Information on EC 2.4.1.150 - N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
2.4.1.150
-
RECOMMENDED NAME
GeneOntology No.
N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
show the reaction diagram
-
-
-
-
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
show the reaction diagram
mechanism, model for regulation by putrescine
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Glycosphingolipid biosynthesis - lacto and neolacto series
-
Metabolic pathways
-
terminal O-glycans residues modification
-
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-glucosamine:beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminide 6-beta-N-acetyl-D-glucosaminyltransferase
Acts on beta-galactosyl-1,4-N-acetylglucosaminyl termini on asialo-alpha1-acid glycoprotein.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
acetylglucosaminyltransferase, uridine diphosphoacetylglucosamine-acetyllactosaminide beta1-->6-
-
-
-
-
beta1-6GnT
-
-
-
-
C2GnT2
Q5JCT0
-
Galbeta1-->4GlcNAc-R beta1-->6 N-acetylglucosaminyltransferase
-
-
-
-
Gcnt2 gene product
-
-
Gcnt2 gene product
-
gene contains one variable exon and two constant exons
gcnt3
Q5JCT0
-
I beta1,6-N-acetylglucosaminyltransferase
-
-
I N-acetylglucosaminyltransferase
-
-
-
-
IGnT
-
-
-
-
N-acetylglucosaminyltransferase
-
-
-
-
UDP-GlcNAc:Gal-R, beta-D-6-N-acetylglucosaminyltransferase
-
-
-
-
uridine diphosphoacetylglucosamine-acetyllactosaminide beta1-->6-acetylglucosaminyltransferase
-
-
-
-
additional information
-
C2GnT forms the core 2 O-glycan branch, IGnT forms the I antigen, both are members of a beta-1,6-N-acetylglucosaminyltransferase gene family
CAS REGISTRY NUMBER
COMMENTARY
85638-40-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
gene contains three highly similar variable exons and two constant exons, each variable exon is preceded by a distinct promoter and is separately spliced to a set of two constant exons to generate functional Gcnt2 mRNA
-
-
Manually annotated by BRENDA team
gene contains two highly similar variable exons and two constant exons, each variable exon is preceded by a distinct promoter and is separately spliced to a set of two constant exons to generate functional Gcnt2 mRNA
-
-
Manually annotated by BRENDA team
gene contains three highly similar variable exons and two constant exons, each variable exon is preceded by a distinct promoter and is separately spliced to a set of two constant exons to generate functional Gcnt2 mRNA
-
-
Manually annotated by BRENDA team
gene contains three highly similar variable exons and two constant exons, each variable exon is preceded by a distinct promoter and is separately spliced to a set of two constant exons to generate functional Gcnt2 mRNA
-
-
Manually annotated by BRENDA team
gene contains two highly similar variable exons and two constant exons, each variable exon is preceded by a distinct promoter and is separately spliced to a set of two constant exons to generate functional Gcnt2 mRNA
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
gene contains three highly similar variable exons and two constant exons, each variable exon is preceded by a distinct promoter and is separately spliced to a set of two constant exons to generate functional Gcnt2 mRNA
-
-
Manually annotated by BRENDA team
IGnT A, 2 isoenzymes: IGnT A and B
UniProt
Manually annotated by BRENDA team
IGnT B, 2 isoenzymes: IGnT A and B
UniProt
Manually annotated by BRENDA team
gene contains three highly similar variable exons and two constant exons, each variable exon is preceded by a distinct promoter and is separately spliced to a set of two constant exons to generate functional Gcnt2 mRNA
-
-
Manually annotated by BRENDA team
gene contains three highly similar variable exons and two constant exons, each variable exon is preceded by a distinct promoter and is separately spliced to a set of two constant exons to generate functional Gcnt2 mRNA
-
-
Manually annotated by BRENDA team
Sprague Dawley rats
-
-
Manually annotated by BRENDA team
gene contains two highly similar variable exons and two constant exons, each variable exon is preceded by a distinct promoter and is separately spliced to a set of two constant exons to generate functional Gcnt2 mRNA
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
Q5JCT0
C2GnT2 deficiency, impair of mucosal barrier, increase of susceptibility to colitis, reduced immunoglobulin abundance, loss of all core 4 O-glycan biosynthetic activity
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-glucosamine + asialo-alpha1-acid glycoprotein
UDP + N-acetylglucosaminylated asialo-alpha1-acid glycoprotein
show the reaction diagram
-
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
show the reaction diagram
-
acts on beta-galactosyl-1,4-N-acetylglucosaminyl-termini on asialo-alpha1-acid glycoproteins, 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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
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
show the reaction diagram
-
acts on beta-galactosyl-1,4-N-acetylglucosaminyl-termini on asialo-alpha1-acid glycoproteins, 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
?
show the reaction diagram
A2IQH4, A2IQH5
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
?
show the reaction diagram
A2IQH4, A2IQH5
IGnT B: at 148% of the rate with lacto-N-neotetraose
-
-
?
