Any feedback?
Information on EC 2.4.1.144 - beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase and Organism(s) Rattus norvegicus and UniProt Accession Q02527
for references in articles please use BRENDA:EC2.4.1.144Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
Word Map
- 2.4.1.144
-
bisect
- n-glycans
- glycosyltransferases
- n-acetylglucosamine
-
fucosyltransferase
- gnt-iv
-
beta-linked
-
xenoantigens
-
tetraantennary
-
e4-pha
- medicine
-
alpha-galactosylation
-
antennary
-
glcnac-tiii
-
trimannosyl
-
erythroagglutinating
- alpha-gal
- diagnostics
- synthesis
The taxonomic range for the selected organisms is: Rattus norvegicus
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, n-acetylglucosaminyltransferase-iii, beta-1,4-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
-
-
-
-
beta-1,4-mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase
-
-
-
-
beta1,4-N-acetylglucosaminyltransferase III
-
-
GnT-III
-
-
N-acetylglucosaminyltransferase III
-
-
-
-
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III
-
-
-
-
uridine diphosphoacetylglucosamine-glycopeptide beta4-acetylglucosaminyltransferase III
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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]
sequential, random or partially random mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
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
-
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-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-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
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
-
GnT-III catalyzes the removal of the bisecting GlcNAc from the bisected oligosaccharide, producing the corresponding nonbisected sugar chain
-
-
r
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
UDP-N-acetyl-D-galactosamine + (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-galactosaminyl-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
UDP-N-acetyl-D-glucosamine + gamma-glutamyltranspeptidase
UDP + gamma-glutamyltranspeptidase with bisecting N-acetyl-D-glucosamine
-
-
?
UDP-N-acetyl-D-glucosamine + GlcNAc-beta-1,2-Man-alpha-1,6-(GlcNAc-beta-1,2-Man-alpha-1,3)-Man-beta-1,4-GlcNAc-beta-1,4-GlcNAc-2-aminopyridine
UDP + GlcNAc-beta-1,2-Man-alpha-1,6-(GlcNAc-beta-1,2-Man-alpha-1,3)(GlcNAc-beta-1,4)-Man-beta-1,4-GlcNAc-beta-1,4-GlcNAc-2-aminopyridine
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + pyridylaminated acceptor substrate
?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + transferrin
UDP + transferrin with bisecting N-acetyl-D-glucosamine
-
-
?
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
-
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
-
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
-
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
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
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
R represents the remainder of the N-oligosaccharide core (+/-fucose), essential for biosynthesis of complex N-linked oligosaccharides
-
-
?
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
-
pyridylaminated biantennary sugar chain
-
-
?
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
-
0.2% activity compared to donor substrate UDP-N-acetyl-D-glucosamine
-
-
?
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
0.2% activity compared to donor substrate UDP-N-acetyl-D-glucosamine
-
-
?
UDP-N-acetyl-D-galactosamine + (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-galactosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
pyridylaminated biantennary sugar chain
-
-
?
UDP-N-acetyl-D-galactosamine + (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-galactosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
0.1% activity compared to donor substrate UDP-N-acetyl-D-glucosamine
-
-
?
UDP-N-acetyl-D-galactosamine + (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-galactosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
0.1% activity compared to donor substrate UDP-N-acetyl-D-glucosamine
-
-
?
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
-
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
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
-
pyridylaminated biantennary sugar chain
-
?
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
-
pyridylaminated biantennary sugar chain
-
-
?
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
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
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
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
-
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
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
-
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
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
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
-
absolute requirement for the conserved residues Asp321 and Asp323 as part of a D-X-D motif
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
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
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
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
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 + (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
-
-
?
additional information
?
-
-
ADP-, CDP-, GDP-, and TDP-glucose are no donor substrates
-
-
?
additional information
?
-
-
specificity towards the sugar moiety of the donor substrate appears to be critically determined during the catalytic process but not during binding to the enzyme in ground state
-
-
?
additional information
?
-
specificity towards the sugar moiety of the donor substrate appears to be critically determined during the catalytic process but not during binding to the enzyme in ground state
-
-
?
additional information
?
-
-
biosynthetic pathway of the core structures of Asn-linked sugar chains, overview
-
-
?
additional information
?
-
biosynthetic pathway of the core structures of Asn-linked sugar chains, overview
-
-
?
additional information
?
-
-
beta1,4-N-acetylglucosaminyltransferase III potentiates beta1 integrin-mediated neuritogenesis induced by serum deprivation in Neuro2a cells
-
-
?
additional information
?
