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Literature summary extracted from

  • Carrizo, M.E.; Miozzo, M.C.; Goldraij, A.; Curtino, J.A.
    Purification of rabbit skeletal muscle proteoglycogen: studies on the glucosyltransferase activity of polysaccharide-free and -bound glycogenin (1997), Glycobiology, 7, 571-578.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.186 UDP inhibits both autoglucosylation and glucosylation of exogenous acceptor Oryctolagus cuniculus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.1.186 Mn2+ dependent on, also required for transglucosylation Oryctolagus cuniculus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.1.186 200000
-
 gel filtration, active proteoglycogen Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.186 UDP-glucose + glycogenin Oryctolagus cuniculus enzyme forms the protein part of proteoglycogen UDP + glucosylated glycogenin
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.186 Oryctolagus cuniculus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.4.1.186 glycoprotein autoglycosylation Oryctolagus cuniculus

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.186 separation from proteoglycogen Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.1.186 skeletal muscle
-
 Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.1.186 additional information
-
-
 Oryctolagus cuniculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.186 additional information no activity with nonapeptide SISIYSYLP and N-lactosylated peptide Oryctolagus cuniculus ?
-
 ?
2.4.1.186 UDP-galactose + glycogenin autoglycosylation reaction Oryctolagus cuniculus UDP + galactosylated glycogenin
-
 ?
2.4.1.186 UDP-glucose + glycogenin autoglycosylation reaction Oryctolagus cuniculus UDP + glucosylated glycogenin
-
 ?
2.4.1.186 UDP-glucose + glycogenin enzyme forms the protein part of proteoglycogen Oryctolagus cuniculus UDP + glucosylated glycogenin
-
 ?
2.4.1.186 UDP-glucose + glycogenin no activity with UDP-N-acetylglucosamine and GDP-mannose Oryctolagus cuniculus UDP + glucosylated glycogenin
-
 ?
2.4.1.186 UDP-glucose + N-(maltosyl-alpha-1,4-(1-deoxyglucitol))-peptide simultaneously and independently of the autoglycosylation reaction Oryctolagus cuniculus UDP + glucosylated N-(maltosyl-alpha-1,4-(1-deoxyglucitol))-peptide
-
 ?
2.4.1.186 UDP-glucose + N-(maltosyl-alpha-1,4-(1-deoxyglucitol))-peptide peptide sequence: SISIYSYLP Oryctolagus cuniculus UDP + glucosylated N-(maltosyl-alpha-1,4-(1-deoxyglucitol))-peptide
-
 ?
2.4.1.186 UDP-glucose + n-dodecyl-beta-D-maltoside simultaneously and independently of the autoglycosylation reaction Oryctolagus cuniculus UDP + n-dodecyl-beta-D-maltotriose
-
 ?

Subunits

EC Number Subunits Comment Organism
2.4.1.186 More enzyme forms the protein part of proteoglycogen Oryctolagus cuniculus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.186 30
-
 assay at Oryctolagus cuniculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.186 7
-
 assay at Oryctolagus cuniculus