UDP-N-acetyl-D-glucosamine + Galalpha(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
?
show the reaction diagram
-
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
?
show the reaction diagram
A2IQH4, A2IQH5
poor substrate
-
-
?
UDP-N-acetyl-D-glucosamine + Galbeta(1-3)GlcNAcbeta(1-3)Galbeta(1-4)Glc
?
show the reaction diagram
A2IQH4, A2IQH5
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
?
show the reaction diagram
A2IQH4, A2IQH5
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
?
show the reaction diagram
A2IQH4, A2IQH5
poor substrate
-
-
?
UDP-N-acetyl-D-glucosamine + Galbeta(1-3)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
?
show the reaction diagram
A2IQH4, A2IQH5
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
?
show the reaction diagram
A2IQH4, A2IQH5
IGnT A: at 6% of the rate with lacto-N-neotetraose
-
-
?
UDP-N-acetyl-D-glucosamine + Galbeta(1-4)(Fucalpha(1-3))GlcNAcbeta(1-3)Galbeta(1-4)Glc
?
show the reaction diagram
A2IQH4, A2IQH5
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
show the reaction diagram
A2IQH4, A2IQH5
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
show the reaction diagram
-
cIGnT6
-
?
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
show the reaction diagram
-
cIGnT
-
?
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
show the reaction diagram
A2IQH4, A2IQH5
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
show the reaction diagram
A2IQH4, A2IQH5
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
show the reaction diagram
A2IQH4, A2IQH5
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
show the reaction diagram
A2IQH4, A2IQH5
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
show the reaction diagram
-
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 + 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
show the reaction diagram
A2IQH4, A2IQH5
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
show the reaction diagram
A2IQH4, A2IQH5
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)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
show the reaction diagram
-
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
show the reaction diagram
-
dIGnT
-
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta(1-3)Galbeta(1-4)Glc
UDP + GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)Glc
show the reaction diagram
-
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
show the reaction diagram
-
dIGnT
-
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
UDP + GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)GlcNAc
show the reaction diagram
-
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
?
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
A2IQH4, A2IQH5
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
show the reaction diagram
A2IQH4, A2IQH5
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
show the reaction diagram
-
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
show the reaction diagram
-
cIGnT6
-
?
UDP-N-acetyl-D-glucosamine + lactose
UDP + GlcNAcbeta(1-6)Galbeta(1-4)Glc
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyllactosamine
UDP + GlcNAcbeta(1-6)Galbeta(1-4)GlcNAc
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + NeuAcalpha(2-3)Galbeta(1-4)GlcNacbeta(1-3)Galbeta(1-4)Glc
?
show the reaction diagram
A2IQH4, A2IQH5
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
?
show the reaction diagram
A2IQH4, A2IQH5
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
?
show the reaction diagram
A2IQH4, A2IQH5
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
?
show the reaction diagram
A2IQH4, A2IQH5
IGnT B: at 148% of the rate with lacto-N-neotetraose
-
-
?
UDP-N-acetyl-D-glucosamine + oligo-N-acetyllactosaminoglycan
?
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
show the reaction diagram
-
cIGnT6
-
-
?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
show the reaction diagram
-
forms branches in poly-N-acetyllactosamines
-
-
?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
show the reaction diagram
-
forms branches in poly-N-acetyllactosamines
-
-
?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
show the reaction diagram
-
forms branches in poly-N-acetyllactosamines
-
-
?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
show the reaction diagram
A2IQH4, A2IQH5
forms branches in poly-N-acetyllactosamines
-
-
?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
show the reaction diagram
-
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
?
show the reaction diagram
-
cIGnT6 transfers one or multiple GlcNAc branches to midchain galactoses of long linear polylactosamines
-
-
?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
show the reaction diagram
-
IGnT
-
-
?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
show the reaction diagram
-
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
?
show the reaction diagram
-
forms branches in poly-N-acetyllactosamines, which bear the I blood group antigen
-
-
-
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
show the reaction diagram
A2IQH4, A2IQH5
forms branches in poly-N-acetyllactosamines, which bear the I blood group antigen
-
-
-
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
show the reaction diagram
-
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
-
-
-
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosaminoglycan
?
