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Information on EC 2.4.1.144 - beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase and Organism(s) Homo sapiens
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2.4.1.144 beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferaseIUBMB Comments
The enzyme, found in vertebrates, participates in the processing of N-glycans in the Golgi apparatus. The residue added by the enzyme at position 4 of the beta-linked mannose of the trimannosyl core of N-glycans is known as a bisecting GlcNAc. Unlike GlcNAc residues added to other positions, it is not extended or modified. In addition, its presence prevents the action of other branching enzymes involved in the process such as GlcNAc-T IV (EC 2.4.1.145) and GlcNAc-T V (EC 2.4.1.155), and thus increased activity of GlcNAc-T III leads to a decrease in highly branched N-glycan structures.
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Word Map
- 2.4.1.144
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bisect
- n-glycans
- glycosyltransferases
- n-acetylglucosamine
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fucosyltransferase
- gnt-iv
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beta-linked
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xenoantigens
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tetraantennary
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e4-pha
- medicine
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alpha-galactosylation
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antennary
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glcnac-tiii
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trimannosyl
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erythroagglutinating
- alpha-gal
- diagnostics
- synthesis
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
gnt-iii, n-acetylglucosaminyltransferase iii, gntiii, beta1,4-n-acetylglucosaminyltransferase iii, beta-1,4-n-acetylglucosaminyltransferase iii, n-acetylglucosaminyltransferase-iii, glcnac-transferase-iii, beta-1,4-mannosyl-glycoprotein 4-beta-n-acetylglucosaminyltransferase, beta-d-mannoside beta-1,4-n-acetylglucosaminyltransferase, (gnt)-iii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylglucosaminyltransferase, uridine diphosphoacetylglucosamine-glycopeptide beta4-, III
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beta-1,4-mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase
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GnT-III
Golgi beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase III
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MGAT3
N-acetylglucosaminyltransferase III
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III
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uridine diphosphate (UDP)-N-acetylglucosamin/beta-D-mannoside beta-1,4-N-acetylglucosaminyltransferase III
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uridine diphosphoacetylglucosamine-glycopeptide beta4-acetylglucosaminyltransferase III
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GnT-III
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N-acetylglucosaminyltransferase III
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N-acetylglucosaminyltransferase III
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-alpha-D-glucosamine:beta-D-mannosyl-glycoprotein 4-beta-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
The enzyme, found in vertebrates, participates in the processing of N-glycans in the Golgi apparatus. The residue added by the enzyme at position 4 of the beta-linked mannose of the trimannosyl core of N-glycans is known as a bisecting GlcNAc. Unlike GlcNAc residues added to other positions, it is not extended or modified. In addition, its presence prevents the action of other branching enzymes involved in the process such as GlcNAc-T IV (EC 2.4.1.145) and GlcNAc-T V (EC 2.4.1.155), and thus increased activity of GlcNAc-T III leads to a decrease in highly branched N-glycan structures.
CAS REGISTRY NUMBER
COMMENTARY
83744-93-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-D-glucose + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(beta-D-glucosyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
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?
UDP-D-glucose + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(beta-D-glucosyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
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?
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[Notch receptor]
UDP + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-[beta-D-GlcNAc-(1->4)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[Notch receptor]
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?
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
UDP + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-[beta-D-GlcNAc-(1->4)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-N-acetyl-D-glucosaminyl-2-aminopyridine
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-N-acetyl-D-glucosaminyl-2-aminopyridine
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ir
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP-N-acetyl-D-glucosamine + beta-D-mannosyl-R
UDP + 4-(N-acetyl-beta-D-glucosaminyl)-beta-D-mannosyl-R
UDP-N-acetyl-D-glucosamine + E-cadherin
UDP + E-cadherin with bisecting N-acetyl-D-glucosamine
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recombinant enzyme expressed in murine lung melanoma cells
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?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta(1->2)Manalpha(1->6)(GlcNAcbeta(1->2)Manbeta(1->3)Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc-NH(CH2)4NH(2-pyridyl)
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?
UDP-N-acetyl-D-glucosamine + GnGnbi-PA
UDP + 4-(N-acetyl-beta-D-glucosaminyl)-GnGnbi-PA
the bi-branched N-glycan carrying a pyridylamino (PA) group at the reducing terminus (GnGnbi-PA) serves as a typical acceptor substrate and UDP-GlcNAc as a donor substrate
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?
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
UDP + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-[beta-D-GlcNAc-(1->4)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
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?
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
UDP + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-[beta-D-GlcNAc-(1->4)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
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?
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
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?
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
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ir
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
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incorporates a N-acetylglucosamine residue in beta-1,4-linkage to beta-linked mannosyl, i.e. bisecting N-acetylglucosamine
?
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
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incorporates a N-acetylglucosamine residue in beta-1,4-linkage to beta-linked mannosyl, i.e. bisecting N-acetylglucosamine
?
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
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incorporates a N-acetylglucosamine residue in beta-1,4-linkage to beta-linked mannosyl, i.e. bisecting N-acetylglucosamine
?
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
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incorporates a N-acetylglucosamine residue in beta-1,4-linkage to beta-linked mannosyl, i.e. bisecting N-acetylglucosamine
ir
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
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incorporates a N-acetylglucosamine residue in beta-1,4-linkage to beta-linked mannosyl, i.e. bisecting N-acetylglucosamine
ir
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
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substrate specificity
incorporates a N-acetylglucosamine residue in beta-1,4-linkage to beta-linked mannosyl, i.e. bisecting N-acetylglucosamine
?
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
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substrate specificity
incorporates a N-acetylglucosamine residue in beta-1,4-linkage to beta-linked mannosyl, i.e. bisecting N-acetylglucosamine
ir
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
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pyridylaminated biantennary sugar chain
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ir
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
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structural requirements, stereochemistry
incorporates a N-acetylglucosamine residue in beta-1,4-linkage to beta-linked mannosyl, i.e. bisecting N-acetylglucosamine
ir
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
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beta1,2-GlcNAc linked to alpha1,3-Man is required for activity, beta1,2-GlcNAc linked to alpha1,6-Man is not required
incorporates a N-acetylglucosamine residue in beta-1,4-linkage to beta-linked mannosyl, i.e. bisecting N-acetylglucosamine
ir
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
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any agalacto form of the bi-, tri- and tetraantennary sugar chains is capable of serving as ana cceptor substrate
incorporates a N-acetylglucosamine residue in beta-1,4-linkage to beta-linked mannosyl, i.e. bisecting N-acetylglucosamine
ir
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
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beta1,4-galactosylation of N-acetylglucosaminyl-1,2-alpha-mannosyl-1,3-beta-mannosyl moiety prevents transferase III action
incorporates a N-acetylglucosamine residue in beta-1,4-linkage to beta-linked mannosyl, i.e. bisecting N-acetylglucosamine
?
