Information on EC 2.4.1.101 - alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY hide
2.4.1.101
-
RECOMMENDED NAME
GeneOntology No.
alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-D-glucosamine + 3-(alpha-D-mannosyl)-beta-D-mannosyl-R = UDP + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
mannosyl-glycoprotein N-acetylglucosaminyltransferases
-
-
Metabolic pathways
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N-Glycan biosynthesis
-
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Various types of N-glycan biosynthesis
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-
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-glucosamine:3-(alpha-D-mannosyl)-beta-D-mannosyl-glycoprotein 2-beta-N-acetyl-D-glucosaminyltransferase
R represents the remainder of the N-linked oligosaccharide in the glycoprotein acceptor. Note that this enzyme acts before N-acetylglucosaminyltransferases II, III, IV, V and VI (click here for diagram).
CAS REGISTRY NUMBER
COMMENTARY hide
102576-81-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
sycamore
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
no activity in Saccharomyces cerevisiae
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-
-
Manually annotated by BRENDA team
diatom
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-
Manually annotated by BRENDA team
constitutive single copy gene
Uniprot
Manually annotated by BRENDA team
2 isozymes A and B
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-glucosamine + 2-deoxy-Manalpha6(Manalpha3)Man-beta-octyl
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 3-(alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
show the reaction diagram
UDP-N-acetyl-D-glucosamine + 3-O-(4,4-azopentyl)-Manalpha6(Manalpha3)Man-beta-octyl
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 3-O-(4,5-epoxypentyl)-Manalpha6(Manalpha3)Man-beta-octyl
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 3-O-(5-iodoacetamidopentyl)-Manalpha6(Manalpha3)Man-beta-octyl
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 3-O-pentyl-Manalpha6(Manalpha3)Man-beta-octyl
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 4-O-methyl-Manalpha6(Manalpha3)Man-beta-octyl
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 6-O-methyl-Manalpha6(Manalpha3)Man-beta-octyl
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,3-(alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
show the reaction diagram
UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,3-beta-D-mannosyl-1,4-N-acetyl-D-glucosamine
UDP + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-beta-D-mannosyl-1,4-N-acetyl-D-glucosamine
show the reaction diagram
UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-1,4-N-acetyl-D-glucosaminyl-Asn-peptide
UDP + alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-alpha-D-mannosyl-1,6-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-Asn-peptide
show the reaction diagram
UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-alpha-D-mannosyl-1,6-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
show the reaction diagram
UDP-N-acetyl-D-glucosamine + asialofetuin
?
show the reaction diagram
-
beta-galactosidase-, beta-N-acetylhexosamidase- and alpha-mannosidase-treated asialofetuin, beta-galactosidase- and beta-N-acetylhexosamidase-treated asialofetuin
-
-
?
UDP-N-acetyl-D-glucosamine + beta-galactosidase- and beta-N-acetylhexosamidase-treated asialotransferrin
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + dehexoso-orosomucoid
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + desialo-degalacto-dehexosamine-orosomucoid
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + fowl plague virus hemagglutinin
UDP + fowl plague virus hemagglutinin with terminal N-acetyl-D-glucosaminyl residues
show the reaction diagram
-
recombinant coexpression of enzyme and substrate in SF9 insect cells
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?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta(1-2)Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
UDP + GlcNAcbeta(1-2)Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
show the reaction diagram
3.9% activity compared to Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
-
-
?
UDP-N-acetyl-D-glucosamine + GlcUAcbeta1-3Galbeta1-O-naphthalenemethanol
?
show the reaction diagram
-
synthetic substrate
-
-
?
