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UDP-N-acetyl-D-glucosamine + asialo-alpha1-acid glycoprotein
UDP + N-acetylglucosaminylated asialo-alpha1-acid glycoprotein
UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP-N-acetyl-D-glucosamine + Galalpha(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
?
UDP-N-acetyl-D-glucosamine + Galalpha(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
?
-
reaction rate is 38% of that with GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
-
-
?
UDP-N-acetyl-D-glucosamine + Galbeta(1-3)GlcNAcbeta(1-3)Galbeta(1-4)Glc
?
UDP-N-acetyl-D-glucosamine + Galbeta(1-3)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
?
UDP-N-acetyl-D-glucosamine + Galbeta(1-4)(Fucalpha(1-3))GlcNAcbeta(1-3)Galbeta(1-4)Glc
?
very poor substrate
-
-
?
UDP-N-acetyl-D-glucosamine + Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
UDP + Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)Glc
i.e. lacto-N-neotetraose, IGnT B forms branch in the internal Gal residue
no transfer to the terminal Gal residue
?
UDP-N-acetyl-D-glucosamine + Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
UDP + Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)GlcNAc
UDP-N-acetyl-D-glucosamine + Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
UDP + Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
UDP-N-acetyl-D-glucosamine + Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
UDP + Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
UDP-N-acetyl-D-glucosamine + Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
UDP + (GlcNAc)1-Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
-
cIGnT
also as product: (GlcNAc)2-Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc, cIGnT6 generates in a partial reaction nona- and decasaccharide products, which represent mixtures of isomers carrying one or two GlcNAc-branches on the linear octasaccharide acceptor
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta(1-3)Galbeta(1-3)GalNAcalpha1-R
UDP + GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-3)GalNAcalpha1-R
-
dIGnT
-
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta(1-3)Galbeta(1-4)Glc
UDP + GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)Glc
-
dIGnT
-
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta(1-3)Galbeta(1-4)Glc(NAc)beta1-R
UDP + GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)Glc(NAc)beta1-R
-
dIGnT
-
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
UDP + GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)GlcNAc
-
very poor acceptor, reaction rate is 2% of that with GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
-
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Gal
?
-
poor acceptor, reaction rate is 6% of that with GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
-
-
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
UDP + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)Glc
UDP-N-acetyl-D-glucosamine + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
UDP + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)GlcNAc
UDP-N-acetyl-D-glucosamine + GlcNAcbeta1-3Galbeta1-4Glc-2-aminopyridine
UDP + GlcNAcbeta1-3(GlcNAcbeta1-6)Galbeta1-4Glc-2-aminopyridine
-
-
-
?
UDP-N-acetyl-D-glucosamine + lactose
UDP + GlcNAcbeta(1-6)Galbeta(1-4)Glc
-
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyllactosamine
UDP + GlcNAcbeta(1-6)Galbeta(1-4)GlcNAc
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + NeuAcalpha(2-3)Galbeta(1-4)GlcNacbeta(1-3)Galbeta(1-4)Glc
?
UDP-N-acetyl-D-glucosamine + NeuAcalpha(2-6)Galbeta(1-4)GlcNacbeta(1-3)Galbeta(1-4)Glc
?
UDP-N-acetyl-D-glucosamine + oligo-N-acetyllactosaminoglycan
?
-
involved in midchain branching of oligo-N-acetyllactosaminoglycans by transferring GlcNAc in beta1,6-linkage to internal galactose residues
-
-
?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosaminoglycan
?
-
might function in biosynthesis of cell surface polylactosaminoglycans on Novikoff cells and blood group I antigenic structures, formation of the GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Gal-R branching points in the branched type of polylactosylaminoglycans
-
-
?
UDP-N-acetyl-D-glucosamine + porcine submaxillary asialo-afuco-mucin
UDP + N-acetylglucosaminylated porcine submaxillary asialo-afuco-mucin
-
poor acceptor, Galbeta(1-3)GalNAc as terminal acceptor structure
-
-
?
UDP-N-acetyl-D-glucosamine + pyridylaminated Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
UDP + pyridylaminated Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)Glc
-
i.e. pyridylaminated lacto-N-neotetraose, cIGnT6
-
?
additional information
?