-
-
expression of GnTIII leads to a high proportion of N-glycans of the complex type, modified with the bisecting GlcNAc (median value 37%, q1, 33%, q3, 39%) and a strong reduction of paucimannosidic type N-glycans (median value 2%, q1, 1%, q3.2%) that are abundant in secreted proteins of tobacco BY-2 cells. Native GnTIII expression, the coexpression of Arabidopsis thaliana ManII leads to an increase in the proportion of complex bisected N-glycan structures, whereas the expression of native human ManII does not significantly increase these structures. In the case of chimeric GnTIIIA.th. and chimeric ManIIA.th. expression, reduction in hybrid bisected structures. No viable cultures expressing GnTIIIA.th. and A. thaliana ManII. Plant-specific core fucosylation and xylosylation can be greatly reduced, with up to 59% of N-glycans on endogenous secreted protein lacking the plant-specific modifications
-
-
?
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-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
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
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
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
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
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
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
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
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 + (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
-
-
?
additional information
?
-
-
biosynthetic pathway of the core structures of Asn-linked sugar chains, overview
-
-
?
additional information
?
-
biosynthetic pathway of the core structures of Asn-linked sugar chains, overview
-
-
?
additional information
?
-
-
beta1,4-N-acetylglucosaminyltransferase III potentiates beta1 integrin-mediated neuritogenesis induced by serum deprivation in Neuro2a cells
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
Mn2+
-
Asp321 and Asp323 are absolutely required for the coordination of Mn2+ during enzyme reaction
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
castanospermine
-
activity is not affected, but the enzyme is not localized in the Golgi apparatus
tunicamycin
-
completely abolishes the enzyme activity due to deglycosylation of the enzyme, not localized in the Golgi apparatus
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.021
pyridylaminated acceptor substrate
-
with UDP-GlcNAc as donor substrate
-
0.023
pyridylaminated acceptor substrate
-
with UDP-Glc as donor substrate
-
0.024
pyridylaminated acceptor substrate
-
with UDP-GalNAc as donor substrate
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.3
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
about 100fold increased activity compared to normal liver tissue
additional information
primary, about 100fold increased activity compared to normal liver tissue
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
tunicamycin-treated and castanospermine-treated enzyme, not native enzyme
-
deglycosylated mutants are not localized in the Golgi apparatus
deglycosylated mutants are not localized in the Golgi apparatus
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
levels of fucosylation (79%, median value 80%, q1, 78%, q3, 82%) and xylosylation (94, median value 94%, q1, 93%, q3, 95%) are not significantly reduced in cells expressing GnTIII under the control of the CaMV 35S promoter compared to the levels observed in wild-type cells. Expression of GnTIII under the control of the UAS123mas promoter reduces fucosylation, but not xylosylation
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_RAT
538
1
62022
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
glycoprotein
-
3 N-glycosylation sites: Asn243, Asn261, Asn399, essential for activity, tunicamycin-treated enzyme, which is not glycosylated, shows no activity
glycoprotein
3 N-glycosylation sites: Asn243, Asn261, Asn399, essential for activity, tunicamycin-treated enzyme, which is not glycosylated, shows no activity
glycoprotein
-
3 N-glycosylation sites: Asn243, Asn261, Asn399, essential for activity, tunicamycin-treated enzyme, which is not glycosylated, shows no activity
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D321A
D323A
N243Q
N243Q/N261Q
N243Q/N261Q/N399Q
N243Q/N399Q
N261Q
N261Q/N399Q
N399Q
D321A
-
site-directed mutagenesis, expression level in COS-1 cells similar to wild-type, but no remaining catalytic activity
D323A
-
site-directed mutagenesis, expression level in COS-1 cells similar to wild-type, but no remaining catalytic activity
D323A
-
expression of a catalytically inactive D232A mutant in human hepatoblastoma cell line Huh6, leading to suppression of the endogenous enzyme activity, but not to a significant decrease in the expression level of the endogenous enzyme
N243Q
-
site-directed mutagenesis of 1 N-glycosylation site, 40-50% activity compared to the wild-type, slightly increased Km-value for the donor substrate
N243Q/N261Q
-
site-directed mutagenesis of 2 N-glycosylation sites, 10% activity compared to the wild-type
N243Q/N261Q/N399Q
-
site-directed mutagenesis of all N-glycosylation sites, no remaining activity
N243Q/N399Q
-
site-directed mutagenesis of 2 N-glycosylation sites, highly reduced activity
N261Q
-
site-directed mutagenesis of 1 N-glycosylation site, 40-50% activity compared to the wild-type, slightly increased Km-value for the donor substrate