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
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beta1,4-galactosylation of N-acetylglucosaminyl-1,2-alpha-mannosyl-1,3-beta-mannosyl moiety prevents transferase III action
incorporates a N-acetylglucosamine residue in beta-1,4-linkage to beta-linked mannosyl, i.e. bisecting N-acetylglucosamine
ir
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
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R represents the remainder of the N-oligosaccharide core, (+/-)-fucose, favourite substrate
incorporates a N-acetylglucosamine residue in beta-1,4-linkage to beta-linked mannosyl, i.e. bisecting N-acetylglucosamine
?
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
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R represents the remainder of the N-oligosaccharide core, (+/-)-fucose, favourite substrate
incorporates a N-acetylglucosamine residue in beta-1,4-linkage to beta-linked mannosyl, i.e. bisecting N-acetylglucosamine
?
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
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R represents the remainder of the N-oligosaccharide core, (+/-)-fucose, favourite substrate
incorporates a N-acetylglucosamine residue in beta-1,4-linkage to beta-linked mannosyl, i.e. bisecting N-acetylglucosamine
ir
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
key regulatory role in N-glycan biosynthesis, responsible for cancer-associated alterations
-
-
?
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
important role in carcinogenesis and cancer metastasis
-
-
?
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
key enzyme in the biosynthesis of N-glycans since it inhibits the other involved glycosyltransferases by adding the GlcNAc-residue in an beta-1,4- linkage
-
-
?
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
R represents the remainder of the N-oligosaccharide core (+/-fucose), essential for biosynthesis of complex N-linked oligosaccharides
-
-
?
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
numerous target proteins, multifacial glycosyltransferase
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-mannosyl-R
UDP + 4-(N-acetyl-beta-D-glucosaminyl)-beta-D-mannosyl-R
-
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-mannosyl-R
UDP + 4-(N-acetyl-beta-D-glucosaminyl)-beta-D-mannosyl-R
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-mannosyl-R
UDP + 4-(N-acetyl-beta-D-glucosaminyl)-beta-D-mannosyl-R
-
GnT-III catalyzes the formation of a bisecting GlcNAc structure in N-glycans, resulting in the suppression of metastasis. The priority of GnT-III for the modification of the integrin alpha3 subunit may be an explanation for why GnT-III inhibits GnT-V-induced cell migration. TGnT-III and GnT-V can competitively modify the same target glycoprotein and furthermore positively or negatively regulate its biological functions
-
-
?
additional information
?
-
-
the biantennary structure of a core mannose is twisted in presence of bisecting GlcNAc, probably responsible for the substrate inaccessibility to N-acetylglucosamine transferase V to form the beta-1,6 structure
-
-
?
additional information
?
-
-
biosynthetic pathway of the core structures of Asn-linked sugar chains, overview
-
-
?
additional information
?
-
-
key enzyme that inhibits the extension of N-glycans by introducing a bisecting N-acetylglucosamine residue, modification of N-glycans by the enzyme affects a number of intracellular signalling pathways
-
-
?
additional information
?
-
-
key enzyme that inhibits the extension of N-glycans by introducing a bisecting N-acetylglucosamine residue, modification of N-glycans by the enzyme affects a number of intracellular signalling pathways
-
-
?
additional information
?
-
-
N-acetylglucosaminyltransferase III expression is regulated by cell-cell adhesion via the E-cadherin-catenin-actin complex
-
-
?
additional information
?
-
-
GnT-III selectively modifies N-glycosylation site-4 on the integrin alpha5 subunit (S-3,4,5), which down-regulates its biological functions
-
-
?
additional information
?
-
-
N-glycosylation of laminin-332, GnT-III down-regulates activities of laminin-332
-
-
?
additional information
?
-
-
the enzyme catalyzes the transfer of N-acetylglucosamine in a beta1,4 linkage to mannose on N-glycans forming a bisecting N-acetylglucosamine structure
-
-
?
additional information
?
-
-
the enzyme introduces a N-acetylglucosamine in a beta1,4-linkage to the mannose residue located at the base of the trimannosyl core (bisecting N-acetylglucosamine) in N-glycans
-
-
?
additional information
?
-
N-acetylglucosaminyltransferase III is a glycosyltransferase which produces bisected N-glycans by transferring GlcNAc to the 4-position of core mannose
-
-
?
additional information
?
-
the MCAM glycoprotein, which is a biomarker of cutaneous melanoma, as a potential target for overexpressed glycosyltransferases
-
-
?
additional information
?
-
-
the MCAM glycoprotein, which is a biomarker of cutaneous melanoma, as a potential target for overexpressed glycosyltransferases
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[Notch receptor]
UDP + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-[beta-D-GlcNAc-(1->4)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[Notch receptor]
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
UDP + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-[beta-D-GlcNAc-(1->4)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP-N-acetyl-D-glucosamine + beta-D-mannosyl-R
UDP + 4-(N-acetyl-beta-D-glucosaminyl)-beta-D-mannosyl-R
UDP-N-acetyl-D-glucosamine + E-cadherin
UDP + E-cadherin with bisecting N-acetyl-D-glucosamine
-
recombinant enzyme expressed in murine lung melanoma cells
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
UDP + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-[beta-D-GlcNAc-(1->4)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
UDP + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-[beta-D-GlcNAc-(1->4)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
key regulatory role in N-glycan biosynthesis, responsible for cancer-associated alterations
-
-
?
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
important role in carcinogenesis and cancer metastasis
-
-
?
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
key enzyme in the biosynthesis of N-glycans since it inhibits the other involved glycosyltransferases by adding the GlcNAc-residue in an beta-1,4- linkage
-
-
?
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
R represents the remainder of the N-oligosaccharide core (+/-fucose), essential for biosynthesis of complex N-linked oligosaccharides
-
-
?
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
numerous target proteins, multifacial glycosyltransferase
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-mannosyl-R
UDP + 4-(N-acetyl-beta-D-glucosaminyl)-beta-D-mannosyl-R
-
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-mannosyl-R
UDP + 4-(N-acetyl-beta-D-glucosaminyl)-beta-D-mannosyl-R
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-mannosyl-R
UDP + 4-(N-acetyl-beta-D-glucosaminyl)-beta-D-mannosyl-R
-
GnT-III catalyzes the formation of a bisecting GlcNAc structure in N-glycans, resulting in the suppression of metastasis. The priority of GnT-III for the modification of the integrin alpha3 subunit may be an explanation for why GnT-III inhibits GnT-V-induced cell migration. TGnT-III and GnT-V can competitively modify the same target glycoprotein and furthermore positively or negatively regulate its biological functions
-
-
?
additional information
?