-
UDP-N-acetyl-D-glucosamine + asialo-alpha1-acid glycoprotein
UDP + N-acetylglucosaminylated asialo-alpha1-acid glycoprotein
-
acts on beta-galactosyl-1,4-N-acetylglucosaminyl-termini on asialo-alpha1-acid glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + asialo-alpha1-acid glycoprotein
UDP + N-acetylglucosaminylated asialo-alpha1-acid glycoprotein
-
acts on beta-galactosyl-1,4-N-acetylglucosaminyl-termini on asialo-alpha1-acid glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + asialo-alpha1-acid glycoprotein
UDP + N-acetylglucosaminylated asialo-alpha1-acid glycoprotein
-
GlcNAc residues are introduced to position C-6 of the terminal galactose of the glycoprotein, relative high activity towards asialo-alpha1-acid glycoprotein in Novikoff ascites tumor cells
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
-
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
-
acts on beta-galactosyl-1,4-N-acetylglucosaminyl-termini on asialo-alpha1-acid glycoproteins
-
?
UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
-
acts on beta-galactosyl-1,4-N-acetylglucosaminyl-termini on asialo-alpha1-acid glycoproteins
-
?
UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
-
GlcNAc residues are introduced to position C-6 of the terminal galactose of the glycoprotein
-
?
UDP-N-acetyl-D-glucosamine + Galalpha(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
?
IGnT A: at 256% of the rate with lacto-N-neotetraose
-
-
?
UDP-N-acetyl-D-glucosamine + Galalpha(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
?
IGnT B: at 148% of the rate with lacto-N-neotetraose
-
-
?
UDP-N-acetyl-D-glucosamine + Galbeta(1-3)GlcNAcbeta(1-3)Galbeta(1-4)Glc
?
poor substrate
-
-
?
UDP-N-acetyl-D-glucosamine + Galbeta(1-3)GlcNAcbeta(1-3)Galbeta(1-4)Glc
?
IGnT B: at 6% of the rate with lacto-N-neotetraose
-
-
?
UDP-N-acetyl-D-glucosamine + Galbeta(1-3)GlcNAcbeta(1-3)Galbeta(1-4)Glc
?
IGnT A: at 4% of the rate with lacto-N-neotetraose
-
-
?
UDP-N-acetyl-D-glucosamine + Galbeta(1-3)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
?
poor substrate
-
-
?
UDP-N-acetyl-D-glucosamine + Galbeta(1-3)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
?
IGnT B: at 10% of the rate with lacto-N-neotetraose
-
-
?
UDP-N-acetyl-D-glucosamine + Galbeta(1-3)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
?
IGnT A: at 6% of the rate with lacto-N-neotetraose
-
-
?
UDP-N-acetyl-D-glucosamine + Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
UDP + Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)GlcNAc
-
cIGnT
-
?
UDP-N-acetyl-D-glucosamine + Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
UDP + Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)GlcNAc
-
cIGnT6
-
?
UDP-N-acetyl-D-glucosamine + Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
UDP + Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
IGnT B: at 181% of the rate with lacto-N-neotetraose
IGnT B: major product, minor product is Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)Glc, IGnT B forms beta-1,6 branch in both of the internal galactosyl residues, prolonged incubation results in di-branched oligosaccharide
?
UDP-N-acetyl-D-glucosamine + Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
UDP + Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
IGnT A: at 170% of the rate with lacto-N-neotetraose
-
?
UDP-N-acetyl-D-glucosamine + Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
UDP + Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
i.e. para-lacto-N-neohexaose
-
?
UDP-N-acetyl-D-glucosamine + Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
UDP + Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
i.e. para-lacto-N-neohexaose
IGnT B: major product, minor product is Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)Glc, IGnT B forms beta-1,6 branch in both of the internal galactosyl residues, prolonged incubation results in di-branched oligosaccharide
?
UDP-N-acetyl-D-glucosamine + Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
UDP + Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
IGnT B: at 164% of the rate with lacto-N-neotetraose
-
-
?
UDP-N-acetyl-D-glucosamine + Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
UDP + Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
IGnT A: at 194% of the rate with lacto-N-neotetraose
-
-
?
