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Information on EC 2.4.1.101 - alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
for references in articles please use BRENDA:EC2.4.1.101
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EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.101 alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
IUBMB Comments
The enzyme, found in plants and animals, participates in the processing of N-glycans in the Golgi apparatus. Its action is required before the other N-acetylglucosaminyltransferases involved in the process (GlcNAcT-II through VI) can act. While the natural substrate (produced by EC 3.2.1.113, mannosyl-oligosaccharide 1,2-α-mannosidase) is described here, the minimal substrate recognized by the enzyme is α-D-Man-(1→3)-β-D-Man-R.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 2.4.1.101
- n-glycans
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n-linked
- glycosyltransferases
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mannosidase
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oligomannose
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high-mannose
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complex-type
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paucimannose
- swainsonine
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golgi-resident
- beta-1,4-galactosyltransferase
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paucimannosidic
- man3glcnac2
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medial-golgi
- glcnacman5glcnac2
- biotechnology
- medicine
- molecular biology
Synonyms
n-acetylglucosaminyltransferase i, glcnac-ti, gnt i, gnt-i, gly-13, gly-12, glcnac transferase i, glcnac-t i, gly-14, glcnact-i, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylglucosaminyltransferase, uridine diphosphoacetylglucosamine-alpha-1,3-mannosylglycoprotein beta-1,2-N-
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alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase
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AtGnTI
ChGnTI
EC 2.4.1.51
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formerly, part transferred
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GlcNAc-T I
gly-12
GLY-13
gly-14
GnT I
GnT-I
GnTI
MGAT1
N-acetylglucosaminyltransferase I
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I
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TbGnTI
UDP-GlcNAc:alpha3-D-mannoside beta1,2-N-acetylglucosaminyltransferase
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UDP-GlcNAc:alpha3-D-mannoside beta1,2-N-acetylglucosaminyltransferase I
UDP-GlcNac:alpha3-D-mannoside beta1,2-Nacetylglucosaminyltransferase I
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UDP-GlcNAc:alpha3-D-mannoside beta1-2-N-acetylglucosaminyltransferase I
UDP-N-acetyl-D-glucosamine:glycoprotein (N-acetyl-D-glucosamine to alpha-D-mannosyl-1,3-(R1)-beta-D-mannosyl-R2) beta-1,2-N-acetyl-D-glucosaminyltransferase
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UDP-N-acetylglucosamine:alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I
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UDP-N-acetylglucosaminyl:alpha-1,3-D-mannoside-beta-1,2-N-acetylglucosaminyltransferase I
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UDP-N-acetylglucosaminyl:alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I
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UDP-N-GlcNAc:alpha3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I
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uridine diphosphoacetylglucosamine-alpha-1,3-mannosylglycoprotein beta-1,2-N-acetylglucosaminyltransferase
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N-acetylglucosaminyltransferase I
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UDP-GlcNAc:alpha3-D-mannoside beta1,2-N-acetylglucosaminyltransferase I
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UDP-GlcNAc:alpha3-D-mannoside beta1,2-N-acetylglucosaminyltransferase I
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UDP-GlcNAc:alpha3-D-mannoside beta1-2-N-acetylglucosaminyltransferase I
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UDP-GlcNAc:alpha3-D-mannoside beta1-2-N-acetylglucosaminyltransferase I
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-glucosamine + Man5GlcNAc2-[protein] = UDP + Man5GlcNAc3-[protein]
mechanism
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UDP-N-acetyl-alpha-D-glucosamine + Man5GlcNAc2-[protein] = UDP + Man5GlcNAc3-[protein]
active site
UDP-N-acetyl-alpha-D-glucosamine + Man5GlcNAc2-[protein] = UDP + Man5GlcNAc3-[protein]
active site
UDP-N-acetyl-alpha-D-glucosamine + Man5GlcNAc2-[protein] = UDP + Man5GlcNAc3-[protein]
R represents the reminder of the N-linked oligosaccharide in the glycoprotein acceptor. Note that this enzyme acts before N-acetylglucosaminyltransferase II, III, IV, V and VI.