-
-
the biantennary structure of a core mannose is twisted in presence of bisecting GlcNAc, probably responsible for the substrate inaccessibility to N-acetylglucosamine transferase V to form the beta-1,6 structure
-
-
?
additional information
?
-
-
biosynthetic pathway of the core structures of Asn-linked sugar chains, overview
-
-
?
additional information
?
-
-
key enzyme that inhibits the extension of N-glycans by introducing a bisecting N-acetylglucosamine residue, modification of N-glycans by the enzyme affects a number of intracellular signalling pathways
-
-
?
additional information
?
-
-
key enzyme that inhibits the extension of N-glycans by introducing a bisecting N-acetylglucosamine residue, modification of N-glycans by the enzyme affects a number of intracellular signalling pathways
-
-
?
additional information
?
-
-
N-acetylglucosaminyltransferase III expression is regulated by cell-cell adhesion via the E-cadherin-catenin-actin complex
-
-
?
additional information
?
-
N-acetylglucosaminyltransferase III is a glycosyltransferase which produces bisected N-glycans by transferring GlcNAc to the 4-position of core mannose
-
-
?
additional information
?
-
the MCAM glycoprotein, which is a biomarker of cutaneous melanoma, as a potential target for overexpressed glycosyltransferases
-
-
?
additional information
?
-
-
the MCAM glycoprotein, which is a biomarker of cutaneous melanoma, as a potential target for overexpressed glycosyltransferases
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
hepatitis B virus
-
selective suppression of enzyme activity on transcription level in transfected cells, e.g. cell line Hb611
-
inactive rat mutant D323A enzyme
-
acts as an inhibitor of endogenous enzyme activity when expressed in human Huh6 cells
-
methyl 3,6-di-O-(2-deoxy-2-acetamide-beta-D-glucopyranosyl-2-O-alpha-D-mannopyranosyl)-4-O-(2-deoxy-2-acetamide-beta-D-glucopyranosyl)-alpha-D-mannopyranoside
-
methyl 3,6-di-O-(2-deoxy-2-acetamide-beta-D-glucopyranosyl-2-O-alpha-D-mannopyranosyl)-alpha-D-mannopyranoside
-
methyl 3,6-di-O-(alpha-D-mannopyranosyl)-4-O-(2-deoxy-2-acetamide-beta-D-glucopyranosyl)-alpha-D-mannopyranoside
-
additional information
-
transgenic expression of the enzyme in hepatitis B virus infected cells suppress the virus expression, cell line HB611
-
additional information
-
transgenic expression of the enzyme in hepatitis B virus infected cells suppress the virus expression, cell line HB611
-
additional information
systematic synthesis of four N-glycan units, the branching parts of the bisected and non-bisected N-glycans, from a common core trimannose, giving bisected tetra- and hexasaccharides as well as non-bisected tri- and pentasaccharides, and evaluation as enzyme inhibitors, overview. The competitive GnT-III inhibition assay using the synthetic substrates reveals a vital role for the Manbeta(1-4)GlcNAc moiety, GlcNAc at the alpha1,3-branch is also involved in the interaction. Competitive inhibition, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
interferon-alpha-2a leads to an increase in enzyme activity in hepatitis B virus infected cells due to reduction of virus expression
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
solid-phase enzyme-linked immunosorbent sandwich assay for enzyme activity
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.5 - 14
methyl 3,6-di-O-(2-deoxy-2-acetamide-beta-D-glucopyranosyl-2-O-alpha-D-mannopyranosyl)-4-O-(2-deoxy-2-acetamide-beta-D-glucopyranosyl)-alpha-D-mannopyranoside
1.2 - 1.4
methyl 3,6-di-O-(alpha-D-mannopyranosyl)-4-O-(2-deoxy-2-acetamide-beta-D-glucopyranosyl)-alpha-D-mannopyranoside
1.5
methyl 3,6-di-O-(2-deoxy-2-acetamide-beta-D-glucopyranosyl-2-O-alpha-D-mannopyranosyl)-4-O-(2-deoxy-2-acetamide-beta-D-glucopyranosyl)-alpha-D-mannopyranoside
pH and temperature not specified in the publication, versus UDP-N-acetyl-D-glucosamine
14
methyl 3,6-di-O-(2-deoxy-2-acetamide-beta-D-glucopyranosyl-2-O-alpha-D-mannopyranosyl)-4-O-(2-deoxy-2-acetamide-beta-D-glucopyranosyl)-alpha-D-mannopyranoside
pH and temperature not specified in the publication, versus GnGnbi-PA
1.2
methyl 3,6-di-O-(alpha-D-mannopyranosyl)-4-O-(2-deoxy-2-acetamide-beta-D-glucopyranosyl)-alpha-D-mannopyranoside
pH and temperature not specified in the publication, versus GnGnbi-PA
1.4
methyl 3,6-di-O-(alpha-D-mannopyranosyl)-4-O-(2-deoxy-2-acetamide-beta-D-glucopyranosyl)-alpha-D-mannopyranoside
pH and temperature not specified in the publication, versus UDP-N-acetyl-D-glucosamine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
activity and expression level in various leukemic cells
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
488370, 638214, 638217, 638220, 638222, 638223, 638224, 638226, 638227, 638229, 658123, 658863, 673888, 674676, 676107, 689981, 702516, 703093, 703956, 704446, 704468, 705381, 721738, 722734, 722755, 722856, 723551
-
-
patients with extrahepatic bile duct carcinoma or benign biliary duct diseases
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
chronic myelogenous leukemia granulocyte cell lines, e.g. clone KU812 and subclone KU812F
-
DLD-1/DELTAalpha cells lacking alpha-catenin expression
-
hepatoblastoma cell line, derived from Huh6 by transfection of 3 copies of hepatitis B virus genome, decreased transcription level
decreased expression of GnT-III in H/R-exposed HTR8/SVneo cells, and the invasive and migratory abilities of HTR8/SVneo cells were attenuated, too
GnT-III expression significantly increases ovarian cancer growth and metastasis and increases the expansion of the ovarian cancer stem cell (CSC) population
additional information
-
from patients with chronic lymphocytic leukemia CLL or acute lymphoblastic leukemia ALL
enzyme GnT-III is strongly expressed in cytotrophoblast (CTBs), syncytiotrophoblast (STBs), and the trophoblast columns (TCs) of human placental villi, and decidual cells in maternal decidua. The expression of GnT-III is decreased in preeclampsia placentas compared with the normal control placentas
additional information
quantitative real-time PCR enzyme expression analysis
additional information
human first trimester villous tissues from normal pregnancies and third trimester placentas from pregnancies with or without preeclampsia (PE) are used for the detection of GnTIII expression
additional information
-
human first trimester villous tissues from normal pregnancies and third trimester placentas from pregnancies with or without preeclampsia (PE) are used for the detection of GnTIII expression
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
functional localization of enzyme is regulated by caveolin-1
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
-
knockdown of GnT-III by siRNA causes no alteration in expression levels of E-cadherin mRNA and protein, but induces alterations on E-cadherin cellular localization in MCF-7/AZ cells. GnT-III knockdown cells reveal a membrane de-localization of E-cadherin leading to its cytoplasmic accumulation and cause modifications of E-cadherin N-glycans catalyzed by GnT-III and GnT-V
