Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | enzyme is phosphorylated in embryonic muscle | Coturnix sp. |
Application | Comment | Organism |
---|---|---|
analysis | development of assay method with n-dodecyl-beta-D-maltoside as substrate | Gallus gallus |
analysis | development of assay method with n-dodecyl-beta-D-maltoside as substrate | Mus musculus |
analysis | development of assay method with n-dodecyl-beta-D-maltoside as substrate | Rattus norvegicus |
analysis | development of assay method with n-dodecyl-beta-D-maltoside as substrate | Bos taurus |
analysis | development of assay method with n-dodecyl-beta-D-maltoside as substrate | Oryctolagus cuniculus |
Cloned (Comment) | Organism |
---|---|
expression in COS cells | Oryctolagus cuniculus |
expression of glucose-free apo-glycogenin in an Escherichia coli mutant lacking UDP-glucose, enzyme is active towards itself and other substrates | Rattus norvegicus |
expression of mutant Y194F in Escherichia coli | Oryctolagus cuniculus |
Protein Variants | Comment | Organism |
---|---|---|
Y194F | mutant glycosylates other substrates with nearly the same activity as the wild-type | Rattus norvegicus |
Y194F | exchange of glucose attachment site, no autoglucosylation activity | Rattus norvegicus |
Y194F | exchange of glucose attachment site, no autoglucosylation activity | Oryctolagus cuniculus |
Y194T | exchange of glucose attachment site, no autoglucosylation activity, mutant glycosylates other substrates but with less activity compared to the wild-type | Rattus norvegicus |
General Stability | Organism |
---|---|
alkali-stable | Gallus gallus |
alkali-stable | Mus musculus |
alkali-stable | Rattus norvegicus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
ADP | skeletal muscle enzyme, allosteric inhibition of autoglucosylation | Oryctolagus cuniculus | |
ATP | skeletal muscle enzyme, allosteric inhibition of autoglucosylation, complete inhibition at 5 mM, possible role as natural regulator | Oryctolagus cuniculus | |
ATP | slight inhibition, renal enzyme | Rattus norvegicus | |
CDP | renal enzyme, 90% inhibition at 0.025 mM | Rattus norvegicus | |
CDP-choline | renal enzyme, 75% inhibition at 0.1 mM | Rattus norvegicus | |
CDP-glucose | - |
Rattus norvegicus | |
maltose | very poor, 50% inhibition at 40 mM | Bos taurus | |
maltose | very poor, 50% inhibition at 40 mM | Rattus norvegicus | |
additional information | enzyme is phosphorylated in embryonic muscle | Coturnix sp. | |
additional information | - |
Oryctolagus cuniculus | |
TDP-glucose | - |
Rattus norvegicus | |
UDP-xylose | competitive inhibitor to glucosylation of glycogenin by UDP-glucose | Rattus norvegicus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Km-values for UDP-glucose in different tissues | Gallus gallus | |
additional information | - |
additional information | Km-values for UDP-glucose in different tissues | Mus musculus | |
additional information | - |
additional information | Km-values for UDP-glucose in different tissues | Rattus norvegicus | |
additional information | - |
additional information | Km-values for UDP-glucose in different tissues | Bos taurus | |
additional information | - |
additional information | Km-values for UDP-glucose in different tissues | Oryctolagus cuniculus | |
0.1 | - |
n-dodecyl-beta-D-maltoside | - |
Rattus norvegicus | |
3 | - |
p-nitrophenyl-alpha-maltoside | - |
Rattus norvegicus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | - |
Rattus norvegicus | 5829 | - |
additional information | not membrane-bound | Rattus norvegicus | - |
- |
additional information | not membrane-bound | Bos taurus | - |
- |
additional information | not membrane-bound | Oryctolagus cuniculus | - |