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
i.e. pyridylaminated lacto-N-neotetraose, cIGnT6
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
A2IQH4, A2IQH5
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
-
-
-
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
?
-
A2IQH4, A2IQH5
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
-
-
-
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
?
-
-
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
-
-
-
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
?
-
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-glucosamine + oligo-N-acetyllactosaminoglycan
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
forms branches in poly-N-acetyllactosamines, which bear the I blood group antigen
-
-
-
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
show the reaction diagram
A2IQH4, A2IQH5
forms branches in poly-N-acetyllactosamines, which bear the I blood group antigen
-
-
-
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
show the reaction diagram
-
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
-
-
-
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosaminoglycan
?
show the reaction diagram
-
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
-
-
-
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
?
-
-
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Cd2+
-
CdCl2, slightly stimulates
Mg2+
-
MgCl2, slightly stimulates
Mn2+
-
MnCl2, 10-25 mM for optimal activity required
Mn2+
-
requirement
additional information
-
no requirement for any divalent metal ions
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
AMP
-
10% inhibition
GDP
-
19% inhibition
UDP
-
most potent inhibitor of donor substrate analogues, complete inhibition
UDP-galactose
-
42% inhibition
UDP-glucose
-
51% inhibition
UDP-glucuronic acid
-
36% inhibition
UDP-hexanolamine
-
66% inhibition
UMP
-
41% inhibition
UTP
-
most potent inhibitor of donor substrate analogues, complete inhibition
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.44
-
Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
A2IQH4, A2IQH5
IGnT B
0.55
-
Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
A2IQH4, A2IQH5
IGnT B
0.52
-
NeuAcalpha(2-6)Galbeta(1-4)GlcNacbeta(1-3)Galbeta(1-4)Glc
A2IQH4, A2IQH5
IGnT B
0.96
-
pyridylaminated lacto-N-neotetraose
-
-
2.59
-
UDP-N-acetyl-D-glucosamine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.058
-
-
-
additional information
-
A2IQH4, A2IQH5
when expressed as proteins IGnT B shows higher specific activity than IGnT A; when expressed as proteins IGnT B shows higher specific activity than IGnT A
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.8
7.8
-
broad
7
-
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
37
-
-
assay at
37
-
A2IQH4, A2IQH5
assay at; assay at
37
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
IGnT is highly expressed in adult cerebellum and the frontal lobe of adult brain, also expression in fetal brain
Manually annotated by BRENDA team
-
IGnT is highly expressed in adult cerebellum
Manually annotated by BRENDA team
-
IGnT is moderately expressed in adult colon
Manually annotated by BRENDA team
-
native and knockout mutants, mutant cells exhibited a reduced capability in embryoglycan synthesis and adhere weakly to laminin-coated plates
Manually annotated by BRENDA team
A2IQH4, A2IQH5
D-3 embryonic stem cells moderately express IGnT A and B; D-3 embryonic stem cells moderately express IGnT A and B
Manually annotated by BRENDA team
-
F9 embryonal carcinoma cells moderately express IGnT A and B
Manually annotated by BRENDA team
-
IGnT is moderately expressed in adult heart
Manually annotated by BRENDA team
-
C2GnT, promyelocytic leukaemia HL-60 cells
Manually annotated by BRENDA team
-
strong expression of IGnT A and B in adults
Manually annotated by BRENDA team
A2IQH4, A2IQH5
strong expression of IGnT A and B in adults; strong expression of IGnT A and B in adults
Manually annotated by BRENDA team
-
strong expression of IGnT A and B in adults
Manually annotated by BRENDA team
A2IQH4, A2IQH5
strong expression of IGnT A and B in adults; strong expression of IGnT A and B in adults
Manually annotated by BRENDA team
-
IGnT expression in fetal kidney
Manually annotated by BRENDA team
-
strong expression of IGnT A and B in adults
Manually annotated by BRENDA team
A2IQH4, A2IQH5
strong expression of IGnT A and B in adults; strong expression of IGnT A and B in adults
Manually annotated by BRENDA team
-
IGnT expression in fetal lung
Manually annotated by BRENDA team
-
moderate expression of IGnT A and B
Manually annotated by BRENDA team