N261Q/N399Q
-
site-directed mutagenesis of 2 N-glycosylation sites, highly reduced activity
N399Q
-
site-directed mutagenesis of 1 N-glycosylation site, 70-80% activity compared to the wild-type
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
primary structure
recombinant His-tagged protein from medium of Spodoptera frugiperda Sf 21 cell culture
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning from genetic library, DNA sequence determination, functional overexpression in COS-1 or HeLa-cells, transient transfection
construction of genes for expression of native rat GnTIII, human ManII, Arabidopsis thaliana ManII and for the expression of the catalytic domains of rat GnTIII and human ManII fused to the N-terminal region of Arabidopsis thaliana ManII. Binary plasmids for high-level expression of rat GnTIII (pAX67), chimeric rat GnTIIIA.th. (replaced native localization domain with the cytoplasmic tail, transmembrane, and stem region of Arabidopsis thaliana mannosidase II) (pAX70), co-expression of rat GnTIII together with human ManII (pAX73) or Arabidopsis thaliana ManII (pAX100), co-expression of GnTIIIA.th. together with ManIIA.th. (pAX74), and co-expression of GnTIIIA.th. and Arabidopsis thaliana ManII (pAX101). Expression of the transgenes is driven by a chimeric promoter assembled from regulatory elements from mannopine and octopine synthase genes. Expression cassettes comprising the CaMV 35S promoter, GnTIII or ManII and the nos pA, being pSK103 (ManII), pSK124 (ManII-Arabidopsis thaliana), pAX63 (GnTIII-Arabidopsis thaliana) and pAX68 (GnTIII) serve as starting point for further expression constructs. The cassette comprising the CaMV 35 promoter, plant relocalized GnTIII and polyadenylation signal is excised from pAX68 using SbfI, EcoRI and inserted into pAX36 generating pAX90. The construct comprising the rat GnTIII obtained by replacing the XbaI, AflII fragment from pAX90 with the fragment isolated from pAX63, generating pAX91. Mutated fragment from pCLF40 inserted into pAX69 using AvaI, StuI, generating pAX104. The binary expression plasmids for inactive GnTIII and GnTIIIA.th. under the control of the UAS123mas promoter generated by replacing the StuI, EcoRI fragment from pAX104 with that in pAX67 (generating pAX105) and pAX70 (generating pAX106), respectively. The mutated fragment from pCLF40 inserted into pAX91 using Eam1105I, StuI, generating the expression plasmid for inactive GnTIII under the control of the CaMV 35S promoter (pAX108). The exchange of the fragment containing the Arabidopsis thaliana Golgi localization domain from pAX90 in pAX108 using SbfI, StuI yields an expression plasmid for inactive GnTIIIA.th. under the control of the CaMV 35S promoter. Plasmids transferred into Agrobacterium tumefaciens LBA4404 for transformation into tobacco BY-2 cells
-
construction of transgenic mice, disruption of certain functions of apolipoprotein B leading to generation of a aftty liver
expression of a catalytically inactive D232A mutant in human hepatoblastoma cell line Huh6, leading to suppression of the endogenous enzyme activity, but not to a significant decrease in the expression level of the endogenous enzyme
-
expression of soluble His-tagged protein in Spodoptera frugiperda Sf 21 insect cells via baculovirus infection, secretion into the medium
expression of wild-type and mutants in COS-1 cells
GnT-III stable expressing cell lines of Neuro-2a mouse neuroblastoma cells and B16 mouse melanoma cells are established. Overexpression of GnT-III up-regulates adenylyl cyclases activity in Neuro-2a mouse neuroblastoma cells and B16 mouse melanoma cells
-
overexpression in rat pheochromocytoma cell line PC-12, glycoproteins contain elevated levels of bisecting GlcNAc, abolished cell differentiation
rat GnTIII is expressed either with its native localization domain (GnTIII) or with the cytoplasmic tail, transmembrane domain and stem region (CTS) of Arabidopsis thaliana mannosidase II. N-Glycans of plants expressing rat GnTIII contain three major glycan structures of complex bisected, complex, or hybrid bisected type, accounting for 70%-85% of the total N-glycans. Expression of rat beta(1,4)-N-acetylglucosaminyltransferase III in Nicotiana tabacum remodels the plant-specific N-glycosylation
-
construction of transgenic mice, disruption of certain functions of apolipoprotein B leading to generation of a aftty liver
construction of transgenic mice, disruption of certain functions of apolipoprotein B leading to generation of a aftty liver
expression of soluble His-tagged protein in Spodoptera frugiperda Sf 21 insect cells via baculovirus infection, secretion into the medium
-
expression of soluble His-tagged protein in Spodoptera frugiperda Sf 21 insect cells via baculovirus infection, secretion into the medium
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
apart from GnT-III overexpression, engineering of GnT-III localization is a versatile tool to modulate the biological activities of antibodies relevant for their therapeutic application
synthesis
-
RC12 cells, apheochromocytoma cell line, transfected with enzyme gene, result in suppression of neurite outgrowth induced by costimulation of epidermal growth factor and integrins. Epidermal growth factor receptor-mediated ERK-activation is blocked in transfectants. Epidermal growth factor receptor of transfectants is modified by bisecting GlcNAc in its N-glycan structures
REF.