UDP-N-acetyl-D-glucosamine + Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
UDP + Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
-
cIGnT6
cIGnT6, 60% of the heptasaccharide product, 40% of the heptasaccharide product is Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)GlcNAc, 95% heptasaccharide and 5% di-branched octasaccharide product
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
UDP + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)Glc
-
reaction rate is 41% of that with GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
-
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
UDP + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)Glc
IGnT A: at 22% of the rate with lacto-N-neotetraose
only product
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
UDP + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)Glc
IGnT B: at 41% of the rate with lacto-N-neotetraose
only product
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
UDP + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)GlcNAc
-
GlcNAc residue at the reducing end side of the branching galactose plays a role in the reaction
-
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
UDP + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)GlcNAc
-
cIGnT6
-
?
UDP-N-acetyl-D-glucosamine + NeuAcalpha(2-3)Galbeta(1-4)GlcNacbeta(1-3)Galbeta(1-4)Glc
?
IGnT B: at 123% of the rate with lacto-N-neotetraose
-
-
?
UDP-N-acetyl-D-glucosamine + NeuAcalpha(2-3)Galbeta(1-4)GlcNacbeta(1-3)Galbeta(1-4)Glc
?
IGnT A: at 35% of the rate with lacto-N-neotetraose
-
-
?
UDP-N-acetyl-D-glucosamine + NeuAcalpha(2-6)Galbeta(1-4)GlcNacbeta(1-3)Galbeta(1-4)Glc
?
IGnT A: at 256% of the rate with lacto-N-neotetraose
-
-
?
UDP-N-acetyl-D-glucosamine + NeuAcalpha(2-6)Galbeta(1-4)GlcNacbeta(1-3)Galbeta(1-4)Glc
?
IGnT B: at 148% of the rate with lacto-N-neotetraose
-
-
?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
-
forms branches in poly-N-acetyllactosamines
-
-
?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
-
transfer of GlcNAc to beta1,4-linked Gal residue in a linear poly-N-acetyllactosamine with the approximate structure Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc(NAc)-R, forming Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)Glc(NAc)-R
-
-
?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
-
cIGnT6 transfers one or multiple GlcNAc branches to midchain galactoses of long linear polylactosamines
-
-
?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
-
IGnT
-
-
?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
-
responsible for the conversion of linear to branched polylactosamines, cIGnT6 actions at central rather than peridistal galactose residues of linear polylactosamines in the biosynthesis of blood group I antigens
-
-
?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
-
forms branches in poly-N-acetyllactosamines
-
-
?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
forms branches in poly-N-acetyllactosamines
-
-
?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
-
forms branches in poly-N-acetyllactosamines, which bear the I blood group antigen
-
-
?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
forms branches in poly-N-acetyllactosamines, which bear the I blood group antigen
-
-
?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
-
cIGnT6
-
-
?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
-
forms branches in poly-N-acetyllactosamines
-
-
?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
-
responsible for the formation of the beta1-6-branched poly-N-acetyllactosamine structure, involved in generating branches to central positions of preformed as well as growing polylactosamine chains but not in synthesizing the distal branches to growing chains
-
-
?
additional information
?
-
-
2 types of branching enzyme activities: cIGnT6 generates beta-1,6-N-acetylglucosaminyl branches at the central galactose residue, and dIGnT6 acts on peridistal galactose residues
-
-
?
additional information
?
-
-
2 types of branching enzyme activities: cIGnT6 generates beta-1,6-N-acetylglucosaminyl branches at the central galactose residue, and dIGnT6 acts on peridistal galactose residues
-
-
?
additional information
?
-
-
no substrate of cIGnT6: GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc, Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)(Fucalpha(1-3))GlcNAc, no transfer of GlcNAc to substrates with alpha1-3-fucosyl residues and to midchain galactoses that belongs to Lewis x determinants
-
-
?
additional information
?
-
-
initiates formation of side chains, key enzyme in biosynthesis of I antigen of erythrocytes, N-acetyllactosamine is a more physiological acceptor than lactose
-
-
?
additional information
?
-
-
expression of I-antigen is entirely dependent on IGnT, expression of IGnT is developmentally regulated
-
-
?
additional information
?