UDP-N-acetyl-D-glucosamine + glycopeptides prepared from porcine IgC
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Man3Man-O-beta4-N-acetyl-D-glucosamine
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Man5-RNAse B
UDP + RNAse B-GlcNAc2-Man5-GlcNAc
show the reaction diagram
-
wild type hGnT1 and mutants C121A, C121S and R120A/C121H transfer GlcNAc from UDP-GlcNAc to the glycoprotein acceptor Man5-RNAse B, whereas mutants C121T and C121D are inactive. After 1 h, the wild-type MBP-hGnT1(D103) and C121A mutant convert more than 50% of RNAse BM5 to RNAse BM5Gn, while the C121S mutant shows less than 25% conversion. The wild-type MBP-hGnT1(D103) and both C121A and C121S mutants convert RNAse BM5 nearly completely to RNAse BM5Gn following overnight incubation. The R120A/C121H mutant is less active than the wild-type and the single mutants. It converts more than half of the RNAse BM5 into RNAse BM5Gn after 17 h
-
-
?
UDP-N-acetyl-D-glucosamine + Man5GlcNAc2
?
show the reaction diagram
UDP-N-acetyl-D-glucosamine + Man5GlcNAc2-glycopeptide
UDP + GlcNAc(1-2)Man5GlcNAc2-glycopeptide
show the reaction diagram
UDP-N-acetyl-D-glucosamine + Manalpha(1-2)Manalpha(1-3)[Manalpha(1-6)]Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
UDP + Manalpha(1-2)Manalpha(1-3)[Manalpha(1-6)]Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
show the reaction diagram
0.5% activity compared to Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha(1-3)Man
UDP + ?
show the reaction diagram
UDP-N-acetyl-D-glucosamine + Manalpha(1-3)Manalpha(1-6)Man
UDP + ?
show the reaction diagram
UDP-N-acetyl-D-glucosamine + Manalpha(1-3)Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-R
UDP + Manalpha(1-3)Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-R
show the reaction diagram
UDP-N-acetyl-D-glucosamine + Manalpha(1-3)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
UDP + GlcNAcbeta(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
show the reaction diagram
0.7% activity compared to Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha(1-6)Man
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
UDP + Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
show the reaction diagram
100% activity
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-R
UDP + Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-R
show the reaction diagram
UDP-N-acetyl-D-glucosamine + Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
UDP + Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
show the reaction diagram
6.9% activity compared to Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-R
UDP + Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-R
show the reaction diagram
UDP-N-acetyl-D-glucosamine + Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)[Fucalpha(1-3)]GlcNAc-pyridylaminoside
UDP + Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)[Fucalpha(1-3)]GlcNAc-pyridylaminoside
show the reaction diagram
6.2% activity compared to Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha1,6(Manalpha1,3)Manbeta-1-O-octyl
UDP + GlcNAc(1-2)Manalpha(1-6)Manalpha(1-3)Manbeta-1-O-octyl
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha1,6(Manalpha1,3)Manbeta-1-O-octyl
UDP + GlcNAcalpha(1-2)Manalpha(1-6)Manalpha(1-3)Manbeta-1-O-octyl
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha6(4-deoxy-Manalpha3)Man-beta-octyl
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha6(4-O-(5-iodoacetamidopentyl)-Manalpha3)Man-beta-octyl
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha6(4-O-methyl-Manalpha3)Man-beta-octyl
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha6(Manalpha3)Man-O-beta hexyl
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha6(Manalpha3)Man-O-beta(8-methoxycarbonyl)octyl
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha6(Manalpha3)Man-O-beta-octyl
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha6(Manalpha3)Man-O-beta4-N-acetyl-D-glucosamine
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha6(Manalpha3)Man-O-beta4-N-acetyl-D-glucosamine-beta4(L-fucose-alpha6)-N-acetyl-D-glucosamine-Asn
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha6(Manalpha3)Man-O-beta4-N-acetyl-D-glucosamine-beta4-N-acetyl-D-glucosamine
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosamine-beta2-Manalpha6(Manalpha3)Man-beta4-N-acetyl-D-glucosamine
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetylglucosamine-1,4-(fucose-1,6)-N-acetyl-glucosamine-Asn-peptide
UDP + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetylglucosamine-1,4-(fucose-1,6)-N-acetyl-glucosamine-Asn-peptide
show the reaction diagram
UDP-N-acetyl-D-glucosamine + ovalbumin
?