AUTHORS
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
Taniguchi, N.; Nishikawa, A.; Fujii, S.; Gu, J.
Glycosyltransferase assays using pyridylaminated acceptors: N-acetylglucosaminyltransferase III, IV, and V
Methods Enzymol.
179
397-408
1989
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)
Nagai, K.; Ihara, Y.; Wada, Y.; Taniguchi, N.
N-Glycosylation is requisite for the enzyme activity and Golgi retention of N-acetylglucosaminyltransferase III
Glycobiology
7
769-776
1997
Rattus norvegicus
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)
Ikeda, Y.; Koyota, S.; Ihara, H.; Yamaguchi, Y.; Korekane, H.; Tsuda, T.; Sasai, K.; Taniguchi, N.
Kinetic basis for the donor nucleotide-sugar specificity of beta1,4-N-acetylglucosaminyltransferase III
J. Biochem.
128
609-619
2000
Rattus norvegicus
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
Gu, J.; Zhao, Y.; Isaji, T.; Shibukawa, Y.; Ihara, H.; Takahashi, M.; Ikeda, Y.; Miyoshi, E.; Honke, K.; Taniguchi, N.
beta1,4-N-Acetylglucosaminyltransferase III down-regulates neurite outgrowth induced by costimulation of epidermal growth factor and integrins through the Ras/ERK signaling pathway in PC12 cells
Glycobiology
14
177-186
2004
Rattus norvegicus
Ferrara, C.; Bruenker, P.; Suter, T.; Moser, S.; Puentener, U.; Umana, P.
Modulation of therapeutic antibody effector functions by glycosylation engineering: influence of Golgi enzyme localization domain and co-expression of heterologous beta1,4-N-acetylglucosaminyltransferase III and Golgi alpha-mannosidase II
Biotechnol. Bioeng.
93
851-861
2006
Rattus norvegicus
Shigeta, M.; Shibukawa, Y.; Ihara, H.; Miyoshi, E.; Taniguchi, N.; Gu, J.
beta1,4-N-Acetylglucosaminyltransferase III potentiates beta1 integrin-mediated neuritogenesis induced by serum deprivation in Neuro2a cells
Glycobiology
16
564-571
2006
Rattus norvegicus
Li, W.; Takahashi, M.; Shibukawa, Y.; Yokoe, S.; Gu, J.; Miyoshi, E.; Honke, K.; Ikeda, Y.; Taniguchi, N.
Introduction of bisecting GlcNAc in N-glycans of adenylyl cyclase III enhances its activity
Glycobiology
17
655-662
2007
Rattus norvegicus
Frey, A.D.; Karg, S.R.; Kallio, P.T.
Expression of rat beta(1,4)-N-acetylglucosaminyltransferase III in Nicotiana tabacum remodels the plant-specific N-glycosylation
Plant Biotechnol. J.
7
33-48
2009
Rattus norvegicus
Okada, T.; Ihara, H.; Ito, R.; Taniguchi, N.; Ikeda, Y.
Bidirectional N-acetylglucosamine transfer mediated by beta-1,4-N-acetylglucosaminyltransferase III
Glycobiology
19
368-374
2009
Rattus norvegicus
Karg, S.R.; Frey, A.D.; Kallio, P.T.
Reduction of N-linked xylose and fucose by expression of rat beta1,4-N-acetylglucosaminyltransferase III in tobacco BY-2 cells depends on Golgi enzyme localization domain and genetic elements used for expression
J. Biotechnol.
146
54-65
2010
Rattus norvegicus
EXTERNAL LINKS (specific for EC-Number 2.4.1.144)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
