Information on EC 2.4.1.148 - acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.1.148
-
RECOMMENDED NAME
GeneOntology No.
acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-D-glucosamine + N-acetyl-beta-D-glucosaminyl-(1->3)-N-acetyl-D-galactosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-(1->6)-[N-acetyl-beta-D-glucosaminyl-(1->3)]-N-acetyl-D-galactosaminyl-R
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
-
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mucin core 3 and core 4 O-glycosylation
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Mucin type O-glycan biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-glucosamine:N-acetyl-beta-D-glucosaminyl-(1->3)-N-acetyl-D-galactosaminyl-R 6-beta-N-acetyl-D-glucosaminyltransferase
cf. EC 2.4.1.102 (beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase), EC 2.4.1.146 (beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase) and EC 2.4.1.147 (acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase).
CAS REGISTRY NUMBER
COMMENTARY hide
87927-98-8
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95978-15-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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the triple knockout mice lack the ability to synthesize all three known isoforms of core 2 beta1,6-N-acetylglucosaminyltransferase. This multiple deficiency causes a complete absence of core 2 O-glycans in the colon
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-glucosamine + N-acetyl-beta-D-glucosaminyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-Ser/Thr
UDP + N-acetyl-beta-D-glucosaminyl-(1->6)-[N-acetyl-beta-D-glucosaminyl-(1->3)]-N-acetyl-alpha-D-galactosaminyl-Ser/Thr
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + blood group i oligosaccharide
UDP + N-acetyl-beta-D-glucosaminyl-1,6-blood group i oligosaccharide
show the reaction diagram
-
I branching activity
-
-
?
UDP-N-acetyl-D-glucosamine + core 1 oligosaccharide
UDP + core 2 oligosaccharide
show the reaction diagram
UDP-N-acetyl-D-glucosamine + core 3 oligosaccharide
UDP + core 4 oligosaccharide
show the reaction diagram
UDP-N-acetyl-D-glucosamine + N-acetyl-beta-D-glucosaminyl-1,3-N-acetyl-alpha-D-galactosaminyl-benzyl
UDP + N-acetyl-beta-D-glucosaminyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,3)-N-acetyl-alpha-D-galactosaminyl-benzyl
show the reaction diagram
UDP-N-acetyl-D-glucosamine + N-acetyl-beta-D-glucosaminyl-1,3-N-acetyl-alpha-D-galactosaminyl-p-nitrophenol
UDP + N-acetyl-beta-D-glucosaminyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,3)-N-acetyl-alpha-D-galactosaminyl-p-nitrophenol
show the reaction diagram
recombinant chimeric soluble enzyme
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-beta-D-glucosaminyl-1,3-N-acetyl-alpha-D-galactosaminyl-phenyl
UDP + N-acetyl-beta-D-glucosaminyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,3)-N-acetyl-alpha-D-galactosaminyl-phenyl
show the reaction diagram
UDP-N-acetyl-D-glucosamine + N-acetyl-beta-D-glucosaminyl-1,3-N-acetyl-alpha-D-galactosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,3)-N-acetyl-alpha-D-galactosaminyl-R
show the reaction diagram
UDP-N-acetyl-D-glucosamine + N-acetyl-beta-D-glucosaminyl-1,3-N-acetyl-alpha-D-galactosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,3)-N-acetyl-D-alpha-galactosaminyl-R
show the reaction diagram
UDP-N-acetyl-D-glucosamine + N-acetyl-beta-D-glucosaminyl-1,3-N-acetyl-D-galactosaminyl-4-nitrophenyl
UDP + N-acetyl-beta-D-glucosaminyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,3)-N-acetyl-D-galactosaminyl-4-nitrophenyl
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-beta-D-glucosaminyl-1,3-N-acetyl-D-galactosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,3)-N-acetyl-D-galactosaminyl-R
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-glucosamine + N-acetyl-beta-D-glucosaminyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-Ser/Thr
UDP + N-acetyl-beta-D-glucosaminyl-(1->6)-[N-acetyl-beta-D-glucosaminyl-(1->3)]-N-acetyl-alpha-D-galactosaminyl-Ser/Thr
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + core 1 oligosaccharide
UDP + core 2 oligosaccharide
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + core 3 oligosaccharide
UDP + core 4 oligosaccharide
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-beta-D-glucosaminyl-1,3-N-acetyl-alpha-D-galactosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,3)-N-acetyl-alpha-D-galactosaminyl-R
show the reaction diagram
UDP-N-acetyl-D-glucosamine + N-acetyl-beta-D-glucosaminyl-1,3-N-acetyl-D-galactosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,3)-N-acetyl-D-galactosaminyl-R
show the reaction diagram
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-
-
-
?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AMP
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slight stimulation
ATP
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slight stimulation
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
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-
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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weak
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
interleukin-13
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upregulation of enzyme expression
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interleukin-4
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synergistic with retinoic acid in activating the core 4 N-acetylglucosaminyltransferase activity
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N-acetyl-D-glucosamine
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slight stimulation