malfunction
detailed glycomic analysis of the effect of GnT-III overexpression in WM266-4-GnT-III metastatic melanoma cells, overview. Overexpression of GnT-III in melanoma leads to modification of a broad range of N-glycan types by the introduction of the bisecting GlcNAc residue with highly branched complex structures among them. The presence of these unusual complex N-glycans results in stronger interactions of cellular glycoproteins with the PHA-L. Elevated activity of GnT-III in cancer cells does not necessarily lead to a total abrogation of the formation of highly branched glycans. The modification of pre-existing N-glycans by the introduction of bisecting GlcNAc can modulate their capacity to interact with carbohydrate-binding proteins such as plant lectins
malfunction
downregulated N-acetylglucosaminyltransferase III is involved in attenuating trophoblast migration and invasion under hypoxia-reoxygenation condition. Excessive oxidative stress can decrease GnT-III expression in trophoblast and the decreased expression of GnT-III may be involved in the development of preeclampsia. Clinical characteristics of preeclampsia group comparedwith normal pregnancy group, overview
malfunction
suppression of GnT-III in epithelial ovarian carcinoma (EOC) cell lines and primary tumor-derived cells results in an inhibition of Notch signaling that is more potent than pharmacologic blockage of Notch activation via gamma-secretase inhibition. The inhibition results from the redirection of the Notch receptor to the lysosome, a distinct mechanism
metabolism
-
N-acetylglucosaminyltransferase-III-mediated glycosylation, specifically on E-cadherin, is a major component of the Epithelial-Mesenchymal-Transition /Mesenchymal-Epithelial-Transition mechanism signature
metabolism
existence of a bi-directional cross-talk between E-cadherin and two major N-glycan processing enzymes, N-acetylglucosaminyltransferase-III or -V (GnT-III or GnT-V). Molecular mechanisms underlying E-cadherin regulation in gastric cancer, overview
metabolism
interplay between GnT-III and sialyltransferases in the expression of their enzymatic products and also their functions in tumor metastasis. Interplay between GnT-III and ST6GAL1 in regulating cell migration
metabolism
GnT-III is considered to be a key glycosyltransferase in the N-glycan biosynthetic pathway because the introduction of the bisecting GlcNAc residue suppresses further processing and elongation of the N-glycans catalyzed by GnT-V. So, in the tumor context, GnT-III and GnT-V have generally a dual role where GnT-III acts as metastases suppressors whereas GnT-V is associated with increased malignancy and metastasis
physiological function
-
all subunits of laminin-332 are modified by GnT-III, introduction of GnT-III inhibits GnT-V products
physiological function
-
GnT-III is an antagonistic of GnT-V, thereby contributing to the suppression of cancer metastasis. Modification of the alpha3 subunit by GnT-III supersedes modification by GnT-V. Overexpression of GnT-III in highly metastatic melanoma cells reduces beta1,6 GlcNAc branching in cell-surface N-glycans and increases bisected N-glycans, which results in an enhancement of cell-cell adhesion due to prolonged turnover of E-cadherin on the cell surface. Overexpression of GnT-III significantly reduces the ability of epithelial growth factor receptor to bind to its receptor, reduces epithelial growth factor receptor autophosphorylation, and subsequently blocks epithelial growth factor receptor-mediated Erk phosphorylation in U373 MG glioma cells and in PC12 cells. GnT-III also inhibits the formation of the alpha-Gal epitope, which is a major xenotransplantation antigen that is problematic in swine-to-human organ transplantation. GnT-III affects antibody-dependent cellular cytotoxicity activity. Transgenic mice, in which GnT-III is expressed specifically in the liver by use of a serum amyloid P component gene promoter, exhibits fatty liver. Ectopic expression of GnT-III disrupts the function of apolipoprotein B, resulting in abnormal lipid accumulation
physiological function
-
integrins are modified by GnT-III, which inhibits cell migration and cancer metastasis. Overexpression of GnT-III results in an inhibition of alpha5beta1 integrin-mediated cell spreading and migration, and the phosphorylation of the focal adhesion kinase. Overexpression of GnT-III in highly metastatic melanoma cells reduces beta1, six branching in cell-surface N-glycans and increases bisected N-glycans. GnT-III is an antagonistic of GnT-V, contributing to the suppression of cancer metastasis, overexpression of GnT-III inhibits GnT-V-induced cell migration. Overexpression of GnT-III slows E-cadherin turnover, resulting in increased E-cadherin expression on the surface of B16 melanoma cells
physiological function
-
introduction of GnT-III suppresses additional processing and branching formation of N-glycans catalyzed by other endogenous glycosyltransferases, such as GnT-V and GnT-IV. Cell adhesion on fibronectin is down-regulated in GnT-III transfectants compared with mock and GnT-V transfectants. Overexpression of GnT-III significantly inhibits cell migration on fibronectin. GnT-III significantly down-regulates cell spreading on fibronectin in wild-type transfectants, whereas the deletion of site-4 abolishes the suppression of cell spread induced by GnT-III in D-4 transfectants
physiological function
-
overexpression of GnT-III downregulates alpha5beta1 integrin-mediated cell spreading and migration, and the phosphorylation of the focal adhesion kinase. Overexpression of GnT-III slows E-cadherin turnover, resulting in increased E-cadherin expression on the surface of B16 melanoma cells. GnT-III inhibits GnT-V-induced cell migration. Overexpression of GnT-III inhibits cancer metastasis by at least two mechanisms: an enhancement in cell-cell adhesion and a downregulation of cell-ECM adhesion
physiological function
the enzyme induces a stabilizing effect on E-cadherin at the cell membrane by inducing a delay in the turnover rate of the protein, contributing for the formation of stable and functional adherens-junctions, and further preventing clathrin-dependent E-cadherin endocytosis. The enzyme plays a role on E-cadherin-mediated tumor suppression
physiological function
-
the enzyme plays an important role in the suppression of cancer metastasis. The enzyme influences epithelial-to-mesenchymal transition-like changes through not only prolongation of E-cadherin turnover but also suppression of beta-catenin-p-Smad complex formation. The enzyme plays important roles in transforming growth factor-beta-induced epithelial-to-mesenchymal transition-like changes. The enzyme does not significantly affect the expression of E-cadherin mRNA
physiological function