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UDP-N-acetyl-alpha-D-glucosamine + Man5GlcNAc2-[protein] = UDP + Man5GlcNAc3-[protein]
ordered sequential bi bi mechanism
UDP-N-acetyl-alpha-D-glucosamine + Man5GlcNAc2-[protein] = UDP + Man5GlcNAc3-[protein]
R303 is important for enzyme activity, conserved throughout all species
UDP-N-acetyl-alpha-D-glucosamine + Man5GlcNAc2-[protein] = UDP + Man5GlcNAc3-[protein]
SGC domain of SGC superfamily
UDP-N-acetyl-alpha-D-glucosamine + Man5GlcNAc2-[protein] = UDP + Man5GlcNAc3-[protein]
DxD motif
UDP-N-acetyl-alpha-D-glucosamine + Man5GlcNAc2-[protein] = UDP + Man5GlcNAc3-[protein]
D212 is the central residue of the DxD motif, conserved throughout all species
UDP-N-acetyl-alpha-D-glucosamine + Man5GlcNAc2-[protein] = UDP + Man5GlcNAc3-[protein]
modeling study provides detailed insight into the mechanism of the GlcNAc transfer
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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PATHWAY SOURCE
PATHWAYS
MetaCyc
complex N-linked glycan biosynthesis (plants), complex N-linked glycan biosynthesis (vertebrates)
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-alpha-D-glucosamine:alpha-D-mannosyl-(1->3)-beta-D-mannosyl-glycoprotein 2-beta-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
The enzyme, found in plants and animals, participates in the processing of N-glycans in the Golgi apparatus. Its action is required before the other N-acetylglucosaminyltransferases involved in the process (GlcNAcT-II through VI) can act. While the natural substrate (produced by EC 3.2.1.113, mannosyl-oligosaccharide 1,2-alpha-mannosidase) is described here, the minimal substrate recognized by the enzyme is alpha-D-Man-(1->3)-beta-D-Man-R.
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CAS REGISTRY NUMBER
COMMENTARY
102576-81-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP + 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
?
UDP + alpha-D-mannosyl-1,3-(alpha-D-mannosyl-1,6)-alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosamine-1,4-N-acetyl-D-glucosamine
?
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Substrates: -
Products: -
Products: -
?
UDP + alpha-D-mannosyl-1,3-(alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-D-glucosamine
?
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Substrates: -
Products: -
Products: -
?
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-pyridinylamine
?
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Substrates: -
Products: -
Products: -
?
UDP + [Manalpha6(Manalpha3)Manalpha6][Manalpha3]Man-beta4-N-acetyl-D-glucosamine-beta4-N-acetyl-D-glucosamine-Asn
?
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Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + 2-deoxy-Manalpha6(Manalpha3)Man-beta-octyl
UDP + ?
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Substrates: -
Products: -
Products: -
?
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
UDP-N-acetyl-D-glucosamine + 3-O-(4,4-azopentyl)-Manalpha6(Manalpha3)Man-beta-octyl
UDP + ?
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Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + 3-O-(4,5-epoxypentyl)-Manalpha6(Manalpha3)Man-beta-octyl
UDP + ?
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Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + 3-O-(5-iodoacetamidopentyl)-Manalpha6(Manalpha3)Man-beta-octyl
UDP + ?
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Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + 3-O-pentyl-Manalpha6(Manalpha3)Man-beta-octyl
UDP + ?
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Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + 4-O-methyl-Manalpha6(Manalpha3)Man-beta-octyl
UDP + ?
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Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + 6-O-methyl-Manalpha6(Manalpha3)Man-beta-octyl
UDP + ?
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Substrates: -
Products: -
Products: -
?
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
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
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
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
UDP-N-acetyl-D-glucosamine + asialofetuin
?
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Substrates: beta-galactosidase-, beta-N-acetylhexosamidase- and alpha-mannosidase-treated asialofetuin, beta-galactosidase- and beta-N-acetylhexosamidase-treated asialofetuin
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + beta-galactosidase- and beta-N-acetylhexosamidase-treated asialotransferrin
?
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Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + dehexoso-orosomucoid
?
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Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + desialo-degalacto-dehexosamine-orosomucoid
?
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Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + fowl plague virus hemagglutinin
UDP + fowl plague virus hemagglutinin with terminal N-acetyl-D-glucosaminyl residues
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Substrates: recombinant coexpression of enzyme and substrate in SF9 insect cells
Products: -
Products: -
?