show the reaction diagram
UDP-N-acetyl-D-glucosamine + ovalbumin glycopeptide III A-C
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + ovalbumin glycopeptide IV
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + ovalbumin glycopeptide V
UDP + ovalbumin glycopeptide IIIA
show the reaction diagram
UDP-N-acetyl-D-glucosamine + R-Manalpha6(Manalpha3)Man-beta-octyl
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + [Manalpha(1-6)Manalpha(1-3)Manalpha(1-6)][Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-Asn
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + [Manalpha1,6(Manalpha1,3)Manalpha1,6](Manalpha1,3)Manbeta1,4GlcAcbeta1,4GlcNAc-R
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetylglucosamine + 3-(alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2-(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D-mannosyl-R
show the reaction diagram
-
-
-
-
-
UDP-N-acetylglucosamine + alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-1,4-N-acetyl-D-glucosaminyl-Asn-peptide
UDP + alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-alpha-D-mannosyl-1,6-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
show the reaction diagram
-
regioselective and stereoselective addition of beta-1,2-N-acetylglucosamine to a high mannose oligosaccharide from yeast, room temperature, 2.7fold excess of UDP-N-acetylglucosamine over the oligosaccharide substrate, 20 mM HEPES, pH 7.5, 150 mM NaCl, 20 mM MnCl2
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-glucosamine + 3-(alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
show the reaction diagram
UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-1,4-N-acetyl-D-glucosaminyl-Asn-peptide
UDP + alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-alpha-D-mannosyl-1,6-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-Asn-peptide
show the reaction diagram
UDP-N-acetyl-D-glucosamine + ovalbumin glycopeptide V
UDP + ovalbumin glycopeptide IIIA
show the reaction diagram
-
physiological substrate
-
-
?
UDP-N-acetylglucosamine + 3-(alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2-(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D-mannosyl-R
show the reaction diagram
-
-
-
-
-
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Sn2+
-
slight activation
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2'-dUDP
-
weak
2'-O-Methyl-UDP
-
weak
5-Bromo-UTP
-
-
5-Mercury-UDP
-
-
alpha-D-Mannosyl-1,3-(alpha-D-mannosyl-1,6)-4-O-methyl-beta-D-mannosyl-1,4-N-acetyl-D-glucosamine
-
weak
alpha-D-mannosyl-1,6-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
-
Antibodies to pig liver N-acetylglucosaminyltransferase I
-
-
-
Ca2+
-
-
Manalpha6(6-O-(4,4-azopentyl)-Manalpha3)Man-beta-octyl
-
-
Manalpha6(6-O-(4,5-epoxypentyl)-Manalpha3)Man-beta-octyl
-
-
Manalpha6(6-O-(4-oxopentyl)-Manalpha3)Man-beta-octyl
-
-
Manalpha6(6-O-(5-pentanolyl)-Manalpha3)Man-beta-octyl
-
-
Manalpha6(6-O-methyl-Manalpha3)Man-beta-octyl
-
-
UDP-glucose
-
weak
UDP-N-acetylgalactosamine
-
weak
UDP-N-acetylglucosamine
-
competitively to UDP
Zn2+
-
-
[Manalpha6(Manalpha3)][4-O-methyl-Man]-beta4-N-acetyl-D-glucosamine
-
-
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CHAPS
-
slight activation
Triton X-100
Zwittergent 3-12
-
slight activation
additional information
-
no activation by 2-mercaptoethanol
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6
2-deoxy-Manalpha6(Manalpha3)Man-beta-octyl
-
-
1.2
3-O-(4,4-azopentyl)-Manalpha6(Manalpha3)Man-beta-octyl
-
-
1.8
3-O-(4,5-epoxypentyl)-Manalpha6(Manalpha3)Man-beta-octyl
-
-
1.4
3-O-(5-iodoacetamidopentyl)-Manalpha6(Manalpha3)Man-beta-octyl
-
-
3.5
3-O-pentyl-Manalpha6(Manalpha3)Man-beta-octyl
-
-
0.9
4-O-methyl-Manalpha6(Manalpha3)Man-beta-octyl
-
-
0.3
6-O-methyl-Manalpha6(Manalpha3)Man-beta-octyl
-