- |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
32000 | - |
kidney enzyme | Rattus norvegicus |
37280 | - |
amino acid sequence determination | Oryctolagus cuniculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-glucose + glycogenin | Gallus gallus | - |
UDP + glucosylated glycogenin | - |
? | |
UDP-glucose + glycogenin | Mus musculus | - |
UDP + glucosylated glycogenin | - |
? | |
UDP-glucose + glycogenin | Bos taurus | - |
UDP + glucosylated glycogenin | - |
? | |
UDP-glucose + glycogenin | Rattus norvegicus | enzyme forms the protein part of proteoglycogen | UDP + glucosylated glycogenin | - |
? | |
UDP-glucose + glycogenin | Oryctolagus cuniculus | enzyme forms the protein part of proteoglycogen | UDP + glucosylated glycogenin | - |
? | |
UDP-glucose + glycogenin | Rattus norvegicus | regulation | UDP + glucosylated glycogenin | - |
? | |
UDP-glucose + glycogenin | Oryctolagus cuniculus | regulation | UDP + glucosylated glycogenin | - |
? | |
UDP-glucose + glycogenin | Rattus norvegicus | 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 | - |
? | |
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 |
---|---|---|---|
Bos taurus | - |
- |
- |
Coturnix sp. | - |
Quail | - |
Gallus gallus | - |
hen | - |
Mus musculus | - |
- |
- |
Oryctolagus cuniculus | - |
- |
- |
Rattus norvegicus | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | 1 single glucose attachment site at tyrosine-194 | Oryctolagus cuniculus |
glycoprotein | autoglycosylation | Gallus gallus |
glycoprotein | autoglycosylation | Mus musculus |
glycoprotein | autoglycosylation | Rattus norvegicus |
glycoprotein | autoglycosylation | Oryctolagus cuniculus |
glycoprotein | one attached glucose molecule is needed for intramolecular self-glucosylation | Rattus norvegicus |
Purification (Comment) | Organism |
---|---|
separation from glycogen synthase, EC 2.4.1.11, by LiBr | Oryctolagus cuniculus |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin | highly conserved protein | Rattus norvegicus | |
UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin | highly conserved protein | Bos taurus | |
UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin | highly conserved protein | Oryctolagus cuniculus | |
UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin | stereochemistry and mechanism | Rattus norvegicus | |
UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin | stereochemistry and mechanism | Bos taurus | |
UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin | stereochemistry and mechanism | Oryctolagus cuniculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
embryo | - |
Coturnix sp. | - |
kidney | - |
Rattus norvegicus | - |
kidney | - |
Bos taurus | - |
kidney | - |
Oryctolagus cuniculus | - |
liver | - |
Rattus norvegicus | - |
liver | - |
Oryctolagus cuniculus | - |
mastocytoma cell | - |
Mus musculus | - |
additional information | a glycogenin-like protein has also been found in retina | Bos taurus | - |
additional information | enzyme activity does not depend on physiological state of the organism | Rattus norvegicus | - |
additional information | enzyme activity does not depend on physiological state of the organism | Oryctolagus cuniculus | - |
additional information | a glycogenin-like protein has also been found in thymus, brain, heart | Rattus norvegicus | - |
oviduct | - |
Gallus gallus | - |
skeletal muscle | - |
Rattus norvegicus | - |
skeletal muscle | - |
Bos taurus | - |
skeletal muscle | - |
Oryctolagus cuniculus | - |
skeletal muscle | - |
Coturnix sp. | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
CDP-glucose + glycogenin | recombinant enzyme expressed in E. coli, 71% activity compared to UDP-glucose | Rattus norvegicus | CDP + glucosylated glycogenin | - |
