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Literature summary extracted from

  • Tai, V.W.F.; O'Reilly, M.K.; Imperiali, B.
    Substrate specificity of N-acetylglucosaminyl(diphosphodolichol) N-acetylglucosaminyl transferase, a key enzyme in the dolichol pathway (2001), Bioorg. Med. Chem., 9, 1133-1140.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.141 P1-dolichyl P2-(2-deoxy-2-fluoro-alpha-D-glucopyranosyl) diphosphate inhibitors when studied in competition with N-acetyl-D-glucosaminyl-diphosphodolichol Sus scrofa
2.4.1.141 P1-dolichyl P2-(2-deoxy-2-trifluoroacetamido-alpha-D-glucopyranosyl) diphosphate inhibitors when studied in competition with N-acetyl-D-glucosaminyl-diphosphodolichol Sus scrofa
2.4.1.141 P1-dolichyl P2-(2-O-ethyl-alpha-D-glucopyranosyl) diphosphate inhibitors when studied in competition with N-acetyl-D-glucosaminyl-diphosphodolichol Sus scrofa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.4.1.141 microsome
-
Sus scrofa
-
-

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.141 Sus scrofa
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.1.141 liver
-
Sus scrofa
-

Storage Stability

EC Number Storage Stability Organism
2.4.1.141 -80ΒΊC, 30% glycerol, several months Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.141 7
-
-
Sus scrofa