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
Substrates: 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
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + GlcUAcbeta1-3Galbeta1-O-naphthalenemethanol
?
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Substrates: synthetic substrate
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + glycopeptides prepared from porcine IgC
?
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Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + Man3Man-O-beta4-N-acetyl-D-glucosamine
UDP + ?
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Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + Man5-RNAse B
UDP + RNAse B-GlcNAc2-Man5-GlcNAc
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Substrates: 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
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + Man5GlcNAc2-glycopeptide
UDP + GlcNAc(1-2)Man5GlcNAc2-glycopeptide
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
Substrates: 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
Products: -
Products: -
?
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
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
Substrates: 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
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + Manalpha(1-6)Man
UDP + ?
-
Substrates: -
Products: -
Products: -
?
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
Substrates: 100% activity
Products: -
Products: -
?
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
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
Substrates: 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
Products: -
Products: -
?
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
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
Substrates: 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
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + Manalpha6(4-deoxy-Manalpha3)Man-beta-octyl
UDP + ?
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + Manalpha6(4-O-(5-iodoacetamidopentyl)-Manalpha3)Man-beta-octyl
UDP + ?
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + Manalpha6(4-O-methyl-Manalpha3)Man-beta-octyl
UDP + ?
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + Manalpha6(Manalpha3)Man-O-beta hexyl
UDP + ?
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + Manalpha6(Manalpha3)Man-O-beta(8-methoxycarbonyl)octyl
UDP + ?
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + Manalpha6(Manalpha3)Man-O-beta-octyl
UDP + ?
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + Manalpha6(Manalpha3)Man-O-beta4-N-acetyl-D-glucosamine
UDP + ?
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + Manalpha6(Manalpha3)Man-O-beta4-N-acetyl-D-glucosamine-beta4(L-fucose-alpha6)-N-acetyl-D-glucosamine-Asn
UDP + ?
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + Manalpha6(Manalpha3)Man-O-beta4-N-acetyl-D-glucosamine-beta4-N-acetyl-D-glucosamine
UDP + ?
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosamine-beta2-Manalpha6(Manalpha3)Man-beta4-N-acetyl-D-glucosamine
UDP + ?
-
Substrates: -
Products: -
Products: -
?
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
UDP-N-acetyl-D-glucosamine + ovalbumin glycopeptide III A-C
?
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + ovalbumin glycopeptide IV
?
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + R-Manalpha6(Manalpha3)Man-beta-octyl
UDP + ?
-
Substrates: -
Products: -
Products: -
?
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 + ?
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + [Manalpha1,6(Manalpha1,3)Manalpha1,6](Manalpha1,3)Manbeta1,4GlcAcbeta1,4GlcNAc-R
UDP + ?
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
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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
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Substrates: 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
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Products: -
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UDP + 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
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Substrates: -
Products: -
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UDP + 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
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Substrates: -
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UDP-N-acetyl-alpha-D-glucosamine + Man5GlcNAc2-[protein]
UDP + Man5GlcNAc3-[protein]
Substrates: -
Products: -
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UDP-N-acetyl-alpha-D-glucosamine + Man5GlcNAc2-[protein]
UDP + Man5GlcNAc3-[protein]
Substrates: -
Products: -
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UDP-N-acetyl-alpha-D-glucosamine + Man5GlcNAc2-[protein]
UDP + Man5GlcNAc3-[protein]
Substrates: -
Products: -
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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
Substrates: -
Products: -
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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
Substrates: GlcNAc transfer catalyzed by GnT-I is the first step in the conversion of high mannose oligosaccharides to complex and hybrid N-glycan structures
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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
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Substrates: -
Products: -
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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
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Substrates: -
Products: -
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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
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Substrates: enzyme TbGnTI transfers UDP-GlcNAc to biantennary Man3GlcNAc2, but not to triantennary Man5GlcNAc2, which is the preferred substrate for metazoan enzymes
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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
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Substrates: -
Products: -
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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
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Substrates: enzyme TbGnTI transfers UDP-GlcNAc to biantennary Man3GlcNAc2, but not to triantennary Man5GlcNAc2, which is the preferred substrate for metazoan enzymes
Products: -
Products: -
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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
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Substrates: pyridylamine
Products: R: pyridylamine
Products: R: pyridylamine
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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
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Substrates: R: H
Products: -
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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
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Substrates: 1,4-N-acetyl-D-glucosaminyl-R
Products: -
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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
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Substrates: 1,4-N-acetyl-D-glucosaminyl-R
Products: -
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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
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Substrates: 1,4-N-acetyl-D-glucosaminyl-R
Products: -
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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
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Substrates: R: H
Products: R: H
Products: R: H
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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