-
-
C2GnT forms the core 2 O-glycan branch, which is critical for oligosaccharide-mediated cell-cell interaction, IGnT forms the I antigen, both are members of a beta-1,6-N-acetylglucosaminyltransferase gene family
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
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2 isoforms IGnT A and IGnT B, C-terminal 1/4 of IGnT B is identical to that of IGnT A, the rest of the sequences shows 63% identity
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additional information
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2 isoforms IGnT A and IGnT B, C-terminal 1/4 of IGnT B is identical to that of IGnT A, the rest of the sequences shows 63% identity
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additional information
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2 isoforms IGnT A and IGnT B, C-terminal 1/4 of IGnT B is identical to that of IGnT A, the rest of the sequences shows 63% identity
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additional information
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generally, oligosaccharides with the Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc(Nac) sequence serve as good substrates, addition of Galalpha(1-3) or sialic acid alpha(2-6) to the non-reducing end gelactose enhances the acceptor activity, while sialic acid alpha2-3 linkage shows a repressive effect, no substrate: N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucose
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additional information
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generally, oligosaccharides with the Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc(Nac) sequence serve as good substrates, addition of Galalpha(1-3) or sialic acid alpha(2-6) to the non-reducing end gelactose enhances the acceptor activity, while sialic acid alpha2-3 linkage shows a repressive effect, no substrate: N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucose
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additional information
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a major enzyme involved in the branching of poly-N-acetyllactosamine chains in embryoglycan, branching of poly-N-acetyllactosamine chains is performed by beta1,6-N-acetylglucosaminylation of the galactosyl residue
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additional information
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the enzyme should mostly be responsible for making distal I-branch structures on poly-N-acetyllactosamine sequences in small intestine, as well as making mucin core 2 and core 4 structures, it alos has high C2/C4GnT activities
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additional information
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the enzyme also shows C2GnT activity and C4GnT activity
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additional information
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2 types of branching enzyme activities: cIGnT6 generates beta-1,6-N-acetylglucosaminyl branches at the central galactose residue, and dIGnT6 acts on peridistal galactose residues
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additional information
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2 types of branching enzyme activities: cIGnT6 generates beta-1,6-N-acetylglucosaminyl branches at the central galactose residue, and dIGnT6 acts on peridistal galactose residues
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additional information
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absolute requirement of at least a complete Galbeta(1-4)GlcNAc residue bound to position 3 of the acceptor Gal residues, i.e. it is capable of acting only on the Gal residues of internal Galbeta(1-4)GlcNAc units, no substrates: pyridylaminated GlcNAcbeta(1-3)Galbeta(1-4)Glc and pyridylaminated Galbeta(1-3)GlcNAcbeta(1-3)Galbeta(1-4)Glc, 4 major groups according to their acceptor specificities: blood group I structure: IGnT6, core 2 in O-glycans: C2GnT6, core 4 in O-glycans: C4GnT6, 2,6-branched N-linked core: GnT V
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Breast Neoplasms
Engagement of I-Branching {beta}-1, 6-N-Acetylglucosaminyltransferase 2 in Breast Cancer Metastasis and TGF-{beta} Signaling.
Breast Neoplasms
I-branching N-acetylglucosaminyltransferase regulates prostate cancer invasiveness by enhancing ?5?1 integrin signaling.
Carcinoma
GCNT2 induces epithelial-mesenchymal transition and promotes migration and invasion in esophageal squamous cell carcinoma cells.
Cataract
A nonsense mutation in the glucosaminyl (N-acetyl) transferase 2 gene (GCNT2): association with autosomal recessive congenital cataracts.
Cataract
An Alu repeat-mediated genomic GCNT2 deletion underlies congenital cataracts and adult i blood group.
Cataract
An update on the I blood group system.
Cataract
Autosomal recessive congenital cataract in captive-bred vervet monkeys (Chlorocebus aethiops).
Cataract
Case report of homozygous deletion involving the first coding exons of GCNT2 isoforms A and B and part of the upstream region of TFAP2A in congenital cataract.
Cataract
Clinical and genetic characteristics of Chinese patients with familial or sporadic pediatric cataract.
Cataract
Correction: Deletion at the GCNT2 Locus Causes Autosomal Recessive Congenital Cataracts.
Cataract
Deletion at the GCNT2 Locus Causes Autosomal Recessive Congenital Cataracts.
Cataract
High Throughput Genetic Screening of 51 Paediatric Cataract Genes Identifies Causative Mutations in Inherited Paediatric Cataract in South Eastern Australia.
Cataract
Phenotypes of Recessive Pediatric Cataract in a Cohort of Children with Identified Homozygous Gene Mutations (An American Ophthalmological Society Thesis).
