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Literature summary extracted from

  • Sadler, J.E.; Rearick, J.I.; Hill, R.L.
    Purification to homogeneity and enzymatic characterization of an alpha-N-acetylgalactosaminide alpha 2 leads to 6 sialyltransferase from porcine submaxillary glands (1979), J. Biol. Chem., 254, 5934-5941.
    View publication on PubMed

General Stability

EC Number General Stability Organism
2.4.3.3 50 mM NaCl stabilizes during purification Sus scrofa
2.4.3.3 glycerol, 50% w/v, stabilizes during storage Sus scrofa

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.3.3 Antifreeze glycoprotein competitive to ovine submaxillary asialo-mucin, non-competitive to CMP-NeuAc Sus scrofa
2.4.3.3 CTP competitive to CMP-NeuAc Sus scrofa
2.4.3.3 additional information not inhibited by EDTA; not inhibited by Mg2+; not inhibited by Zn2+, Mn2+ Sus scrofa
2.4.3.3 Triton X-100 above critical micelle concentration of 0.016%, 15% inhibition, reversible Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.3.3 0.52
-
CMP-N-acetylneuraminate pH 6.5, 37°C, antifreeze glycoprotein 8 as acceptor Sus scrofa
2.4.3.3 0.66
-
CMP-N-acetylneuraminate pH 6.5, 37°C, ovine submaxillary asialo-mucin as acceptor Sus scrofa
2.4.3.3 1.02
-
Antifreeze glycoprotein antifreeze glycoprotein 8, pH 6.5, 37°C Sus scrofa
2.4.3.3 2.93
-
submaxillary asialo-mucin ovine, pH 6.5, 37°C Sus scrofa

Localization

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.3.3 additional information no metal ion requirement, e.g. Mn2+, Mg2+ or Zn2+ Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.3.3 100000 172000 enzyme exists in several active molecular weight forms from 100000-172000, gel filtration or PAGE Sus scrofa
2.4.3.3 160000
-
x * 160000, enzyme consists of several electrophoretic forms, 160 kDa: largest one, SDS-PAGE Sus scrofa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.3.3 CMP-N-acetylneuraminate + glycano-1,3-(N-acetyl-alpha-D-galactosaminyl)-glycoprotein Sus scrofa involved in biosynthesis of O-linked oligosaccharide chains of glycoproteins CMP + glycano-(2,6-alpha-N-acetylneuraminyl)-(N-acetyl-D-galactosaminyl)-glycoprotein
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.4.3.3 Sus scrofa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.3.3 solubilized with Triton X-100, CDP-agarose affinity chromatography, 117000fold Sus scrofa

Reaction

EC Number Reaction Comment Organism Reaction ID
2.4.3.3 CMP-N-acetylneuraminate + glycano-(1->3)-(N-acetyl-alpha-D-galactosaminyl)-glycoprotein = CMP + glycano-[(2->6)-alpha-N-acetylneuraminyl]-(N-acetyl-D-galactosaminyl)-glycoprotein mechanism Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.3.3 submaxillary gland
-
Sus scrofa
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.3.3 44.6
-
-
Sus scrofa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.3.3 CMP-N-acetylneuraminate + antifreeze glycoprotein antifreeze glycoprotein 8, best acceptor Sus scrofa ?
-
?
2.4.3.3 CMP-N-acetylneuraminate + asialo-fetuin good substrate Sus scrofa CMP + fetuin
-
?
2.4.3.3 CMP-N-acetylneuraminate + glycano-1,3-(N-acetyl-alpha-D-galactosaminyl)-glycoprotein involved in biosynthesis of O-linked oligosaccharide chains of glycoproteins Sus scrofa CMP + glycano-(2,6-alpha-N-acetylneuraminyl)-(N-acetyl-D-galactosaminyl)-glycoprotein
-
?
2.4.3.3 CMP-N-acetylneuraminate + R-1,3-(N-acetyl-alpha-D-galactosaminyl)-glycoprotein acceptor substrate specificity Sus scrofa CMP + R-(2,6-alpha-N-acetylneuraminyl)-(N-acetyl-D-galactosaminyl)-glycoprotein
-
?
2.4.3.3 CMP-N-acetylneuraminate + R-1,3-(N-acetyl-alpha-D-galactosaminyl)-glycoprotein antifreeze glycoprotein is the best substrate Sus scrofa CMP + R-(2,6-alpha-N-acetylneuraminyl)-(N-acetyl-D-galactosaminyl)-glycoprotein
-
?
2.4.3.3 CMP-N-acetylneuraminate + R-1,3-(N-acetyl-alpha-D-galactosaminyl)-glycoprotein R: H or a beta-galactoside Sus scrofa CMP + R-(2,6-alpha-N-acetylneuraminyl)-(N-acetyl-D-galactosaminyl)-glycoprotein
-
?
2.4.3.3 CMP-N-acetylneuraminate + R-1,3-(N-acetyl-alpha-D-galactosaminyl)-glycoprotein asialo-fetuin Sus scrofa CMP + R-(2,6-alpha-N-acetylneuraminyl)-(N-acetyl-D-galactosaminyl)-glycoprotein
-
?
2.4.3.3 CMP-N-acetylneuraminate + R-1,3-(N-acetyl-alpha-D-galactosaminyl)-glycoprotein specific for alpha-N-acetylgalactosamine attached through alpha-glycosidic linkage to threonine or serine in polypeptide chain Sus scrofa CMP + R-(2,6-alpha-N-acetylneuraminyl)-(N-acetyl-D-galactosaminyl)-glycoprotein
-
?
2.4.3.3 CMP-N-acetylneuraminate + R-1,3-(N-acetyl-alpha-D-galactosaminyl)-glycoprotein porcine submaxillary asialo-mucin Sus scrofa CMP + R-(2,6-alpha-N-acetylneuraminyl)-(N-acetyl-D-galactosaminyl)-glycoprotein
-
?
2.4.3.3 CMP-N-acetylneuraminate + R-1,3-(N-acetyl-alpha-D-galactosaminyl)-glycoprotein antifreeze glycoprotein Sus scrofa CMP + R-(2,6-alpha-N-acetylneuraminyl)-(N-acetyl-D-galactosaminyl)-glycoprotein
-
?
2.4.3.3 CMP-N-acetylneuraminate + R-1,3-(N-acetyl-alpha-D-galactosaminyl)-glycoprotein ovine submaxillary asialo-mucin, with simple O-linked GalNAcalpha-Thr/Ser Sus scrofa CMP + R-(2,6-alpha-N-acetylneuraminyl)-(N-acetyl-D-galactosaminyl)-glycoprotein
-
?
2.4.3.3 CMP-N-acetylneuraminate + submaxillary asialo-mucin ovine and porcine submaxillary asialo-mucin are good acceptors Sus scrofa CMP + submaxillary mucin linkage formed is NeuAc(2-6)GalNAcalpha(1-)O-Thr/Ser ?
2.4.3.3 additional information no acceptors: glycoproteins with Asn-linked oligosaccharides, glycosides, mono- and oligosaccharides Sus scrofa ?
-
?

Subunits

EC Number Subunits Comment Organism
2.4.3.3 ? x * 160000, enzyme consists of several electrophoretic forms, 160 kDa: largest one, SDS-PAGE Sus scrofa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.3.3 37
-
assay at Sus scrofa

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.4.3.3 0.92
-
Antifreeze glycoprotein pH 6.5, 37°C Sus scrofa