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Literature summary extracted from

  • Shailubhai, K.; Dong-Yu, B.; Saxena, E.S.; Vijay, I.K.
    Purification and characterization of UDP-N-acetyl-D-glucosamine:dolichol phosphate N-acetyl-D-glucosamine-1-phosphate transferase involved in the biosynthesis of asparagine-linked glycoproteins in the mammary gland (1988), J. Biol. Chem., 263, 15964-15972.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.8.15 Dolichyl-phosphoryl-mannose stimulates Bos taurus

General Stability

EC Number General Stability Organism
2.7.8.15 purified enzyme is resistant to digestion with either endo-beta-N-acetylglucosaminidase H or F Bos taurus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.8.15 Diumycin
-
 Bos taurus
2.7.8.15 dolichyl phosphate at high concentrations Bos taurus
2.7.8.15 Hg2+ partially reversed by dithiothreitol Bos taurus
2.7.8.15 iodoacetamide
-
 Bos taurus
2.7.8.15 PCMB
-
 Bos taurus
2.7.8.15 tunicamycin
-
 Bos taurus
2.7.8.15 UDP
-
 Bos taurus
2.7.8.15 UDP-glucose
-
 Bos taurus
2.7.8.15 UDP-hexanolamine
-
 Bos taurus
2.7.8.15 UDP-xylose
-
 Bos taurus
2.7.8.15 UMP
-
 Bos taurus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.8.15 0.0045
-
 UDP-GlcNAc pH 7.6, 37°C Bos taurus
2.7.8.15 0.016
-
 dolichyl phosphate pH 7.6, 37°C Bos taurus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.8.15 microsome
-
 Bos taurus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.8.15 Mg2+ stimulates Bos taurus
2.7.8.15 Mn2+ stimulates Bos taurus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.8.15 330000 360000 large molecular mass of the enzyme can be due to aggregation of the hydrophobic, membrane-derived enzyme rather than resulting from subunit interaction, gel filtration Bos taurus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.8.15 UDP-N-acetyl-D-glucosamine + dolichyl phosphate Bos taurus enzyme initiates the dolichol cycle for the biosynthesis of asparagine-linked glycoproteins ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.8.15 Bos taurus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.8.15 additional information the enzyme is not a glycoprotein of the asparagine-linked type Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.8.15 mammary gland lactating Bos taurus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.8.15 additional information
-
-
 Bos taurus

Storage Stability

EC Number Storage Stability Organism
2.7.8.15 4°C, solubilized enzyme loses most of its activity within 12 h Bos taurus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.8.15 UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
-
 Bos taurus UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
 ?
2.7.8.15 UDP-N-acetyl-D-glucosamine + dolichyl phosphate enzyme initiates the dolichol cycle for the biosynthesis of asparagine-linked glycoproteins Bos taurus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.8.15 More results indicate that either 70000 MW band in SDS-PAGE is a precursor form of the enzyme or this polypeptide, representing the native enzyme or its subunit, is proteolyzed to smaller, enzymatically active peptides of 50000 Da and 46000 Da during purification Bos taurus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.8.15 7.4 7.6
-
 Bos taurus