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 | 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 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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | - |
C57BL/6 wild-type, isozyme ppGalNAcT-1, encoded by gene Galnt1, and isozymes ppGalNAcT-2, and ppGalNAcT-3 | - |
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 | 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 | 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 | Comment | Organism |
---|---|---|
? | x * 57000, recombinant isozyme ppGalNAcT-1, SDS-PAGE, x * 60000, recombinant isozyme ppGalNAcT-2, SDS-PAGE | Mus musculus |
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 | Comment | Organism |
---|---|---|
physiological function | UDP-GalNAc polypeptide:N-acetylgalactosaminyltransferases regulate the mucin-type O-glycan biosynthesis | Mus musculus |