GnT-III induced a stabilizing effect on E-cadherin at the cell membrane by inducing a delay in the turnover rate of the protein, contributing for the formation of stable and functional adherens-junctions, and further preventing clathrin-dependent E-cadherin endocytosis. Role of GnT-III on E-cadherin-mediated tumor suppression. GnT-III catalyzes the formation of a bisecting GlcNAc structure in N-glycans and is a metastases suppressor. E-cadherin is specifically modified with bisecting GlcNAc or beta1,6 GlcNAc branched structures
physiological function
N-acetylglucosaminyltransferase III catalyzes the addition of the bisecting GlcNAc branch on N-glycans, and is a metastasis suppressor with an important role of GnT-III in N-glycan biosynthesis and tumor cell behaviours. Increased expression of GnT-III in human hepatomas, glioma, and ovarian cancers. Overexpression of GnT-III significantly inhibits alpha2,3-sialylation but not alpha2,6-sialylation via post-transcriptional mechanisms. GnT-III plays an anti-migratory role in tumor cells without or with a low level of alpha2,6-linked sialic acids but not in those alpha2,6-hypersialylated
physiological function
N-acetylglucosaminyltransferase III is a glycosyltransferase which produces bisected N-glycans by transferring GlcNAc to the 4-position of core mannose. Bisected N-glycans are involved in physiological and pathological processes through the functional regulation of their carrier proteins
physiological function
N-acetylglucosaminyltransferase III is involved in formation of beta1,4 linkage between GlcNAc and beta-mannose residue within the core of oligosaccharide. The resulting bisected N-glycan acquires a characteristic conformation that renders inaccessibility to many other enzymes participating in biosynthetic pathways of hybrid and complex multiantennary N-glycans as well as to lectins
physiological function
glycosyltransferase GnT-III activates Notch signaling and drives stem cell expansion to promote the growth and invasion of ovarian cancer. Glycosylation mediated by GnT-III increases Notch receptor levels and activity. GnT-III expression controls the expansion of side-population cells, also known as cancer stem cells, GnT-III expression regulates the levels and activation of the heavily glycosylated Notch receptor involved in normal and malignant development. The gene Mgat3 encoding the glycosyltransferase GnT-III is elevated in epithelial ovarian carcinomas (EOCs) and leads to the production of abnormal truncated N-linked glycan structures instead of the typical bisected forms, role for bisecting glycosylation in the control of Notch transport, overview. GnT-III expression maintains the side-population and promotes spheroid formation in ovarian cancer cells
physiological function
N-acetylglucosaminyltransferase III (GnT-III) is known to catalyze N-glycan bisection and thereby modulate the formation of highly branched complex structures within the Golgi apparatus. While active, it inhibits the action of other GlcNAc transferases such as GnT-IVand GnT-V. Moreover, GnT-III is considered an inhibitor of the metastatic potential of cancer cells both in vitro and in vivo
physiological function
N-acetylglucosaminyltransferases III (GnT-III) is one of the most important N-glycosyltransferases encoded by the MGAT3 gene. GnT-III catalyzes the addition of GlcNAc via b1-4 linkage to the b-mannose of the mannosyl core of N-glycans. N-acetylglucosaminyltransferase III (GnT-III) is correlated with tumor invasion and metastasis. GnT-III is an important regulator at the maternal-fetal interface during early pregnancy
additional information
GnT-III overexpression does not affect cell morphology
additional information
usage of MALDI-TOF and ESIion-trap-MS/MS together with HILIC-HPLC of 2-AA labeled N-glycans to study the N-glycome of membrane-attached and secreted proteins. Characterization of N-glycan epitopes on membrane and secreted proteins using plant lectins, several plant lectins are used in lectin blot assay, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MGAT3_HUMAN
533
1
61313
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
GnT-III overexpression does not affect cell morphology. Gastric cells overexpressing GnT-III appears to exhibit a more focused immunolocalization at cell-cell borders than control cells. In GnT-III transfected cells there is a well-localized continuous staining of E-cadherin at the cell membrane that correlates with F-actin staining, suggesting co-localization, GnT-III overexpression prevents clathrin-dependent E-cadherin endocytosis, phenotype, overview
additional information
GnT-III overexpression does not affect cell morphology. Gastric cells overexpressing GnT-III appears to exhibit a more focused immunolocalization at cell-cell borders than control cells. In GnT-III transfected cells there is a well-localized continuous staining of E-cadherin at the cell membrane that correlates with F-actin staining, suggesting co-localization, GnT-III overexpression prevents clathrin-dependent E-cadherin endocytosis, phenotype, overview
additional information
overexpression of GnT-III significantly inhibits alpha2,3-sialylation but not alpha2,6-sialylation. The migratory ability of cells, HeLa-S3, CHO-K1 and Pro-5, without or with a low level of alpha2,6-sialylation is consistently suppressed after overexpression of GnT-III, while in alpha2,6-hypersialylated MDA-MB-231 and MKN-45 cells little effects are observed. Phenotypes, detailed overview
additional information
-
overexpression of GnT-III significantly inhibits alpha2,3-sialylation but not alpha2,6-sialylation. The migratory ability of cells, HeLa-S3, CHO-K1 and Pro-5, without or with a low level of alpha2,6-sialylation is consistently suppressed after overexpression of GnT-III, while in alpha2,6-hypersialylated MDA-MB-231 and MKN-45 cells little effects are observed. Phenotypes, detailed overview
additional information
gene mgat3 suppression via shRNA. A significant increase in ovarian masses and metastasis in control shRNA cells compared with GnT-III shRNA cells is observed. Control cell tumors are more invasive following i.p. injections in NOD/SCID mice or human carcinoma samples, whereas GnT-III shRNA tumors are less vascularized and never invade surrounding tissues
additional information
WM-266-4-GnT-III human metastatic melanoma cells stably overexpress the MGAT3 gene together with mock control cells WM-266-4-pIRESneo
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type, diethyl(2-hydroxypropyl)aminoethyl-Sepharose and immunoaffinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
amplified for cloning into pENTR-D-Topo vector, cloned gene inserted into the virus expression vector, pBABE-puro. GnT-III and GnT-V constructs transfected into Phoenix-Ampho cells
-
enzyme overexpression in HeLa-S3, CHO-K1, Pro-5, and MDA-MB-231 cells using vector CSIV-TRE-RfA-CMV-KT, cloning in HEK-293T cells
expression in erythroleukemia cell line K562, leading to increased resistance to lysis by natural killer cells and enhanced spleen colonization ability
-
expression of mutant aglycosyl-enzyme, lacking the first 23 amino acid residues, in Escherichia coli
-
gene MGAT3, quantitative real-time PCR enzyme expression analysis