? | |
CDP-glucose + p-nitrophenyl-alpha-maltoside | recombinant enzyme expressed in E. coli | Rattus norvegicus | CDP + ? | - |
? | |
TDP-glucose + glycogenin | recombinant enzyme expressed in E. coli, 33% activity compared to UDP-glucose | Rattus norvegicus | TDP + glucosylated glycogenin | - |
? | |
TDP-glucose + p-nitrophenyl-alpha-maltoside | recombinant enzyme expressed in E. coli | Rattus norvegicus | TDP + ? | - |
? | |
UDP-glucose + glycogenin | - |
Gallus gallus | UDP + glucosylated glycogenin | - |
? | |
UDP-glucose + glycogenin | - |
Mus musculus | UDP + glucosylated glycogenin | - |
? | |
UDP-glucose + glycogenin | - |
Bos taurus | UDP + glucosylated glycogenin | - |
? | |
UDP-glucose + glycogenin | autoglycosylation reaction | Gallus gallus | UDP + glucosylated glycogenin | forms glucosyl-alpha1,4-glucosyl linkage | ? | |
UDP-glucose + glycogenin | autoglycosylation reaction | Mus musculus | UDP + glucosylated glycogenin | forms glucosyl-alpha1,4-glucosyl linkage | ? | |
UDP-glucose + glycogenin | autoglycosylation reaction | Rattus norvegicus | UDP + glucosylated glycogenin | forms glucosyl-alpha1,4-glucosyl linkage | ? | |
UDP-glucose + glycogenin | autoglycosylation reaction | Bos taurus | UDP + glucosylated glycogenin | forms glucosyl-alpha1,4-glucosyl linkage | ? | |
UDP-glucose + glycogenin | autoglycosylation reaction | Oryctolagus cuniculus | UDP + glucosylated glycogenin | forms glucosyl-alpha1,4-glucosyl linkage | ? | |
UDP-glucose + glycogenin | one attached glucose molecule is needed for intramolecular self-glucosylation | Rattus norvegicus | UDP + glucosylated glycogenin | forms glucosyl-alpha1,4-glucosyl linkage | ? | |
UDP-glucose + glycogenin | enzyme forms the protein part of proteoglycogen | Rattus norvegicus | UDP + glucosylated glycogenin | - |
? | |
UDP-glucose + glycogenin | enzyme forms the protein part of proteoglycogen | Oryctolagus cuniculus | UDP + glucosylated glycogenin | - |
? | |
UDP-glucose + glycogenin | enzyme forms the protein part of proteoglycogen | Gallus gallus | UDP + glucosylated glycogenin | forms glucosyl-alpha1,4-glucosyl linkage | ? | |
UDP-glucose + glycogenin | enzyme forms the protein part of proteoglycogen | Mus musculus | UDP + glucosylated glycogenin | forms glucosyl-alpha1,4-glucosyl linkage | ? | |
UDP-glucose + glycogenin | enzyme forms the protein part of proteoglycogen | Rattus norvegicus | UDP + glucosylated glycogenin | forms glucosyl-alpha1,4-glucosyl linkage | ? | |
UDP-glucose + glycogenin | enzyme forms the protein part of proteoglycogen | Bos taurus | UDP + glucosylated glycogenin | forms glucosyl-alpha1,4-glucosyl linkage | ? | |
UDP-glucose + glycogenin | enzyme forms the protein part of proteoglycogen | Oryctolagus cuniculus | UDP + glucosylated glycogenin | forms glucosyl-alpha1,4-glucosyl linkage | ? | |
UDP-glucose + glycogenin | no activity with CDP-glucose | Rattus norvegicus | UDP + glucosylated glycogenin | forms glucosyl-alpha1,4-glucosyl linkage | ? | |
UDP-glucose + glycogenin | UDP-glucose can not be replaced by ADP- or GDP-glucose | Rattus norvegicus | UDP + glucosylated glycogenin | forms glucosyl-alpha1,4-glucosyl linkage | ? | |
UDP-glucose + glycogenin | regulation | Rattus norvegicus | UDP + glucosylated glycogenin | - |
? | |
UDP-glucose + glycogenin | regulation | Oryctolagus cuniculus | UDP + glucosylated 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 | Rattus norvegicus | UDP + glucosylated 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 | - |
? | |
UDP-glucose + n-dodecyl-beta-D-maltoside | - |
Oryctolagus cuniculus | UDP + n-dodecyl-beta-D-maltotriose | - |
? | |
UDP-glucose + n-dodecyl-beta-D-maltoside | hydrophobic nature of the aglycon is required for binding to the active site | Rattus norvegicus | UDP + n-dodecyl-beta-D-maltotriose | - |