-
0.078
alpha-D-mannosyl-1,3-(alpha-D-mannosyl-1,6)-alpha-D-mannosyl-1,3-(alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-D-glucosamine
-
-
0.25 - 0.47
alpha-D-mannosyl-1,3-(alpha-D-mannosyl-1,6)-alpha-D-mannosyl-1,3-(alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-1,4-N-acetylglucosamine
2.03
alpha-D-mannosyl-1,3-(alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-D-glucosamine
-
-
0.0384 - 0.2
alpha-D-mannosyl-1,3-(alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
0.39 - 0.45
alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetyl-D-glucosamine
7.4
alpha-mannosyl-1,3-beta-mannosyl-1,4-N-acetylglucosamine
-
-
0.26 - 5.43
Man5GlcNAc2
0.5
Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
recombinant enzyme, pH not specified in the publication, at 25C
22
Manalpha6(4-deoxy-Manalpha3)Man-beta-octyl
-
-
5
Manalpha6(4-O-(5-iodoacetamidopentyl)-Manalpha3)Man-beta-octyl
-
-
2.6
Manalpha6(4-O-methyl-Manalpha3)Man-beta-octyl
-
-
1.7
Manalpha6(Manalpha3)Man-O-beta hexyl
-
-
1.5
Manalpha6(Manalpha3)Man-O-beta(8-methoxycarbonyl)octyl
-
-
0.7
Manalpha6(Manalpha3)Man-O-beta-octyl
-
-
2.7 - 4.5
Manalpha6(Manalpha3)Man-O-beta4-N-acetyl-D-glucosamine
0.4
Manalpha6(Manalpha3)Man-O-beta4-N-acetyl-D-glucosamine-beta4(L-fucose-alpha6)-N-acetyl-D-glucosamine-Asn
-
-
1.8
Manalpha6(Manalpha3)Man-O-beta4-N-acetyl-D-glucosamine-beta4-N-acetyl-D-glucosamine
-
-
1.9
N-acetyl-D-glucosamine-beta2-Manalpha6(Manalpha3)Man-beta4-N-acetyl-D-glucosamine
-
-
0.43
N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-pyridinylamine
-
-
-
10
N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
immunoglobulin G glycopeptide
0.44 - 4.5
ovalbumin
0.12 - 0.33
ovalbumin glycopeptide V
1.6
pyridylaminated Man3GlcNAc2
-
recombinant isozyme A
0.036 - 7.56
UDP-N-acetyl-D-glucosamine
0.4
[Manalpha6(Manalpha3)Manalpha6][Manalpha3]Man-beta4-N-acetyl-D-glucosamine-beta4-N-acetyl-D-glucosamine-Asn
-
-
additional information
additional information
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.8
alpha-D-mannosyl-1,6-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
-
1.1
Manalpha6(6-O-(4,4-azopentyl)-Manalpha3)Man-beta-octyl
-
-
2.6
Manalpha6(6-O-(4,5-epoxypentyl)-Manalpha3)Man-beta-octyl
-
-
8.8
Manalpha6(6-O-(4-oxopentyl)-Manalpha3)Man-beta-octyl
-
-
10.2
Manalpha6(6-O-(5-pentanolyl)-Manalpha3)Man-beta-octyl
-
-
0.8
Manalpha6(6-O-methyl-Manalpha3)Man-beta-octyl
-
-
0.034
UDP-N-acetylglucosamine
-
-
13
[Manalpha6(Manalpha3)][4-O-methyl-Man]-beta4-N-acetyl-D-glucosamine
-
-
additional information
additional information
-
several inhibitory synthetic acceptor substrate analogues, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000002
-
wild-type S49 cell
0.00000084
-
wild-type CHO cell
0.000015
-
transferase A, liver
0.00065
-
transferase B, hepatoma
0.079
-
alpha-D-mannosyl-1,3-(alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R immunoglobulin G glycopeptide
0.106
-
alpha1-acid glycoprotein treated with mild acid, beta-galactosidase and beta-N-acetylglucosamidase
0.48
-
room temperature, 2.7fold excess of UDP-N-acetylglucosamine over the oligosaccharide substrate, 20 mM HEPES, pH 7.5, 150 mM NaCl, 20 mM MnCl2
0.6
-
recombinant isozyme A
2.51
-
purified enzyme
3.37
-
purified enzyme
4.8
-
liver
19.8
-
low-molecular weight form
20
-
purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
-
broad optimum
5.8
-
-
6.5
-
recombinant fusion protein
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8.5
activity decreases to less than 15% of the maximum at pH values lower than 5.0 and higher than 8.5
5.1 - 6.9
-
about half-maximal activity at pH 5.1 and about 70% of maximal activity at pH 6.9
6.5 - 9
-
recombinant fusion protein
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
recombinant fusion protein