Cataract
Scanning 17 candidate genes for association with primary cataracts in the wire-haired Dachshund.
Colonic Neoplasms
An update on the I blood group system.
Colonic Neoplasms
Downregulation of miR-199a/b-5p is associated with GCNT2 induction upon epithelial-mesenchymal transition in colon cancer.
Esophageal Squamous Cell Carcinoma
GCNT2 induces epithelial-mesenchymal transition and promotes migration and invasion in esophageal squamous cell carcinoma cells.
Lymphatic Metastasis
Aberrant Methylation of GCNT2 Is Tightly Related to Lymph Node Metastasis of Primary CRC.
Lymphoma, T-Cell, Cutaneous
Oncogenomic analysis identifies novel biomarkers for tumor stage mycosis fungoides.
Melanoma
An update on the I blood group system.
Melanoma
Loss of GCNT2/I-branched glycans enhances melanoma growth and survival.
Melanoma
Melanoma-associated glycosyltransferase GCNT2 as an emerging biomarker and therapeutic target.
Neoplasm Metastasis
Aberrant Methylation of GCNT2 Is Tightly Related to Lymph Node Metastasis of Primary CRC.
Neoplasm Metastasis
Engagement of I-Branching {beta}-1, 6-N-Acetylglucosaminyltransferase 2 in Breast Cancer Metastasis and TGF-{beta} Signaling.
Neoplasms
An update on the I blood group system.
Neoplasms
GCNT2 induces epithelial-mesenchymal transition and promotes migration and invasion in esophageal squamous cell carcinoma cells.
Neoplasms
I-branched carbohydrates as emerging effectors of malignant progression.
Prostatic Neoplasms
Determination of carbohydrate structure recognized by prostate-specific F77 monoclonal antibody through expression analysis of glycosyltransferase genes.
Prostatic Neoplasms
I-branching N-acetylglucosaminyltransferase regulates prostate cancer invasiveness by enhancing ?5?1 integrin signaling.
Pulmonary Disease, Chronic Obstructive
Epithelial-Mesenchymal Transition Gene Signature Related to Prognostic in Colon Adenocarcinoma.
Stomach Neoplasms
Gastric Cancer Heterogeneity and Clinical Outcomes.
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malfunction
C2GnT2 deficiency, impair of mucosal barrier, increase of susceptibility to colitis, reduced immunoglobulin abundance, loss of all core 4 O-glycan biosynthetic activity
malfunction
analysis of pleiotropic effect of mutations in GCNT2, especially frameshift mutation N388R, causing congenital cataract and a rare adult I blood group phenotype, detailed overview
malfunction
ectopic overexpression of GCNT2 enhances cell detachment, adhesion to endothelial cells, cell migration and invasion in vitro, and lung metastasis of breast cancer cells in vivo. Knockdown of GCNT2 expression decreases cell migration and invasion in vitro and lung metastasis in vivo. Diminution of the glycosyltransferase activity of I-branching beta-1,6-N-acetylglucosaminyl transferase 2 (GCNT2) abrogates its cell migration and invasion-promoting function and synergistic effect with TGF-beta to induce EMT, effect of GCNT2 expression knockdown on oncogenic properties, overview
malfunction
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GCNT3 overexpression reduces 5-fluorouracil resistance in colorectal cancer (CRC) cells. GCNT3 overexpression reduces proliferation, invasion and changes metabolic capacities of CRC cells. The enzyme's overexpression in epithelial ovarian cancer (EOC) patients is associated with better clinical outcome and response to initial therapy
malfunction
in mouse pancreatic cancer tumors, GCNT3 upregulation is correlated with increased expression of mucins. Aberrant GCNT3 expression is associated with increased mucin production, aggressive tumorigenesis, and reduced survival. CRISPR-mediated knockout of GCNT3 in pancreatic cancer cells reduced proliferation and spheroid formation
malfunction
manipulation of I-branching N-acetylglucosaminyltransferase (GCNT2) expression in esophageal squamous cell carcinoma cells has no effect on cell proliferation. Overexpression of GCNT2 promotes the migration and invasion, and this effect is associated with increased expression of N-cadherin and vimentin and decreased expression of E-cadherin in KYSE30 and EC9706 cells. Knockdown of GCNT2 decreased the expression of N-cadherin and vimentin, increases the expression of E-cadherin, and inhibits the migration and invasion in KYSE150 and EC109 cells
malfunction
miR-BART1-5p directly targets GCNT3. In addition, miR-BART1-5p mimics transfection is observed to reduce cell proliferation and migration, while miR-BART1-5p inhibitor increases cell proliferation and migration following transfection. In conclusion, both miR-BART1-5p and knockdown of GCNT3 inhibit cell proliferation and migration
malfunction
