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Literature summary for 2.4.1.186 extracted from

  • Meezan, E.; Manzella, S.; Roden, L.
    Menage a trois: glycogenin, proteoglycan core protein xylosyltransferase and UDP-xylose (1995), Trends Glycosci. Glycotechnol., 7, 303-332.
No PubMed abstract available
Search for more literature for 2.4.1.186

Activating Compound

Activating Compound Comment Organism Structure
additional information enzyme is phosphorylated in embryonic muscle Coturnix sp.

Application

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(Commentary)

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

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

General Stability Organism
alkali-stable Gallus gallus
alkali-stable Mus musculus
alkali-stable Rattus norvegicus

Inhibitors

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 [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

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 [Da] Molecular Weight Maximum [Da] Comment Organism
32000
-
 kidney enzyme Rattus norvegicus
37280
-
 amino acid sequence determination Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Coturnix sp.
-
 Quail
-
Gallus gallus
-
 hen
-
Mus musculus
-
-
-
Oryctolagus cuniculus
-
-
-
Rattus norvegicus
-
-
-

Posttranslational Modification

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 (Commentary)

Purification (Comment) Organism
separation from glycogen synthase, EC 2.4.1.11, by LiBr Oryctolagus cuniculus

Reaction

Reaction Comment Organism Reaction ID
UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin highly conserved protein Rattus norvegicus
a
UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin highly conserved protein Bos taurus
a
UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin highly conserved protein Oryctolagus cuniculus
a
UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin stereochemistry and mechanism Rattus norvegicus
a
UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin stereochemistry and mechanism Bos taurus
a
UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin stereochemistry and mechanism Oryctolagus cuniculus
a

Source Tissue

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 and Products (Substrate)

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

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