Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Ten Hagen, K.G.; Tetaert, D.; Hagen, F.K.; Richet, C.; Beres, T.M.; Gagnon, J.; Balys, M.M.; VanWuyckhuyse, B.; Bedi, G.S.; Degand, P.; Tabak, L.A.
    Characterization of a UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase that displays glycopeptide N-acetylgalactosaminyltransferase activity (1999), J. Biol. Chem., 274, 27867-27874.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.41 amino acid sequences of ppGaNTase-T3 and –T4 Mus musculus
2.4.1.41 ppGaNTase-T6 from sublingual gland is cloned, sequenced and expressed transiently in COS7 cells as secreted form, 657-amino acid protein, amino acid sequences of ppGaNTase-T1, -T5 and -T6 Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.4.1.41 membrane
-
 Mus musculus 16020
-
2.4.1.41 membrane ppGaNTase-T6: type II membrane protein with a 27-amino acid hydrophobic region Rattus norvegicus 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide Mus musculus initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function UDP + N-acetyl-D-galactosaminyl-polypeptide
-
 ?
2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide Rattus norvegicus initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function UDP + N-acetyl-D-galactosaminyl-polypeptide
-
 ?
2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide Mus musculus O-glycosylation by ppGaNTase-Ts of multisite substrates may proceed in a specific hierarchical manner UDP + N-acetyl-D-galactosaminyl-polypeptide
-
 ?
2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide Rattus norvegicus O-glycosylation by ppGaNTase-Ts of multisite substrates may proceed in a specific hierarchical manner UDP + N-acetyl-D-galactosaminyl-polypeptide
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.41 Mus musculus
-
 BALB/c mouse, ppGaNTase-T6, -T1 and -T4
-
2.4.1.41 Rattus norvegicus Q9R0C5 Wistar rats, ppGaNTase-T6, -T1 and -T4
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.1.41 colon ppGaNTase-T6 Mus musculus
-
2.4.1.41 colon ppGaNTase-T6 Rattus norvegicus
-
2.4.1.41 additional information traces of ppGaNTase-T6 in the ovary, cervix and uterus, ppGaNTase-T1 is present in all tissues examined Mus musculus
-
2.4.1.41 additional information traces of ppGaNTase-T6 in the ovary, cervix and uterus, ppGaNTase-T1 is present in all tissues examined Rattus norvegicus
-
2.4.1.41 small intestine ppGaNTase-T6 Mus musculus
-
2.4.1.41 small intestine ppGaNTase-T6 Rattus norvegicus
-
2.4.1.41 stomach ppGaNTase-T6 Mus musculus
-
2.4.1.41 stomach ppGaNTase-T6 Rattus norvegicus
-
2.4.1.41 sublingual gland ppGaNTase-T6: highest level of mRNA Mus musculus
-
2.4.1.41 sublingual gland ppGaNTase-T6: highest level of mRNA Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.41 additional information multiple enzyme isoforms Mus musculus ?
-
 ?
2.4.1.41 additional information multiple enzyme isoforms Rattus norvegicus ?
-
 ?
2.4.1.41 additional information ppGaNTase-T6: no activity with unglycosylated peptides Rattus norvegicus ?
-
 ?
2.4.1.41 UDP-N-acetyl-D-galactosamine + GalNAc-glycosylated peptide ppGaNTase-T6 requires at least 2 intact GalNAc residues in the substrate, acceptor: MUC5AC-glycopeptide, obtained by the action of ppGaNTase-T1 Rattus norvegicus UDP + N-acetyl-D-galactosaminyl-GalNAc-glucosylated peptide
-
 ?
2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide
-
 Mus musculus UDP + N-acetyl-D-galactosaminyl-polypeptide
-
 ?
2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide ppGaNTase-T1: acceptor is MUC5AC peptide, di-glycopeptide contains GalNAc at Thr-3 and -13, tri-glycopeptide an additional one at Ser-5 Rattus norvegicus UDP + N-acetyl-D-galactosaminyl-polypeptide
-
 ?
2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function Mus musculus UDP + N-acetyl-D-galactosaminyl-polypeptide
-
 ?
2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function Rattus norvegicus UDP + N-acetyl-D-galactosaminyl-polypeptide
-
 ?
2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide O-glycosylation by ppGaNTase-Ts of multisite substrates may proceed in a specific hierarchical manner Mus musculus UDP + N-acetyl-D-galactosaminyl-polypeptide
-
 ?
2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide O-glycosylation by ppGaNTase-Ts of multisite substrates may proceed in a specific hierarchical manner Rattus norvegicus UDP + N-acetyl-D-galactosaminyl-polypeptide
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.41 37
-
 assay at Mus musculus
2.4.1.41 37
-
 assay at Rattus norvegicus