glycogenin | i.e. unprimed glycogenin | Oryctolagus cuniculus | UDP + glucosylated glycogenin | glucosylation reaches a plateau, when 5 additional glucose residues have been added to glycogenin | ? | |
UDP-glucose + glycogenin | i.e. unprimed glycogenin | Oryctolagus cuniculus | UDP + glucosylated glycogenin | i.e. primed glycogenin | ? | |
UDP-glucose + glycogenin | the glycogenin subunit of glycogen synthase, EC 2.4.1.11, catalyzes this reaction, i.e. the enzyme catalyzes its own glucosylation | Oryctolagus cuniculus | UDP + glucosylated glycogenin | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | glycogenin glucosyltransferase, MW 38 kDa, represents the smaller subunit of glycogen synthase, both enzyme form a heterodimeric complex of molar ratio 1:1 | Oryctolagus cuniculus |
Synonyms | Comment | Organism |
---|---|---|
glycogenin glycosyltransferase | - |
Oryctolagus cuniculus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Oryctolagus cuniculus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Oryctolagus cuniculus |