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Literature summary for 2.4.3.4 extracted from

  • Sadler, J.E.; Rearick, J.I.; Paulson, J.C.; Hill, R.L.
    Purification to homogeneity of a beta-galactoside alpha2 leads to 3 sialyltransferase and partial purification of an alpha-N-acetylgalactosaminide alpha2 leads to 6 sialyltransferase from porcine submaxillary glands (1979), J. Biol. Chem., 254, 4434-4443 .
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
CDP less effective than CTP Sus scrofa
CMP less effective than CTP Sus scrofa
CTP most potent inhibitor among cytidine nucleotides Sus scrofa

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Sus scrofa 16020
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
gel filtration, enzyme form A and B Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa Q02745
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
submandibular gland
-
Sus scrofa
-

Storage Stability

Storage Stability Organism
-20°C, 50% (w/v) glycerol, 6 months, no loss of activity Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CMP-N-acetyl-beta-neuraminate + [porcine submaxillary asialo-mucin]-(O-3-(beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-serine
-
Sus scrofa CMP + [porcine submaxillary asialo-mucin]-(O-3-(alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-serine
-
?
CMP-N-acetyl-beta-neuraminate + [porcine submaxillary asialo-mucin]-(O-3-(beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-threonine
-
Sus scrofa CMP + [porcine submaxillary asialo-mucin]-(O-3-(alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-threonine
-
?

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00022
-
CTP pH and temperature not specified in the publication Sus scrofa

General Information

General Information Comment Organism
metabolism the enzyme is involved in biosynthesis of O-linked oligosaccharide chains of glycoproteins Sus scrofa