gene MGAT3, real-time RT-PCR enzyme expression analysis, establishing of human melanoma cell line WM-266-4 with induced stable overexpression of GnT-III, the cells show increased amounts of bisected and beta1-6 branched N-glycans on melanoma cell adhesion molecule MCAM/MUC18, but do not display significant differences in viability and capabilities to migrate through an endothelial layer, coexpression with MGAT5 gene, EC 2.4.1.155
gene MGAT3, stable overexpression of the enzyme in WM-266-4-GnT-III human metastatic melanoma cells
heterozygous alpha 1,3-galactosyltransferase gene knockout pigs produced with transgenic pig fetal cells expressing both human decay-accelerating factor and N-acetylglucosaminyltransferase III
-
highly metastatic melanoma B16 cells transfected with GnT-III and then injected into syngeneic mice via the tail vein
-
introduction of human N-acetylglucosaminyltransferase (GnT)-III gene into Nicotiana tabacum leads to highly efficient synthesis of bisected N-glycans
-
introduction of human N-acetylglucosaminyltransferase gene into tobacco plants leads to highly efficient synthesis of bisected N-glycans. The majority of N-glycans of an antibody produced in a plant expressing GnT-III is also bisected. This might improve the efficacy of therapeutic antibodies produced in this type of transgenic plant
-
overexpression in HeLa cells, leading to suppression of H2O2-induced activation of PKCdelta-JNK1 signalling pathway resulting in inhibition of apoptosis
-
overexpression in murine lung melanoma cell line B16-hm, leading to suppression of the formation of beta-1,6-tri- and tetraantennary N-linked oligosaccharides by inhibiting the responsible enzymes, e.g. N-acetylglucosamine transferase V, EC 2.4.1.155, decrease of the metastatic potential of B16-hm melanoma in vivo, changed phenotype
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
downregulation of GnT-III expression in MDA-MB-231 cells, an E-cadherin-deficient cell line, the MDCK cell, in which GnTIII expression is undetectable, and fibroblasts, which lack E-cadherin
-
during epithelial-mesenchymal-transition, enzyme expression is dramatically decreased and later recoveres when cells return to an epithelial-like phenotype
-
E-cadherin-mediated cell-cell interaction upregulates GnT-III expression, suggesting that regulation of GnT-III and E-cadherin expression may exist as a positive feedback loop
-
E-cadherin-mediated cell-cell interaction upregulates GnT-III expression. Significant upregulation of GnT-III expression in epithelial cells that express basal levels of E-cadherin and GnT-III
-
in MDA-MB231 cells, an E-cadherin-deficient cell line, GnT-III expression is undetectable
-
knockdown of GnT-III, de-localization of E-cadherin and cytoplasmic accumulation, modification of N-glycosylation in E-cadherin
-
shRNA knockdown of beta-catenin results in a dramatic increase in enzyme expression
-
significant up-regulation of GnT-III expression in epithelial cells that express basal levels of E-cadherin and GnT-III. Expression levels of GnT-III and its products, the bisected N-glycans, are up-regulated by cell-cell interaction via the E-cadherin-catenin-actin complex. GnT-III expression is significantly up-regulated in cells cultured under dense conditions. Modest increase in GnT-III expression under dense culture conditions in alpha-catenin-deficient DLD-1 cells as well as in E-cadherin-deficient MDA-MB-231 cells. Mutual regulation of GnT-III expression and E-cadherin-mediated cell-cell interaction exists as a positive-feedback loop
-
stimulation of the Wnt signaling pathway by the addition of exogenous Wnt3a or SB415286 consistently and significantly inhibits enzyme expression
-
the expression levels of GnT-III are suppressed about 25fold in transforming growth factor-beta-treated cells (5 ng/ml)
-
wild-type E-cadherin regulates MGAT3 gene transcription resulting in increased GnT-III expression. GnT-III mRNA transcription levels in MDA-MB-435 cells transfected with E-cadherin wild-type are ca. 2fold higher than those in MDA-MB-435 mock cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
GnT-III expression levels are elevated in high-grade serous ovarian carcinoma tissues and correlate with reduced survival
medicine
synthesis
medicine
-
enzyme activity in extrahepatic bile duct carcinoma is increased 3fold compared to mean enzyme activity values, resulting in increased bisecting-GlcNAc on the glycans of glycoproteins in cancer tissues and a 201 kDa bile glycoprotein
medicine
-
enzyme activity is elevated in serum of 60 out of 86 patients with liver cirrhosis, and of 86 out of 91 patients with chronic hepatitis
medicine
-
enzyme activity is elevated in three choriocarcinoma cell lines compared to normal placenta. Activity in JEG-3 cells is 27 times higher than normal
medicine
-
the majority of N-glycans of a recombinant antibody produced in Nicotiana tabacum expressing GnT-III is bisected and devoid of paucimannosidic structures. This might improve the efficacy of therapeutic antibodies produced in the transgenic plants
medicine
therapeutic potential of inhibiting GnT-III as a treatment for controlling epithelial ovarian carcinoma (EOC) growth and recurrence
synthesis
-
overexpression of enzyme in human hepatoma cells fails to reduce branch formation of N-glycans, coexpression of caveolin-1 leads to a dramatic decrease in the extent of branching with no enhancement of enzyme activity
synthesis
-
transfection of mouse aorta endothelial cells with enzyme results in reduction of their susceptibility to complement-mediated cell lysis by normal human serum and suppresses the antigenicity of cells to human natural antibodies. Reactivity of glycoproteins of transfectants to normal human serum and GSIB4 lectin is reduced
synthesis
-
introduction of human N-acetylglucosaminyltransferase gene into tobacco plants leads to highly efficient synthesis of bisected N-glycans. The majority of N-glycans of an antibody produced in a plant expressing GnT-III is also bisected. This might improve the efficacy of therapeutic antibodies produced in this type of transgenic plant
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TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schachter, H.; Brockhausen, I.; Hull, E.
High-performance liquid chromatography assays for N-acetylglucosaminyltransferases involved in N- and O-glycan synthesis
Methods Enzymol.
179
351-397
1989
Cricetulus griseus, Gallus gallus, Homo sapiens, Rattus norvegicus
Nishikawa, A.; Ihara, Y.; Hatakeyama, M.; Kangawa, K.; Taniguchi, N.
Purification, cDNA cloning, and expression of UDP-N-acetylglucosamine: beta-D-mannoside beta-1,4N-acetylglucosaminyltransferase III from rat kidney
J. Biol. Chem.
267
18199-18204
1992
Cricetulus griseus, Homo sapiens, Rattus norvegicus (Q02527)
Miyoshi, E.; Nishikawa, A.; Ihara, Y.; Hayashi, N.; Fusamoto, H.; Kamada, T.; Taniguchi, N.
Selective suppression of N-acetylglucosaminyltransferase III activity in a human hepatoblastoma cell line transfected with hepatitis B virus
Cancer Res.
