KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | effect of substrate glycosylation and amino acid substitution of glycopeptides on Km-values and enzyme activity | Bos taurus | |
1.3 | - |
Ac-Pro-Thr-Thr-Thr-Pro-Ile-Ser-Thr-NH2 | derived from the MUC2 repeat sequence | Bos taurus | |
1.3 | - |
Ac-Pro-Thr-Thr-Thr | derived from the bovine myelin basic protein sequence | Bos taurus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-N-acetyl-D-galactosamine + polypeptide | Bos taurus | catalyzes the first step in biosynthesis of O-linked oligosaccharides in many glycoproteins | UDP + N-acetyl-D-galactosaminyl-polypeptide | - |
? | |
UDP-N-acetyl-D-galactosamine + polypeptide | Bos taurus | catalyzes in vivo glycosylation of both threonine and serine | UDP + N-acetyl-D-galactosaminyl-polypeptide | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bos taurus | - |
colostrum | - |
Purification (Comment) | Organism |
---|---|
- |
Bos taurus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
colostrum | - |
Bos taurus | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
30.6 | - |
- |
Bos taurus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-N-acetyl-alpha-D-galactosamine + Ac-Pro-Thr-Thr-Thr | - |
Bos taurus | ? | - |
? | |
UDP-N-acetyl-alpha-D-galactosamine + Ac-Pro-Thr-Thr-Thr-Pro-Ile-Ser-Thr-NH2 | - |
Bos taurus | ? | - |
? | |
UDP-N-acetyl-D-galactosamine + polypeptide | acceptors: synthetic glycopeptides and peptides most of which contain sequences derived from the tandem repeat region of MUC2 mucin | Bos taurus | UDP + N-acetyl-D-galactosaminyl-polypeptide | - |
? | |
UDP-N-acetyl-D-galactosamine + polypeptide | rate of incorporation of GalNAc into Thr is significantly greater than into Ser residues, presence of 1-2 GalNAc-Thr moieties in the subtrate reduces enzyme activity, especially when Galbeta1-3GalNAc is present, O-glycosylation depends on both amino acid sequence and prior glycosylation of substrates, enzyme is selective in glycosylating peptides with the Pro-Thr-Thr-Thr-Pro-Ile-Ser-Thr sequence in that the preferred primary site is the third Thr from the N-terminal end | Bos taurus | UDP + N-acetyl-D-galactosaminyl-polypeptide | - |
? | |
UDP-N-acetyl-D-galactosamine + polypeptide | catalyzes the first step in biosynthesis of O-linked oligosaccharides in many glycoproteins | Bos taurus | UDP + N-acetyl-D-galactosaminyl-polypeptide | - |
? | |
UDP-N-acetyl-D-galactosamine + polypeptide | catalyzes in vivo glycosylation of both threonine and serine | Bos taurus | UDP + N-acetyl-D-galactosaminyl-polypeptide | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Bos taurus |