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 70
-
recombinant fusion protein
0 - 45
the activity decreases with increasing reaction temperature and is completely abolished at temperatures higher than 45C. On the other hand, substantial GnTI activity is detected at low temperatures, even at 0C (approximately 50% of the maximum)
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
two forms of beta 2-N-acetylglucosaminyltransferase I in rat testicular and epididymal fluids
Manually annotated by BRENDA team
-
of oviduct
Manually annotated by BRENDA team
-
isozyme B, low content of isozyme A
Manually annotated by BRENDA team
-
diethylnitrosamine- or dimethylaminoazobenzene-induced hepatoma, Morris 5123D hepatoma or AH-109A, solid or ascitic
Manually annotated by BRENDA team
-
isozyme B, low content of isozyme A
Manually annotated by BRENDA team
-
isozymes A and B
Manually annotated by BRENDA team
-
no significant difference between the GnT I activities from dominant follicles collected before and after surge of luteinizing hormone
Manually annotated by BRENDA team
-
isozymes A and B
Manually annotated by BRENDA team
-
BOEC cell
Manually annotated by BRENDA team
-
two forms of beta 2-N-acetylglucosaminyltransferase I in rat testicular and cauda epididymal fluids
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
in recombinant Saccharomyces cerevisisae
Manually annotated by BRENDA team
-
in recombinant Saccharomyces cerevisisae
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
-
SDS-PAGE
59000
-
SDS-PAGE
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
no glycoprotein
-
recombinant catalytic fragment, no glycosylation sites
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
catalytic enzyme fragment in presence and absence of UDP-N-acetyl-D-glucosamine and Mn2+, hanging drop vapour diffusion method, protein 10 mg/ml + 10 mM MES, pH 5.5, + 270 mM KCl + 2 mM MnCl2, 10 mM UDP-N-acetyl-D-glucosamine, well-solution: 100 mM Tris-HCl, pH 7.9, 15-20% polyethylene glycol , X-ray structure determination and analysis
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
the enzymatic activity is maintained after a 90-min incubation at pH values 6.0-9.5, but it is mostly abolished at pH values 5.0 and 10.0
722834
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 45
the activity is stable after a 2 h incubation at a temperature lower than 25C, but it significantly decreases after incubation at 35C and is completely abolished at temperatures higher than 45C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freeze-thawing, solubilized enzyme, unstable to
-
repeated freeze-thawing, stable to
Triton X-100, 0.1%, and albumin, 0.01%, stabilize solubilized enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 20% glycerol v/v, up to a year
-
-20C, at least 6 months
-
3C, at least a month
-
4C, in 20% glycerol, 0.1% Triton X-100, 25 mM MES-buffer, pH 6.5, 10 mM MnCl2, 1 mM PMSF, 0.1 mM 6-aminocaproic acid and 0.02% NaN3, several months
-
4C, in dilute solution, t1/2: 1 day
-
4C, in the presence of albumin, at least a month
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatography
-
amylose resin column chromatography, gel filtration
antibody purification from homogenized transfected Nicotiniana benthamiana leaves, resuspended in extraction buffer (PBS, pH 7.2, 1% Triton-X-100, protease inhibitor cocktail), centrifugation, supernatant incubated with rProtein A-Sepharose, elution by boiling Laemmli sample buffer, protein gel blot analysis with specific antibodies
-
large scale, recombinant maltose-binding fusion protein
-
liver
-
mutant enzyme D144N
-
one Ni2+-NTA chromatography step is sufficient for oligosaccharide synthesis
-
partial
-
partial; two forms: transferase A and B, the latter only in hepatoma