? | |
UDP-glucose + n-dodecyl-beta-D-maltoside | hydrophobic nature of the aglycon is required for binding to the active site | Bos taurus | UDP + n-dodecyl-beta-D-maltotriose | - |
? | |
UDP-glucose + n-dodecyl-beta-D-maltoside | renal enzyme | Bos taurus | UDP + n-dodecyl-beta-D-maltotriose | - |
? | |
UDP-glucose + n-dodecyl-beta-D-maltoside | transglucosylation reaction | Rattus norvegicus | UDP + n-dodecyl-beta-D-maltotriose | - |
? | |
UDP-glucose + n-dodecyl-beta-D-maltoside | transglucosylation reaction | Bos taurus | UDP + n-dodecyl-beta-D-maltotriose | - |
? | |
UDP-glucose + n-octyl-alpha-D-maltoside | hydrophobic nature of the aglycon is required for binding to the active site | Rattus norvegicus | ? | - |
? | |
UDP-glucose + n-octyl-alpha-D-maltoside | hydrophobic nature of the aglycon is required for binding to the active site | Bos taurus | ? | - |
? | |
UDP-glucose + n-octyl-alpha-D-maltoside | transglucosylation reaction | Rattus norvegicus | ? | - |
? | |
UDP-glucose + n-octyl-alpha-D-maltoside | transglucosylation reaction | Bos taurus | ? | - |
? | |
UDP-glucose + n-octyl-beta-D-maltoside | hydrophobic nature of the aglycon is required for binding to the active site | Rattus norvegicus | ? | - |
? | |
UDP-glucose + n-octyl-beta-D-maltoside | hydrophobic nature of the aglycon is required for binding to the active site | Bos taurus | ? | - |
? | |
UDP-glucose + n-octyl-beta-D-maltoside | transglucosylation reaction | Rattus norvegicus | ? | - |
? | |
UDP-glucose + n-octyl-beta-D-maltoside | transglucosylation reaction | Bos taurus | ? | - |
? | |
UDP-glucose + n-tetradecyl-beta-D-maltoside | hydrophobic nature of the aglycon is required for binding to the active site | Rattus norvegicus | ? | - |
? | |
UDP-glucose + n-tetradecyl-beta-D-maltoside | hydrophobic nature of the aglycon is required for binding to the active site | Bos taurus | ? | - |
? | |
UDP-glucose + n-tetradecyl-beta-D-maltoside | transglucosylation reaction | Rattus norvegicus | ? | - |
? | |
UDP-glucose + n-tetradecyl-beta-D-maltoside | transglucosylation reaction | Bos taurus | ? | - |
? | |
UDP-xylose + glycogenin | autoglycosylation reaction | Gallus gallus | UDP + xylosylated glycogenin | - |
? | |
UDP-xylose + glycogenin | autoglycosylation reaction | Mus musculus | UDP + xylosylated glycogenin | - |
? | |
UDP-xylose + glycogenin | autoglycosylation reaction | Rattus norvegicus | UDP + xylosylated glycogenin | - |
? | |
UDP-xylose + glycogenin | renal and skeletal muscle glycogenin, lower activity compared to UDP-glucose | Rattus norvegicus | UDP + xylosylated glycogenin | - |
? | |
UDP-xylose + n-dodecyl-beta-D-maltoside | transglucosylation reaction | Rattus norvegicus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | in muscle a glycogen beta-particle is bound to glycogenin in a 1:1 ratio, the enzyme/glycogen ratio in liver is lower | Rattus norvegicus |
More | in muscle a glycogen beta-particle is bound to glycogenin in a 1:1 ratio, the enzyme/glycogen ratio in liver is lower | Bos taurus |
More | in muscle a glycogen beta-particle is bound to glycogenin in a 1:1 ratio, the enzyme/glycogen ratio in liver is lower | Oryctolagus cuniculus |
More | enzyme forms the protein part of proteoglycogen | Rattus norvegicus |
More | enzyme forms the protein part of proteoglycogen | Bos taurus |
More | enzyme forms the protein part of proteoglycogen | Oryctolagus cuniculus |
More | glycogenin glucosyltransferase, MW 38 kDa, represents the smaller subunit of glycogen synthase, both enzyme form a heterodimeric complex of molar ratio 1:1 | Rattus norvegicus |
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 |