54
1854-1858
1994
Homo sapiens
Yoshimura, M.; Nishikawa, A.; Ihara, Y.; Nishiura, T.; Nakao, H.; Kanayama, Y.; Matuzawa, Y.; Taniguchi, N.
High expression of UDP-N-acetylglucosamine:beta-D mannoside beta-1,4-N-acetylglucosaminyltransferase III (GnT-III) in chronic myelogenous leukemia in blast crisis
Int. J. Cancer
60
443-449
1995
Homo sapiens
Taniguchi, N.; Yoshimura, M.; Miyoshi, E.; Ihara, Y.; Nishikawa, A.; Kang, R.; Ikeda, Y.
Gene expression and regulation of N-acetylglucosaminyltransferases III and V in cancer tissues
Adv. Enzyme Regul.
38
223-232
1998
Homo sapiens, no activity in Mus musculus
Shibukawa, Y.; Takahashi, M.; Laffont, I.; Honke, K.; Taniguchi, N.
Down-regulation of hydrogen peroxide-induced PKCdelta activation in N-acetylglucosaminyltransferase III-transfected HeLaS3 cells
J. Biol. Chem.
278
3197-3203
2003
Homo sapiens
Taniguchi, N.; Miyoshi, E.; Ko, J.H.; Ikeda, Y.; Ihara, Y.
Implication of N-acetylglucosaminyltransferases III and V in cancer: gene regulation and signaling mechanism
Biochim. Biophys. Acta
1455
287-300
1999
Gallus gallus, Homo sapiens, Mus musculus, Rattus norvegicus, Rattus norvegicus (Q02527)
Song, E.Y.; Kim, K.A.; Kim, Y.D.; Kwon, D.H.; Lee, H.S.; Kim, C.H.; Chung, T.W.; Byun, S.M.
A simplified procedure for the purification of human N-acetylglucosaminyltransferase-III from human hepatocellular carcinoma tissues
Biotechnol. Lett.
22
201-204
2000
Homo sapiens
-
Guo, H.B.; Jiang, A.L.; Ju, T.Z.; Chen, H.L.
Opposing changes in N-acetylglucosaminyltransferase-V and -III during the cell cycle and all-trans retinoic acid treatment of hepatocarcinoma cell line
Biochim. Biophys. Acta
1495
297-307
2000
Homo sapiens
Song, E.Y.; Kang, S.K.; Lee, Y.C.; Park, Y.G.; Chung, T.H.; Kwon, D.H.; Byun, S.M.; Kim, C.H.
Expression of bisecting N-acetylglucosaminyltransferase-III in human hepatocarcinoma tissues, fetal liver tissues, and hepatoma cell lines of Hep3B and HepG2
Cancer Invest.
19
799-807
2001
Homo sapiens
Ikeda, Y.; Taniguchi, N.
Enzymatic properties and biological functions of beta1,4-N-acetylglucosaminyltransferase III
Trends Glycosci. Glycotechnol.
13
167-176
2001
Gallus gallus, Homo sapiens, Rattus norvegicus, Rattus norvegicus (Q02527)
-
Ihara, H.; Ikeda, Y.; Koyota, S.; Endo, T.; Honke, K.; Taniguchi, N.
A catalytically inactive beta1,4-N-acetylglucosaminyltransferase III (GnT-III) behaves as a dominant negative GnT-III inhibitor
Eur. J. Biochem.
269
193-201
2002
Homo sapiens, Rattus norvegicus
Takamatsu, S.; Inoue, N.; Katsumata, T.; Nakamura, K.; Fujibayashi, Y.; Takeuchi, M.
The relationship between the branch-forming glycosyltransferases and cell surface sugar chain structures
Biochemistry
44
6343-6349
2005
Homo sapiens
Song, E.Y.; Kim, K.S.; Kim, K.A.; Kim, Y.D.; Kwon, D.H.; Byun, S.M.; Kim, H.J.; Chung, T.W.; Choe, Y.K.; Chung, T.W.; Kim, C.H.
Determination of UDP-N-acetylglucosamine:beta-D-mannoside-1,4-N-acetylglucosaminyltransferase-III in patients sera with chronic hepatitis and liver cirrhosis using a monoclonal antibody
Glycoconj. J.
19
415-421
2003
Homo sapiens
Jin, X.L.; Liu, H.B.; Zhang, Y.; Wang, B.S.; Chen, H.L.
Alteration in N -acetylglucosaminyltransferase activities and glycan structure in tissue and bile glycoproteins from extrahepatic bile duct carcinoma
Glycoconj. J.
20
399-406
2004
Homo sapiens
Takamatsu, S.; Katsumata, T.; Inoue, N.; Watanabe, T.; Fujibayashi, Y.; Takeuchi, M.
Abnormal biantennary sugar chains are expressed in human chorionic gonadotropin produced in the choriocarcinoma cell line, JEG-3
Glycoconj. J.
20
473-481
2004
Homo sapiens
Sasai, K.; Ikeda, Y.; Ihara, H.; Honke, K.; Taniguchi, N.
Caveolin-1 regulates the functional localization of N-acetylglucosaminyltransferase III within the Golgi apparatus
J. Biol. Chem.
278
25295-25301
2003
Homo sapiens
Chung, T.W.; Kim, K.S.; Kim, C.H.
Reduction of the Gal-alpha1,3-Gal epitope of mouse endothelial cells by transfection with the N-acetylglucosaminyltransferase III gene
Mol. Cells
16
368-376
2003
Homo sapiens
Rouwendal, G.J.; Wuhrer, M.; Florack, D.E.; Koeleman, C.A.; Deelder, A.M.; Bakker, H.; Stoopen, G.M.; van Die, I.; Helsper, J.P.; Hokke, C.H.; Bosch, D.
Efficient introduction of a bisecting GlcNAc residue in tobacco N-glycans by expression of the gene encoding human N-acetylglucosaminyltransferase III
Glycobiology
17
334-344
2007
Homo sapiens
Zhao, Y.; Nakagawa, T.; Itoh, S.; Inamori, K.; Isaji, T.; Kariya, Y.; Kondo, A.; Miyoshi, E.; Miyazaki, K.; Kawasaki, N.; Taniguchi, N.; Gu, J.
N-acetylglucosaminyltransferase III antagonizes the effect of N-acetylglucosaminyltransferase V on alpha3beta1 integrin-mediated cell migration
J. Biol. Chem.
281
32122-32130
2006
Homo sapiens
Takahagi, Y.; Fujimura, T.; Miyagawa, S.; Nagashima, H.; Shigehisa, T.; Shirakura, R.; Murakami, H.
Production of alpha 1,3-galactosyltransferase gene knockout pigs expressing both human decay-accelerating factor and N-acetylglucosaminyltransferase III
Mol. Reprod. Dev.