talniflumate alone and in combination with low-dose gefitinib reduces GCNT3 expression, leading to the disrupted production of mucins in vivo and in vitro. Aberrant GCNT3 expression is associated with increased mucin production, aggressive tumorigenesis, and reduced patient survival. CRISPR-mediated knockout of GCNT3 in pancreatic cancer cells reduced proliferation and spheroid formation
malfunction
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in mouse pancreatic cancer tumors, GCNT3 upregulation is correlated with increased expression of mucins. Aberrant GCNT3 expression is associated with increased mucin production, aggressive tumorigenesis, and reduced survival. CRISPR-mediated knockout of GCNT3 in pancreatic cancer cells reduced proliferation and spheroid formation
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metabolism
GCNT2 is a direct target of the TGF-beta-smad pathway and that change in GCNT2 expression modulates EMT induced by TGF-beta1 treatment. Involvement of GCNT2 in EMT and TGF-beta signaling, and further glycosylation modification of E-cadherin by GCNT2, are the underlying integrative mechanisms for breast cancer metastasis. GCNT2 contributes to distal metastasis in vivo
metabolism
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integrated transcriptomic and proteomic analyses reveal that GCNT3 is linked to cellular cycle, mitosis and proliferation, response to drugs and metabolism pathways. The vascular epithelial growth factor A (VEGFA) arises as an attractive partner of GCNT3 functions in cell invasion and resistance
physiological function
core 2 beta-1,6-N-acetylglucosaminyltransferase (GCNT3) is a core mucin-synthesizing enzyme
physiological function
core 2 beta-1,6-N-acetylglucosaminyltransferase (GCNT3) is a core mucin-synthesizing enzyme. Correlations between GCNT3 expression and pancreatic tumor progression, Kaplan-Meier analysis of patients' survival by GCNT3 expression level, overview
physiological function
GCNT2 is a gene contributing to breast cancer metastasis with preferential expression in basal-like breast cancer. GCNT2 induces epithelial-mesenchymal transition and promotes migration and invasion in esophageal squamous cell carcinoma cells. Involvement of GCNT2 in the epithelial-to-mesenchymal transition (EMT). Specifically, the expression of E-cadherin is significantly changed upon GCNT2 expression at the protein level but not at the RNA level
physiological function
O-glycan synthase glucosamine (N-acetyl)transferase 3 (GCNT3) is a mucin-type responsible for catalyzing core 2 and core 4 O-glycans and forming O-linked glycosylation in protein biosynthesis. Abnormal expression of GCNT3 promotes the progression of several human cancers. GCNT3 expression in Epstein-Barr virus (EBV)-associated gastric cancer cells and tissues is lower than in EBV-negative gastric cancer cells and tissues, and high expression is significantly associated with advanced tumor-lymph node metastasis. EBV may regulate GCNT3 by affecting the NF-kappaB signaling pathway. Patients with EBV-associated gastric cancer (EBVaGC) have a good survival rate. EBV potentially regulates GCNT3 by affecting the NF-kappaB signaling pathway
physiological function
overall survival is significantly lower in esophageal squamous cell carcinoma patients with high GCNT2 expression than those with low GCNT2 expression
physiological function
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the mucin-type core 2 1,6-N-acetylglucosaminyltransferase enzyme (C2GnT-M), encoded by the GCNT3 gene, is a glycosyltransferase enzyme whose expression is altered in cancer processes. GCNT3 catalyzes the formation of core 2 O-glycan, core 4 O-glycan and I branches and its pattern of expression is mainly associated with colorectal cancer (CRC) prognosis. GCNT3 transfection in certain CRC cells reduces cell proliferation, adhesion, invasion, and induced cell death, and also inhibits tumor growth in vivo. Role of glycosyltransferase enzyme GCNT3 in colon and ovarian cancer prognosis and chemoresistance, overview. Integrated transcriptomic and proteomic analyses reveal that GCNT3 is linked to cellular cycle, mitosis and proliferation, response to drugs and metabolism pathways. GCNT3 overexpression contributes to reduce 5-fluorouracil resistance in metastatic CRC cells. GCNT3 also diminishes cell invasion and VEGFA expression in EOC cells. GCNT3 is a cancer prognostic factor. GCNT3 diminishes cell proliferation, invasion and alters metabolic properties of CRC cells. GCNT3 high-expressing Stage III-IV EOC patients have better response to conventional treatment and clinical outcome
physiological function
-
core 2 beta-1,6-N-acetylglucosaminyltransferase (GCNT3) is a core mucin-synthesizing enzyme
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Van den Eijnden, D.H.; Winterwerp, H.; Smeeman, P.; Schiphorst, W.E.C.M.