-
recombinant catalytic fragment from Sf9 insect cells
-
recombinant glutathione S-transferase fusion isozymes and mutants from insect Sf21 cells
-
recombinant N-terminally His-tagged protein from Escherichia coli
-
two molecular weight forms separable by gel filtration, purification of low-molecular weight form
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Agrobacterium-mediated transformation of alfalfa
-
cDNA clone, constructed type-II-surface membrane-protein/human transferase chimeras are transfected into Madin-Darby canine kidney cells
-
cloning and DNA sequence determination and analysis
cloning of isozymes A and B, 2 separate genes, DNA sequence determination and analysis; functional expression of isozymes A and B in Spodoptera frugiperda Sf21 cells as glutathione-S-transferase fusion proteins via baculovirus infection, isozyme B is folded less efficiently
-
expressed in Chinese hamster ovary Lec1 mutant cells defective in endogeneous N-acetylglucosaminyltransferase I
-
expressed in CHO-DUKX-Lec1 cells
-
expression in Saccharomyces cerevisiae, tagged with c-Myc epitope
-
expression of catalytic fragment in Spodoptera frugiperda Sf9 cells via baculovirus infection
-
expression of the enzymes catalytic domain in Escherichia coli strain BL21, unmodified catalytic domain and His-tagged at the C-terminal and at the N-terminal end
-
expression of the histidine-tagged catalytic domain in Escherichia coli which is supplemented with mammalian tRNA codons and with mutations to improve intracellular disulfide bond formation
-
expression of the mutant enzyme D144N in insect cells
-
expression of YFP or CFP fusion enzyme of Arabidopsis and human N-acetylglucosaminyltransferase I, and the chimeric enzyme of Arabidopsis CTS region and human catalytic domain in mutant cgl1-1 Arabidopsis (lacking N-acetylglucosaminyltransferase I), transformed by Agrobacterium tumefaciens
functional expression of c-Myc-tagged full length clone and chimera TfR/GnT1myc and exchange mutants of the latter in CHO Lec 1 cells, lacking GnT-1 activity
-
functional expression of unmodified enzyme and as tagged fusion protein in Spodoptera frugiperda Sf9 cells via baculovirus infection, coexpression of fowl plague virus hemagglutinin HA as endogenous substrate for in vivo activity assay
-
human beta-1-2-N-acetylglucosaminyltransferase (hGnT1) lacking the first 103 amino acids is expressed as a maltose binding protein (MBP) fusion protein in inclusion bodies in Escherichia coli and refolded using an oxido-shuffling method. Cloning and expression of MBP-hGnT1(D103) and mutant MBP-hGnT1 (D103) enzymes
-
in one construct, the catalytic domain of human GNT I (abbreviated as NA) is fused to the MNN9 leader (abbreviated as 15) from Saccharomyces cerevisiae to yield construct NA15. In a second construct, a fungal codon-optimized form is combined with the same MNN9 leader to yield construct coNA15. Expression in Aspergillus nidulans and Aspergillus niger
-
PCR-amplification of CTS region (N-terminal cytoplasmic tail, transmembrane domain, stem region), fusion to GFP (green fluorescent protein), expression of vector in Nicotiana benthamiana mediated by Agrobacterium tumefaciens strain UIA143
-
the enzyme fused to maltose-binding protein is expressed in Escherichia coli Rosetta-gami B(DE3) cells
the full length GnT-I gene is expressed in Aspergillus oryzae. GnT-1 is functionally expressed and N-acetylglusosamine is transferred to N-glycan of alpha-amylase in vivo
-
transformation construct contains either the catalytic domain (amino acids 106-447) of wild-type enzyme or D144N rabbit NgTI fused to the CTS region (amino acids 1-102) of Arabidopsis thaliana GnTI under the control of the strong constitutive cauliflower mosaic virus 35S promoter
