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Literature summary for 2.4.1.92 extracted from

  • Furukawa, K.; Takamiya, K.; Furukawa, K.
    beta1,4-N-acetylgalactosaminyltransferase-GM2/GD2 synthase: a key enzyme to control the synthesis of brain-enriched complex gangliosides (2002), Biochim. Biophys. Acta, 1573, 356-362.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information
-
Homo sapiens
additional information overexpression of gene leads to shift of ganglioside components from b-series to a-series Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
Golgi apparatus
-
Homo sapiens 5794
-

Organism

Organism UniProt Comment Textmining
Homo sapiens Q00973
-
-
Mus musculus Q09200
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein 3 N-glycosylation sites at 79,179, 274 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information overview on substrate specificity Homo sapiens ?
-
?
UDP-N-acetyl-D-galactosamine + (N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide i.e. GM3(N-acetylneuraminic acid), best substrate Homo sapiens UDP + N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide
-
?
UDP-N-acetyl-D-galactosamine + GD3-ganglioside
-
Homo sapiens UDP + GD2-ganglioside
-
?