Inhibitors | Comment | Organism | Structure |
---|---|---|---|
CaCl2 | weak | Rattus norvegicus | |
CdCl2 | - |
Rattus norvegicus | |
EDTA | strong | Rattus norvegicus | |
FeCl2 | - |
Rattus norvegicus | |
NiCl2 | - |
Rattus norvegicus | |
ZnCl2 | strong | Rattus norvegicus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | - |
Rattus norvegicus | |
0.6 | - |
asialo-alpha1-acid glycoprotein | - |
Rattus norvegicus | |
1 | - |
Galbeta(1->4)GlcNAcbeta(1->3)Galbeta(1->4)GlcNAc | - |
Rattus norvegicus | |
2.2 | - |
N-acetyllactosamine | - |
Rattus norvegicus | |
5.2 | - |
lactose | - |
Rattus norvegicus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mn2+ | MnCl2 stimulates 2.5fold, optimal concentration: 20 mM | Rattus norvegicus | |
additional information | absolute requirement for divalent cations, not stimulated by Mg2+ | Rattus norvegicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R | Rattus norvegicus | enzyme functions in both the initiation and elongation of linear i-active polylactosaminoglycan chains of N-glycoproteins and possibly other glycoconjugates | UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R | - |
? | |
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine | Rattus norvegicus | - |
? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | - |
Sprague Dawley rats | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | - |
Rattus norvegicus |
Purification (Comment) | Organism |
---|---|
partial, 178fold, from Novikoff tumor cell ascites fluid | Rattus norvegicus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
Novikoff ascites tumor cell | strain N1S1-67 | Rattus norvegicus | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.00153 | - |
- |
Rattus norvegicus |
Storage Stability | Organism |
---|---|
0-4°C, lyophilized enzyme form, over 6 months, stable | Rattus norvegicus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | asialo-serum glycoproteins are much more effective than O-glycoproteins as acceptors, overview over oligosaccharide substrates | Rattus norvegicus | ? | - |
? | |
UDP-N-acetyl-alpha-D-glucosamine + Galbeta(1->4)GlcNAcbeta(1->3)Galbeta(1->4)GlcNAc | - |
Rattus norvegicus | UDP + GlcNAcbeta(1->3)Galbeta(1->4)GlcNAcbeta(1->3)Galbeta(1->4)GlcNAc | - |
? | |
UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R | highly specific for acceptor oligosaccharides and glycoproteins carrying a terminal Galbeta(1-4)GlcNAcbeta1-R unit, catalyzes the formation of GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta-R sequence, Galbeta(1-4)GlcNAcbeta(1-2)(Galbeta(1-4)GlcNAcbeta(1-6))Man pentasaccharide in the acceptor structure is a requirement for optimal activity, branch specificity, branches of this pentasaccharide structure, when contained in tri- and tetraantennary oligosaccharides, are highly preferred over other branches for attachment of the 1st and 2nd mol of GlcNAc into the acceptor molecule, enzyme also shows activity towards oligosaccharides related to blood group I- and i-active polylactosaminoglycans | Rattus norvegicus | UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R | - |
? | |
UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R | enzyme functions in both the initiation and elongation of linear i-active polylactosaminoglycan chains of N-glycoproteins and possibly other glycoconjugates | Rattus norvegicus | UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R | - |
? | |
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine | - |
Rattus norvegicus | ? | - |
? | |
UDP-N-acetylglucosamine + asialo-alpha1-acid glycoprotein | much more effective than asialo-transferrin and asialo-fetuin, asialo-alpha1-acid glycoprotein from human plasma Cohn fraction V, transfer of GlcNAc to a terminal Gal in a beta1,3-linkage | Rattus norvegicus | UDP + N-acetylglucosaminylated asialo-alpha1-acid glycoprotein | - |
? | |
UDP-N-acetylglucosamine + asialo-fetuin | much less effective than asialo-alpha1-acid glycoprotein, transfer of GlcNAc to a terminal Gal in a beta1,3-linkage | Rattus norvegicus | UDP + N-acetylglucosaminylated asialo-fetuin | - |
? | |
UDP-N-acetylglucosamine + asialo-transferrin | much less effective than asialo-alpha1-acid glycoprotein, transfer of GlcNAc to a terminal Gal in a beta1,3-linkage | Rattus norvegicus | UDP + N-acetylglucosaminylated asialo-transferrin | - |
? | |
UDP-N-acetylglucosamine + lactose | 70% of activity with N-acetyllactosamine | Rattus norvegicus | UDP + GlcNAcbeta(1-3)Galbeta(1-4)Glc | - |
? | |
UDP-N-acetylglucosamine + N-acetyllactosamine | more effective acceptor than lactose | Rattus norvegicus | UDP + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc | - |
? | |
UDP-N-acetylglucosamine + porcine submaxillary asialo-afuco-mucin | very poor substrate | Rattus norvegicus | UDP + N-acetylglucosaminylated porcine submaxillary asialo-afuco-mucin | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Rattus norvegicus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.8 | 7.2 | asialo-alpha1-acid glycoprotein as acceptor | Rattus norvegicus |