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Literature summary for 2.4.1.41 extracted from

  • Miwa, H.E.; Gerken, T.A.; Jamison, O.; Tabak, L.A.
    Isoform-specific O-glycosylation of osteopontin and bone sialoprotein by polypeptide N-acetylgalactosaminyltransferase-1 (2010), J. Biol. Chem., 285, 1208-1219.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
isozymes ppGalNAcT-1, ppGalNAcT-2, and ppGalNAcT-3, recombinant expression of the His-tagged isozymes ppGalNAcT-1, ppGalNAcT-2 in Pichia pastoris and of isozyme ppGalNAcT-3 in COS-7 cells, secretion of the recombinant proteins Mus musculus

Protein Variants

Protein Variants Comment Organism
additional information generation of Galnt1 null mice, that show reduced glycosylation of bone sialoprotein and osteopontin Ser and Thr residues speficially glycosylated by isozyme ppGalNAcT-1, overview Mus musculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
57000
-
x * 57000, recombinant isozyme ppGalNAcT-1, SDS-PAGE, x * 60000, recombinant isozyme ppGalNAcT-2, SDS-PAGE Mus musculus
60000
-
x * 57000, recombinant isozyme ppGalNAcT-1, SDS-PAGE, x * 60000, recombinant isozyme ppGalNAcT-2, SDS-PAGE Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus UDP-GalNAc polypeptide:N-acetylgalactosaminyltransferase catalyzes the first step in the mucin-type O-glycan biosynthesis pathway by transferring GalNAc to Ser or Thr residues in a protein from the sugar donor UDP-GalNAc ?
-
?
UDP-N-acetyl-D-galactosamine + bone sialoprotein Mus musculus preferred substrate of isozyme ppGalNAcT-1, glycosylation of Thr101, Ser131, Thr199, and Ser214, glycosylation pattern, overview UDP + UDP-N-acetyl-D-galactosaminyl-bone sialoprotein
-
?
UDP-N-acetyl-D-galactosamine + osteopontin Mus musculus preferred substrate of isozyme ppGalNAcT-1, glycosylation pattern, overview UDP + N-acetyl-D-galactosaminyl-osteopontin
-
?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
C57BL/6 wild-type, isozyme ppGalNAcT-1, encoded by gene Galnt1, and isozymes ppGalNAcT-2, and ppGalNAcT-3
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged isozymes ppGalNAcT-1 and ppGalNAcT-2 from Pichia pastoris medium by nickel affinity chromatography, the tag is cleaved off by TEV protease, recombinant isozyme ppGalNAcT-3t from medium of COS-7 cells Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
bone isozymes ppGalNAcT-1, ppGalNAcT-2, and ppGalNAcT-3, expression patterns, overview. Expression of isozyme ppGalNAcT-1 especially in calvaria and tibia Mus musculus
-
osteoblast
-
Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information UDP-GalNAc polypeptide:N-acetylgalactosaminyltransferase catalyzes the first step in the mucin-type O-glycan biosynthesis pathway by transferring GalNAc to Ser or Thr residues in a protein from the sugar donor UDP-GalNAc Mus musculus ?
-
?
UDP-N-acetyl-D-galactosamine + bone sialoprotein preferred substrate of isozyme ppGalNAcT-1, glycosylation of Thr101, Ser131, Thr199, and Ser214, glycosylation pattern, overview Mus musculus UDP + UDP-N-acetyl-D-galactosaminyl-bone sialoprotein
-
?
UDP-N-acetyl-D-galactosamine + osteopontin preferred substrate of isozyme ppGalNAcT-1, glycosylation pattern, overview Mus musculus UDP + N-acetyl-D-galactosaminyl-osteopontin
-
?

Subunits

Subunits Comment Organism
? x * 57000, recombinant isozyme ppGalNAcT-1, SDS-PAGE, x * 60000, recombinant isozyme ppGalNAcT-2, SDS-PAGE Mus musculus

Synonyms

Synonyms Comment Organism
More the enzyme belongs to the family of UDP-GalNAc polypeptide:N-acetylgalactosaminyltransferases, i.e. ppGalNAcTs Mus musculus
polypeptide N-acetylgalactosaminyltransferase-1
-
Mus musculus
ppGalNAcT
-
Mus musculus
UDP-GalNAc polypeptide:N-acetylgalactosaminyltransferase
-
Mus musculus

General Information

General Information Comment Organism
physiological function UDP-GalNAc polypeptide:N-acetylgalactosaminyltransferases regulate the mucin-type O-glycan biosynthesis Mus musculus