retinoic acid
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upregulation of enzyme expression, synergistic with interleukin-4 in activating the core 4 N-acetylglucosaminyltransferase activity
Th2 cytokines
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upregulation of enzyme expression
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Triton X-100
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slight stimulation, 0.1% v/v
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6 - 1.8
N-acetyl-beta-D-glucosaminyl-1,3-N-acetyl-D-galactosaminyl-alpha-benzyl
2.8
UDP-N-acetyl-D-glucosamine
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mutant enzyme C217S, in 50 mM Tris (pH 7.5), at 37C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.26
UDP
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mutant enzyme C217S, in 50 mM Tris (pH 7.5), at 37C
0.23
UMP
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mutant enzyme C217S, in 50 mM Tris (pH 7.5), at 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00016
0.00017
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colon
0.00026
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enzyme activity in oviduct homogenate, substrate core 1 oligosaccharide, also including C2GnT1 activity
0.00028
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stomach
0.0003
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submaxillary gland
0.00042
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stomach
0.0018
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colon
0.00278
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stomach
3
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mutant enzyme C217S, in 50 mM Tris (pH 7.5), at 37C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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isoform C2GnT2 is highly expressed mainly in the stomach and the colon
Manually annotated by BRENDA team
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airway epithelial cell line
Manually annotated by BRENDA team
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isoform C2GnT3 is highly expressed mainly in the small intestine, liver and spleen
Manually annotated by BRENDA team
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airway epithelial cell line
Manually annotated by BRENDA team
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enzyme activity is regulated during estrous cycle, overview
Manually annotated by BRENDA team
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the enzyme forms complexes with NMIIA in Panc1-bC2GnT-M (c-Myc) cells
Manually annotated by BRENDA team
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isoform C2GnT3 is highly expressed mainly in the small intestine, liver and spleen
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
a Golgi non-matrix protein
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52479
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x * 58000, recombinant enzyme, SDS-PAGE, x * 52479, sequence calculation
58000
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x * 58000, recombinant enzyme, SDS-PAGE, x * 52479, sequence calculation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 58000, recombinant enzyme, SDS-PAGE, x * 52479, sequence calculation
additional information
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the enzyme possesses 9 cysteine residues, 8 of which forming disulfide bonds, Cys113 remains free, determination in the recombinant enzyme, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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enzyme is N-glycosylated at one or two residues N72 and/or N108
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
mutant enzyme C217S in complex with UDP, hanging drop vapor diffusion method, using 24% (w/v) polyethylene glycol 4000, 0.1 M glycine (pH 9.0) and 0.6 M LiCl
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
IgG-Sepahrose beads chromatography, gel filtration
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recombinant enzyme from CHO cell culture medium by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
functional expression in CHO cells, soluble chimeric enzyme form shows core 4 6beta-GalNAc transferase activity, DNA and amino acid sequence determination
mutant enzyme C217S is expressed in HEK-293T cells
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phylogenetic analysis, the gene Bo17, encoding the enzyme, is acquired from an ancestor of the African buffalo 1.5 million years ago
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stable expression of the enzyme, lacking the cytoplasmic tail and the transmembrane domain, in CHO cells, secretion of the fully active recombinant enzyme to the culture medium
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C217S
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the mutant is not oxidatively inactivated, and its kinetic parameters are very similar to those of the native enzyme
K401A/C217S
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catalytically inactive
R378A/C217S
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catalytically inactive
R378A/K401A/C217S
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catalytically inactive
additional information
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construction of an enzyme-deletion mutant strain, the deletion does not alter the virus replication in vitro
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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the expression of the enzyme in bladder tumors positively correlates with tumor progression