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
human fusion enzyme expression is about 5fold higher in Arabidopsis cgl1-1 mutant than Arabidopsis and chimeric enzyme expression but lower catalytic activity in the plant and partly distinct sub-cellular localization
-
human fusion enzyme expression is about 5fold higher in Arabidopsis than Arabidopsis enzyme and chimeric enzyme expression but catalytic activity in the plant is lower and shows partly distinct sub-cellular localization
-
limited enzyme expression after anti-CD3 stimulation
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D144N
-
D144N muation in the GnTI of cgl mutant lacking GnTI activity is molecular basis of the defect. The mutation creates an additional N-glycosylation site, which interferes with the proper folding of the enzyme
C907T
point mutation in mutant cell line Lec1A.3E and Lec1A.5J, altering interactions important for stabilization of the structure, correction of the mutation by site-directed mutagenesis restores enzyme activity
G634A
point mutation in mutant cell line Lec1A.2C, disrution of DxD motif responsible for interaction with UDP-GlcNAc and Mn2+, correction of the mutation by site-directed mutagenesis restores enzyme activity
C121A
-
active mutant enzyme. After 1 h, the wild-type MBP-hGnT1(D103) and C121A mutant convert more than 50% of Man5-RNAse B to RNAse B-GlcNAc2-Man5-GlcNAc
C121D
-
mutant enzyme shows no transfer of GlcNAc from UDP-GlcNAc to the glycoprotein acceptor Man5-RNAse B
C121S
-
active mutant enzyme. After 1 h, the C121S mutant shows less than 25% conversion of Man5-RNAse B to RNAse B-GlcNAc2-Man5-GlcNAc
C121T
-
mutant enzyme shows no transfer of GlcNAc from UDP-GlcNAc to the glycoprotein acceptor Man5-RNAse B
D77N
-
exchange mutation in chimera TfR/GnT1myc, no effect on Golgi localization and inclusion into high molecular weight complexes, no catalytic activity
R120A/C121H
-
active mutant enzyme. The R120A/C121H mutant is less active than the wild type and the single mutants. It converts more than half of the Man5-RNAse B to RNAse B-GlcNAc2-Man5-GlcNAc
R83S
-
exchange mutation in chimera TfR/GnT1myc, no effect on Golgi localization and inclusion into high molecular weight complexes, no catalytic activity
R85S
-
exchange mutation in chimera TfR/GnT1myc, no effect on Golgi localization and inclusion into high molecular weight complexes, no catalytic activity
D144N
-
expression of D144N muatant enzyme of rabbit in cgl mutant of Arabidopsis thaliana lacking GnTI activity (caused by a D144N mutation in GnTI) can partially restore complex N-glycan formation
D291N
-
inactive
more.
-
deleting seven C-terminal amino acids of the enzyme reduces enzymatic activity by 40%
P138L
-
inactive
R415K
-
inactive
C123R
-
mutant enzyme does not show any activity in an HPLC analysis
G320D
-
mutant enzyme does not show any activity in an HPLC analysis. In the case of pig cell transfectants with pigGnT-I(320), cell surface carbohydrate structures are significantly altered and its antigenicity to human serum is reduced
T223A
-
isozyme B, improvement of properties of isozyme B to the level of isozyme A
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
medicine
-
mutant enzyme does not show any activity in an HPLC analysis. In the case of pig cell transfectants with pigGnT-I(320), cell surface carbohydrate structures are significantly altered and its antigenicity to human serum is reduced. pigGnT-I(320) appears to be potentially useful in xenotransplantation by remodeling the carbohydrate structures on pig cells
molecular biology
-
production of rare hybrid oligosaccharides for biochemical and structural studies, 100% conversion of oligosaccharide substrate at room temperature, yield of 42% after purification from reaction mixture