Novikoff ascites tumor cells contain N-acetyllactosaminide beta 1-3 and beta 1-6 N-acetylglucosaminyltransferase activity
J. Biol. Chem.
258
3435-3437
1983
Rattus norvegicus
brenda
Leppänen, A.; Penttilä, L.; Niemelä, R.; Helin, J.; Seppo, A.; Lusa, S.; Renkonen, O.
Human serum contains a novel beta 1,6-N-acetylglucosaminyltransferase activity that is involved in midchain branching of oligo (N-acetyllactosaminoglycans)
Biochemistry
30
9287-9296
1991
Homo sapiens
brenda
Zielenski, J.; Koscielak, J.
The occurrence of two novel N-acetylglucosaminyltransferase activities in human serum
FEBS Lett.
158
164-168
1983
Homo sapiens
brenda
Chen, G.Y.; Kurosawa, N.; Muramatsu, T.
Functional analysis of promoter activity of murine beta-1,6-N-acetylglucosaminyltransferase
Gene
275
253-259
2001
Mus musculus
brenda
Chen, G.Y.; Kurosawa, N.; Muramatsu, T.
A novel variant form of murine beta-1,6-N-acetylglucosaminyltransferase forming branches in poly-N-acetyllactosamines
Glycobiology
10
1001-1011
2000
Mus musculus (A2IQH4), Mus musculus (A2IQH5)
brenda
Bierhuizen, M.F.A.; Maemura, K.; Kudo, S.; Fukuda, M.
Genomic organization of core 2 and I branching beta-1,6-N-acetylglucosaminyltransferases. Implication for evolution of the beta-1,6-N-acetylglucosaminyltransferase gene family
Glycobiology
5
417-425
1995
Homo sapiens
brenda
Mattila, P.; Salminen, H.; Hirvas, L.; Niittymäki, J.; Salo, H.; Niemelä, R.; Fukuda, M.; Renkonen, O.; Renkonen, R.
The centrally acting beta1,6N-acetylglucosaminyltransferase (GlcNAc to Gal). Functional expression, purification, and acceptor specificity of a human enzyme involved in midchain branching of linear poly-N-acetyllactosamines
J. Biol. Chem.
273
27633-27639
1998
Homo sapiens
brenda
Sakamoto, Y.; Taguchi, T.; Tano, Y.; Ogawa, T.; Leppänen, A.; Kinnunen, M.; Aitio, O.; Parmanne, P.; Renkonen, O.; Taniguchi, N.
Purification and characterization of UDP-GlcNAc:Galb1-4-GlcNAcb1-3*Galb1-4Glc(NAc)-R(GlcNAc to *Gal) beta1,6N-acetylglucosaminyltransferase from hog small intestine
J. Biol. Chem.
273
27625-27632
1998
Sus scrofa
brenda
Fukuda, M.
beta6-N-acetylglucosaminyltransferase (IGnT)
Handbook of Glycosyltransferases and Related Genes
2002
125-132
2002
Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
-
brenda
Bennett, E.M.; Ekstrom, J.L.; Pegg, A.E.; Ealick, S.E.
Monomeric S-adenosylmethionine decarboxylase from plants provides an alternative to putrescine stimulation
Biochemistry
41
14509-14517
2002
Solanum tuberosum
brenda
Korekane, H.; Taguchi, T.; Sakamoto, Y.; Honke, K.; Dohmae, N.; Salminen, H.; Toivonen, S.; Helin, J.; Takio, K.; Renkonen, O.; Taniguchi, N.
