Literature summary extracted from

Nemansky, M.; Van den Eijnden, D.H.
Enzymic characterization of CMP-NeuAc Gal-beta-1,4GlcNAc-R alpha(2,3)-sialyltransferase from human placenta (1993), Glycoconjugate J., 10, 99-108 .

Localization

EC Number	Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.4.3.6	Homo sapiens	-	-	-

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
2.4.3.6	placenta	-	Homo sapiens	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2.4.3.6	CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc-R	the enzyme prefers type 2 chain (Gal beta 1-4GlcNAc) over type 1 chain (Gal beta 1-3GlcNAc) acceptors. Oligosaccharides and glycopeptides are better acceptor substrates than glycoproteins. Of the branched oligosaccharides, those with a bisected N-acetylglucosamine (GlcNAc) structure appear to be poorer substrates, while triantennary structures containing a beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->4)-alpha-Man-(1->3)-beta-D-Man branch are preferred	Homo sapiens	CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-R	-	?

Synonyms

EC Number	Synonyms	Comment	Organism
2.4.3.6	CMP-NeuAc:Gal beta 1-4GlcNAc-R alpha(2-3)-sialyltransferase	-	Homo sapiens

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Release 2023.1 (January 2023)