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Literature summary for 2.4.1.41 extracted from

  • Tenno, M.; Saeki, A.; Kezdy, F.J.; Elhammer, A.P.; Kurosaka, A.
    The lectin domain of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1 is involved in O-glycosylation of a polypeptide with multiple acceptor sites (2002), J. Biol. Chem., 277, 47088-47096.
    View publication on PubMed
Search for more literature for 2.4.1.41

Cloned(Commentary)

Cloned (Comment) Organism
deletion mutant GalNAc-T1 cDNA is cloned and expressed in COS7 cells Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
D444A GalNAc-T1 mutant with severely impaired apomucin glycosylation, D444A/D484A/D525A triple mutant has significantly lower activity than D444A single mutant Rattus norvegicus
F468A GalNAc-T1 mutant with strongly reduced activity and decreased expression Rattus norvegicus
G455Q GalNAc-T1 mutant with reduced reactivity towards apomucin Rattus norvegicus
additional information site-directed mutagenesis at the C-terminus and its deletion inactivates GalNAc-T1, probably caused by conformational changes in the (QXW)3 repeats, deletion of the lectin domain results in complete loss of activity Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
GalNAc inhibition of GalNAc-T1 by free GalNAc: follow-up O-glycosylation of apomucin is sensitive, O-glycosylation of synthetic peptides containing a single glycosylation site is resistant Rattus norvegicus
additional information GalNAc-T1: follow-up glycosylation is inhibited by addition of beta1,3Gal to GalNAc, apomucin glycosylation is not inhibited by galactose, glucose, N-acetylglucosamine, mannose and fucose Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information increased values, mg/ml, for apomucin of several GalNAc-T1 mutants Rattus norvegicus
0.2
-
 Pro-Pro-Asp-Ala-Ala-Thr-Ala-Ala-Pro-Leu GalNAc-T1 Rattus norvegicus
0.8
-
 Gly-Val-Val-Pro-Thr-Val-Val-Pro-Gly GalNAc-T1 Rattus norvegicus
3.6
-
 UDP-GalNAc GalNac-T1 mutant N465A Rattus norvegicus
4
-
 UDP-GalNAc GalNac-T1 mutant G455Q Rattus norvegicus
4.4
-
 UDP-GalNAc GalNac-T1 triple mutant D444A/D484A/D525A Rattus norvegicus
5.1
-
 UDP-GalNAc GalNac-T1 mutants D444A and P-deltaN42 Rattus norvegicus
5.4
-
 UDP-GalNAc GalNac-T1 mutant F457A Rattus norvegicus
6.1
-
 UDP-GalNAc GalNac-T1 mutant Q466A Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane type II membrane protein Rattus norvegicus 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ essential for donor substrate binding Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-N-acetyl-D-galactosamine + polypeptide Rattus norvegicus GalNAc-T1 glycosylates unmodified polypeptides in vivo UDP + N-acetyl-D-galactosaminyl-polypeptide
-
 ?
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
-
 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
 GalNAc-T1
-

Purification (Commentary)

Purification (Comment) Organism
recombinant mutant GalNAc-T1, expressed in COS7 cells Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information contains a lectin-like repeat sequence at the C-terminus, role of GalNAc-T1 lectin domain, which is involved in glycosylation of substrates with multiple acceptor sites Rattus norvegicus ?
-
 ?
UDP-N-acetyl-alpha-D-galactosamine + Gly-Val-Val-Pro-Thr-Val-Val-Pro-Gly
-
 Rattus norvegicus ?
-
 ?
UDP-N-acetyl-alpha-D-galactosamine + Pro-Pro-Asp-Ala-Ala-Thr-Ala-Ala-Pro-Leu
-
 Rattus norvegicus ?
-
 ?
UDP-N-acetyl-D-galactosamine + apomucin deglycosylated bovine submaxillary mucin Rattus norvegicus UDP + N-acetyl-D-galactosaminyl-apomucin
-
 ?
UDP-N-acetyl-D-galactosamine + apomucin GalNAc-T1 Rattus norvegicus UDP + N-acetyl-D-galactosaminyl-apomucin
-
 ?
UDP-N-acetyl-D-galactosamine + GalNAc-glycosylated peptide GalNAc-T1 may also specifically recognize and glycosylate partially glycosylated acceptors Rattus norvegicus UDP + N-acetyl-D-galactosaminyl-GalNAc-glucosylated peptide
-
 ?
UDP-N-acetyl-D-galactosamine + polypeptide GalNAc-T1: Asp-144 is the most important site for GalNAc recognition, primarily recognizes the UDP portion of UDP-GalNAc Rattus norvegicus 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 Rattus norvegicus UDP + N-acetyl-D-galactosaminyl-polypeptide
-
 ?
UDP-N-acetyl-D-galactosamine + polypeptide GalNAc-T1 glycosylates unmodified polypeptides in vivo Rattus norvegicus UDP + N-acetyl-D-galactosaminyl-polypeptide
-
 ?
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
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Rattus norvegicus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
68
-
 GalNAc inhibition of GalNAc-T1 mutant P-deltaN42 Rattus norvegicus
175
-
 GalNAc inhibition of GalNAc-T1 mutant D444A Rattus norvegicus