71
331-338
2005
Homo sapiens
Akama, R.; Sato, Y.; Kariya, Y.; Isaji, T.; Fukuda, T.; Lu, L.; Taniguchi, N.; Ozawa, M.; Gu, J.
N-acetylglucosaminyltransferase III expression is regulated by cell-cell adhesion via the E-cadherin-catenin-actin complex
Proteomics
8
3221-3228
2008
Homo sapiens
Gu, J.; Isaji, T.; Sato, Y.; Kariya, Y.; Fukuda, T.
Importance of N-glycosylation on alpha5beta1 integrin for its biological functions
Biol. Pharm. Bull.
32
780-785
2009
Homo sapiens
Gu, J.; Taniguchi, N.
Potential of N-glycan in cell adhesion and migration as either a positive or negative regulator
Cell Adh. Migr.
2
243-245
2008
Homo sapiens
Pinho, S.S.; Reis, C.A.; Paredes, J.; Magalhaes, A.M.; Ferreira, A.C.; Figueiredo, J.; Xiaogang, W.; Carneiro, F.; Gaertner, F.; Seruca, R.
The role of N-acetylglucosaminyltransferase III and V in the post-transcriptional modifications of E-cadherin
Hum. Mol. Genet.
18
2599-2608
2009
Homo sapiens
Kariya, Y.; Kato, R.; Itoh, S.; Fukuda, T.; Shibukawa, Y.; Sanzen, N.; Sekiguchi, K.; Wada, Y.; Kawasaki, N.; Gu, J.
N-Glycosylation of laminin-332 regulates its biological functions. A novel function of the bisecting GlcNAc
J. Biol. Chem.
283
33036-33045
2008
Homo sapiens
Sato, Y.; Isaji, T.; Tajiri, M.; Yoshida-Yamamoto, S.; Yoshinaka, T.; Somehara, T.; Fukuda, T.; Wada, Y.; Gu, J.
An N-glycosylation site on the beta-propeller domain of the integrin alpha5 subunit plays key roles in both its function and site-specific modification by beta1,4-N-acetylglucosaminyltransferase III
J. Biol. Chem.
284
11873-11881
2009
Homo sapiens
Gu, J.; Sato, Y.; Kariya, Y.; Isaji, T.; Taniguchi, N.; Fukuda, T.
A mutual regulation between cell-cell adhesion and N-glycosylation: implication of the bisecting GlcNAc for biological functions
J. Proteome Res.
8
431-435
2009
Homo sapiens, Mus musculus
Pinho, S.S.; Figueiredo, J.; Cabral, J.; Carvalho, S.; Dourado, J.; Magalhaes, A.; Gaertner, F.; Mendonca, A.M.; Isaji, T.; Gu, J.; Carneiro, F.; Seruca, R.; Taniguchi, N.; Reis, C.A.
E-cadherin and adherens-junctions stability in gastric carcinoma: Functional implications of glycosyltransferases involving N-glycan branching biosynthesis, N-acetylglucosaminyltransferases III and V
Biochim. Biophys. Acta
1830
2690-2700
2012
Homo sapiens, Homo sapiens (Q09327)
Xu, Q.; Akama, R.; Isaji, T.; Lu, Y.; Hashimoto, H.; Kariya, Y.; Fukuda, T.; Du, Y.; Gu, J.
Wnt/beta-catenin signaling down-regulates N-acetylglucosaminyltransferase III expression: the implications of two mutually exclusive pathways for regulation
J. Biol. Chem.
286
4310-4318
2011
Homo sapiens
Xu, Q.; Isaji, T.; Lu, Y.; Gu, W.; Kondo, M.; Fukuda, T.; Du, Y.; Gu, J.
Roles of N-acetylglucosaminyltransferase III in epithelial-to-mesenchymal transition induced by transforming growth factor beta1 (TGF-beta1) in epithelial cell lines
J. Biol. Chem.
287
16563-16574
2012
Homo sapiens, Mus musculus
Reinke, S.; Bayer, M.; Berger, M.; Blanchard, V.; Hinderlich, S.
Analysis of cell surface N-glycosylation of the human embryonic kidney 293T cell line
J. Carbohydr. Chem.
30
218-232
2011
Homo sapiens
-
Pinho, S.S.; Oliveira, P.; Cabral, J.; Carvalho, S.; Huntsman, D.; Gaertner, F.; Seruca, R.; Reis, C.A.; Oliveira, C.
Loss and recovery of Mgat3 and GnT-III mediated E-cadherin N-glycosylation is a mechanism involved in epithelial-mesenchymal-epithelial transitions
PLoS ONE
7
e33191
2012
Homo sapiens
Bubka, M.; Link-Lenczowski, P.; Janik, M.; Pochec, E.; Litynska, A.
Overexpression of N-acetylglucosaminyltransferases III and V in human melanoma cells. Implications for MCAM N-glycosylation
Biochimie
103
37-49
2014
Homo sapiens (Q09327), Homo sapiens
Hanashima, S.; Korekane, H.; Taniguchi, N.; Yamaguchi, Y.
Synthesis of N-glycan units for assessment of substrate structural requirements of N-acetylglucosaminyltransferase III
Bioorg. Med. Chem. Lett.
24
4533-4537
2014
Homo sapiens (Q09327)
Lu, J.; Isaji, T.; Im, S.; Fukuda, T.; Kameyama, A.; Gu, J.
Expression of N-acetylglucosaminyltransferase III suppresses alpha2,3-sialylation, and its distinctive functions in cell migration are attributed to alpha2,6-sialylation levels
J. Biol. Chem.
291
5708-5720
2016
Homo sapiens (Q09327), Homo sapiens
Link-Lenczowski, P.; Bubka, M.; Balog, C.I.A.; Koeleman, C.A.M.; Butters, T.D.; Wuhrer, M.; Litynska, A.
The glycomic effect of N-acetylglucosaminyltransferase III overexpression in metastatic melanoma cells. GnT-III modifies highly branched N-glycans
Glycoconj. J.
35
217-231
2018
Homo sapiens (Q09327)
Allam, H.; Johnson, B.P.; Zhang, M.; Lu, Z.; Cannon, M.J.; Abbott, K.L.
The glycosyltransferase GnT-III activates Notch signaling and drives stem cell expansion to promote the growth and invasion of ovarian cancer
J. Biol. Chem.
292
16351-16359
2017
Homo sapiens (Q09327)
Deng, Q.; Yin, N.; Chen, Y.; Shan, N.; Liu, X.; Qi, H.
Downregulated N-acetylglucosaminyltransferase III is involved in attenuating trophoblast migration and invasion under hypoxia-reoxygenation condition
J. Matern. Fetal. Neonatal. Med.
32
2369-2375
2019
Homo sapiens (Q09327), Homo sapiens
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