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Literature summary for 2.4.1.41 extracted from

  • Hanisch, F.G.; Reis, C.A.; Clausen, H.; Paulsen, H.
    Evidence for glycosylation-dependent activities of polypeptide N-acetylgalactosaminyltransferases rGalNAc-T2 and -T4 on mucin glycopeptides (2001), Glycobiology, 11, 731-740.
    View publication on PubMed
Search for more literature for 2.4.1.41

Cloned(Commentary)

Cloned (Comment) Organism
expression of secreted GalNAc-T4 in CHO cells Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
fully GalNAc-substituted MUC1 repeat peptide inhibits activity of rGalNAc-T4 and -T2 Homo sapiens
additional information elongation of GalNAc by beta3-galactosylation inhibits rGalNAc-T4 activity completely and rGalNAc-T2 activity with respect to the acceptor site GSTA, not inhibited by GlcNAc Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
Golgi apparatus
-
 Homo sapiens 5794
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-N-acetyl-D-galactosamine + polypeptide Homo sapiens post-translational, initial reaction in O-linked oligosaccharide biosynthesis UDP + N-acetyl-D-galactosaminyl-polypeptide
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
 recombinant GalNAc-T2 and -T4
-

Purification (Commentary)

Purification (Comment) Organism
partial Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information multiple enzyme isoforms Homo sapiens ?
-
 ?
additional information all known rGalNAc-Ts are characterized by a putative lectin domain in their C-terminal regions Homo sapiens ?
-
 ?
UDP-N-acetyl-D-galactosamine + GalNAc-glycosylated peptide rGalNAc-T4 is dependent on the presence of GalNAc on acceptor peptides, activity is triggered by a lectin-like interaction of enzyme with the glycopeptide directed by the putative lectin domain found in the C-terminal region, rGalNAc-T2 activity is enhanced on glycosylated acceptor peptides Homo sapiens UDP + N-acetyl-D-galactosaminyl-GalNAc-glucosylated peptide
-
 ?
UDP-N-acetyl-D-galactosamine + polypeptide site-specific O-glycosylation by rGalNAc-T2 and -T4 is controlled by the primary sequence context and the position and structure of previously introduced O-glycans, acceptors: synthetic mucin-type peptides and glycopeptides derived from tandem repeat regions of MUC1, MUC2 and MUC4, minimum peptide length is required, which is larger for glycosylated substrates, concerted and sequential action of rGalNAc-T2 and -T4 fully glycosylates MUC1, but only partially MUC2 and MUC4 tandem repeat peptides Homo sapiens UDP + N-acetyl-D-galactosaminyl-polypeptide
-
 ?
UDP-N-acetyl-D-galactosamine + polypeptide transfer of GalNAc to a serine or threonine residue on the acceptor protein Homo sapiens UDP + N-acetyl-D-galactosaminyl-polypeptide
-
 ?
UDP-N-acetyl-D-galactosamine + polypeptide post-translational, initial reaction in O-linked oligosaccharide biosynthesis Homo sapiens UDP + N-acetyl-D-galactosaminyl-polypeptide
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Homo sapiens