A2IQH4, A2IQH5
moderate expression of IGnT A and B; moderate expression of IGnT A and B
Manually annotated by BRENDA team
A2IQH4, A2IQH5
P-19 embryonal carcinoma cells moderately express IGnT A and B; P-19 embryonal carcinoma cells moderately express IGnT A and B
Manually annotated by BRENDA team
-
IGnT, teratocarcinoma PA-1 cells
Manually annotated by BRENDA team
-
cIGnT6, embryonal carcinoma cell line
Manually annotated by BRENDA team
-
tetracarcinoma cells, IGnT mainly acts as cIGnT, but can also act as dIGnT with 6-30% of the activity of cIGnT
Manually annotated by BRENDA team
-
IGnT is highly expressed in adult prostata
Manually annotated by BRENDA team
-
from freshly drawn human blood of healthy donors
Manually annotated by BRENDA team
-
highest enzyme activity per tissue protein
Manually annotated by BRENDA team
-
IGnT is moderately expressed in adult small intestine
Manually annotated by BRENDA team
-
cIGnT is the dominant form
Manually annotated by BRENDA team
-
moderate expression of IGnT A and B
Manually annotated by BRENDA team
A2IQH4, A2IQH5
moderate expression of IGnT A and B; moderate expression of IGnT A and B
Manually annotated by BRENDA team
-
C2GnT is highly expressed in activated T lymphocytes
Manually annotated by BRENDA team
-
C2GnT is highly expressed in
Manually annotated by BRENDA team
additional information
-
no expression of IGnT A and B in N2a cells
Manually annotated by BRENDA team
additional information
-
high expression of C2GnT in granulocyte-monocyte cell lineage
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
A2IQH4, A2IQH5
type II transmembrane topology; type II transmembrane topology
Manually annotated by BRENDA team
-
type II transmembrane topology
Manually annotated by BRENDA team
-
enzyme is concentrated in the microsome fraction
-
Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 67000-74000, glycosylated protein fused to glutathione S-transferase, size heterogenicity is at least partially due to differences in N-glycosylation, SDS-PAGE
?
-
x * 76000, SDS-PAGE under nonreducing conditions
monomer
-
cristallographic analysis
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
recombinant enzyme, expressed in SF9 insect cells as fusion protein with glutathione S-transferase has 5 potential N-glycosylation sites
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
bovine serum albumin, 2 mg/ml, preserves enzyme activity at 37°C, especially the highly purified enzyme fraction
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20°C, recombinant enzyme, a few days, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cIGnT, purified from PA-1 cells
-
purification of recombinant enzyme, expressed in SF9 insect cells as protein fused to glutathione S-transferase
-
210000fold, cIGnT6
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
C2GnT and IGnT cDNAs are cloned and sequenced, genes are both localized on chromosome 9, band q2l, genomic structures
-
cDNA encoding IGnT is cloned from PA-1 cells, 400-amino acids protein
-
IGnT6 is cloned, sequenced and cDNA encoding cIGnT6 in PA-1 cells is expressed in SF9 insect cells as protein fused to glutathione S-transferase
-
2 isoforms IGnT A and IGnT B are produced by alternative splicing of the IGnT gene, the C-terminal 1/4 of IGnT B is identical to that of IGnT A; 2 isoforms IGnT A and IGnT B are produced by alternative splicing of the IGnT gene, the C-terminal 1/4 of IGnT B is identical to that of IGnT A; IGnT A is cloned; IGnT A is cloned; IGnT B is cloned from mouse liver cDNA, nucleotide and amino acid sequence, exon organization of the IGnT gene, expression of IGnT A and B in COS-7 and CHO cells; IGnT B is cloned from mouse liver cDNA, nucleotide and amino acid sequence, exon organization of the IGnT gene, expression of IGnT A and B in COS-7 and CHO cells
A2IQH4, A2IQH5
2 isoforms IGnT A and IGnT B are produced by alternative splicing of the IGnT gene, the C-terminal 1/4 of IGnT B is identical to that of IGnT A; expression of each isoform is controlled by a different promoter, characterization of the promoters: GT boxes play crucial roles in transcriptional regulation of the genes; IGnT A is cloned
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
mutation experiments at the GT boxes of the promoters of IGnT A and B genes
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
-
cIGnT6 transfers multiple GlcNAc branches to long linear polylactosamines, a prerequisite for improving enzyme-assisted in vitro synthesis of a type of multivalent sialyl Lewis x glycans that are high affinity inhibitors of lymphocyte L-selectin, enzyme allows general polylactosamine synthesis