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Literature summary extracted from

  • Yip, M.; Nguyen, N.
    The enzymic synthesis of GM1b rat-brain CMP-N-acetylneuraminic acid sialo-GM1 sialyltransferase (1981), Lipids, 16, 72-74 .
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.4.3.2 Triton CF54 required for optimal activity Rattus norvegicus
2.4.3.2 Tween 80 required for optimal activity Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.3.2 CMP-N-acetyl-beta-neuraminate inhibition is observed at a concentration greater than 0.25 mM Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.3.2 0.1
-
gangloside asialo-GM1 at pH 6.5 and 37°C Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
2.4.3.2 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.3.2 brain highest activity in fetal and young rat brains Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.3.2 CMP-N-acetyl-beta-neuraminate + gangloside asialo-GM1
-
Rattus norvegicus CMP + ganglioside GM1b
-
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Synonyms

EC Number Synonyms Comment Organism
2.4.3.2 CMP-N-acetylneuraminic acid: sialo-GM1 sialyltransferase
-
Rattus norvegicus
2.4.3.2 CMPNeuNAc: asialo-GM1 sialyltransferase
-
Rattus norvegicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.3.2 6.5
-
in cacodylate buffer Rattus norvegicus