Purification and cDNA cloning of UDP-GlcNAc:GlcNAcbeta1-3Galbeta1-4Glc(NAc)-R [GlcNAc to Gal] beta1,6N-acetylglucosaminyltransferase from rat small intestine: A major carrier of dIGnT activity in rat small intestine
Glycobiology
13
387-400
2003
Rattus norvegicus (Q8CH87)
brenda
Li, C.; Wu, Q.
Adaptive evolution of multiple-variable exons and structural diversity of drug-metabolizing enzymes
BMC Evol. Biol.
7
69
2007
Danio rerio, Canis lupus familiaris, Gallus gallus, Homo sapiens, Macaca mulatta, Mus musculus, Pan troglodytes, Rattus norvegicus, Monodelphis domestica, Xenopus tropicalis
brenda
Muramatsu, H.; Kusano, T.; Sato, M.; Oda, Y.; Kobori, K.; Muramatsu, T.
Embryonic stem cells deficient in I beta1,6-N-acetylglucosaminyltransferase exhibit reduced expression of embryoglycan and the loss of a Lewis X antigen, 4C9
Glycobiology
18
242-249
2008
Mus musculus
brenda
Stone, E.L.; Ismail, M.N.; Lee, S.H.; Luu, Y.; Ramirez, K.; Haslam, S.M.; Ho, S.B.; Dell, A.; Fukuda, M.; Marth, J.D.
Glycosyltransferase function in core 2-type protein O glycosylation
Mol. Cell. Biol.
29
3770-3782
2009
Mus musculus (Q5JCT0)
brenda
Zhang, H.; Meng, F.; Wu, S.; Kreike, B.; Sethi, S.; Chen, W.; Miller, F.R.; Wu, G.
Engagement of I-branching beta-1,6-N-acetylglucosaminyltransferase 2 in breast cancer metastasis and TGF-beta signaling
Cancer Res.
71
4846-4856
2011
Homo sapiens (Q8N0V5)
-
brenda
Rao, C.V.; Janakiram, N.B.; Madka, V.; Kumar, G.; Scott, E.J.; Pathuri, G.; Bryant, T.; Kutche, H.; Zhang, Y.; Biddick, L.; Gali, H.; Zhao, Y.D.; Lightfoot, S.; Mohammed, A.
Small-molecule inhibition of GCNT3 disrupts mucin biosynthesis and malignant cellular behaviors in pancreatic cancer
Cancer Res.
76
1965-1974
2016
Homo sapiens (O95395), Mus musculus (Q5JCT0), Mus musculus C5BL/6 (Q5JCT0)
brenda
Peng, F.; He, Q.; Cheng, C.; Pan, J.
GCNT2 induces epithelial-mesenchymal transition and promotes migration and invasion in esophageal squamous cell carcinoma cells
Cell Biochem. Funct.
37
42-51
2019
Homo sapiens (Q8N0V5), Homo sapiens
brenda
Cheong, S.S.; Hull, S.; Jones, B.; Chana, R.; Thornton, N.; Plagnol, V.; Moore, A.T.; Hardcastle, A.J.
Pleiotropic effect of a novel mutation in GCNT2 causing congenital cataract and a rare adult i blood group phenotype
Hum. Genome Var.
4
17004
2017
Homo sapiens (Q8N0V5)
brenda
Fernandez, L.P.; Sanchez-Martinez, R.; Vargas, T.; Herranz, J.; Martin-Hernandez, R.; Mendiola, M.; Hardisson, D.; Reglero, G.; Feliu, J.; Redondo, A.; Ramirez de Molina, A.
The role of glycosyltransferase enzyme GCNT3 in colon and ovarian cancer prognosis and chemoresistance
Sci. Rep.
8
8485
2018
Homo sapiens
brenda
Liu, J.; Zhang, Y.; Liu, W.; Zhang, Q.; Xiao, H.; Song, H.; Luo, B.
MiR-BART1-5p targets core 2beta-1,6-acetylglucosaminyltransferase GCNT3 to inhibit cell proliferation and migration in EBV-associated gastric cancer
Virology
541
63-74
2020
Homo sapiens (O95395)
brenda