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Substrates: 1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: H
Products: R: H
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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
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Substrates: 1,4-N-acetyl-D-glucosaminyl-R
Products: -
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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
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Substrates: synthetic-beta-D-mannosyl-(1,6-anhydro)-derivative acts as substrate, too
Products: R: H
Products: R: H
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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
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Substrates: pyridylamine
Products: R: pyridylamine
Products: R: pyridylamine
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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
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Substrates: no activity with pyridylaminated substrate
Products: -
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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
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Substrates: R: H
Products: -
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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
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Substrates: 1,4-N-acetyl-D-glucosaminyl-R
Products: -
Products: -
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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
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Substrates: recombinant isozyme A and B mutant T223A
Products: -
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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
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Substrates: pyridylamine
Products: -
Products: -
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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
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Substrates: -
Products: -
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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
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Substrates: -
Products: -
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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
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Substrates: -
Products: -
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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
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Substrates: stimulates galactosyltransferase of bovine milk
Products: -
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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
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Substrates: -
Products: -
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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
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Substrates: key enzyme of biosynthesis of complex and hybrid N-glycans
Products: -
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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
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Substrates: key enzyme of biosynthesis of complex and hybrid N-glycans
Products: -
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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
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Substrates: -
Products: -
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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
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Substrates: key enzyme of biosynthesis of complex and hybrid N-glycans
Products: -
Products: -
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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
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Substrates: key enzyme of biosynthesis of complex and hybrid N-glycans
Products: -
Products: -
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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
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Substrates: R: pyridinylamine
Products: pyridinylamine
Products: pyridinylamine
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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
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Substrates: -
Products: -
Products: -
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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
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Substrates: R: H
Products: R: H
Products: R: H
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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
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Substrates: R: H
Products: R: (fucose-1,6)-1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: (fucose-1,6)-1,4-N-acetyl-D-glucosaminyl-Asn
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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
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Substrates: R: H
Products: R: 1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: 1,4-N-acetyl-D-glucosaminyl-Asn
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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
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Substrates: R: 4-N-acetyl-D-glucosaminyl-Asn-peptide
Products: R: H
Products: R: H
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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
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Substrates: R: 4-N-acetyl-D-glucosaminyl-Asn-peptide
Products: R: (fucose-1,6)-1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: (fucose-1,6)-1,4-N-acetyl-D-glucosaminyl-Asn
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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
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Substrates: R: 4-N-acetyl-D-glucosaminyl-Asn-peptide
Products: R: 1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: 1,4-N-acetyl-D-glucosaminyl-Asn
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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
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Substrates: can act on alpha-mannosyl-1,6-beta-mannosyl-terminus if alpha-mannosyl-1,3-beta-mannosyl-terminus is not available, appreciable higher Km-value
Products: R: H
Products: R: H
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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
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Substrates: can act on alpha-mannosyl-1,6-beta-mannosyl-terminus if alpha-mannosyl-1,3-beta-mannosyl-terminus is not available, appreciable higher Km-value
Products: R: (fucose-1,6)-1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: (fucose-1,6)-1,4-N-acetyl-D-glucosaminyl-Asn
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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
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Substrates: can act on alpha-mannosyl-1,6-beta-mannosyl-terminus if alpha-mannosyl-1,3-beta-mannosyl-terminus is not available, appreciable higher Km-value
Products: R: 1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: 1,4-N-acetyl-D-glucosaminyl-Asn
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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
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Substrates: does not act on alpha-mannosyl-1,2-alpha-mannosyl-, alpha-mannosyl-1,3-alpha-mannosyl-, alpha-mannosyl-1,6-alpha-mannosyl-termini
Products: R: H
Products: R: H
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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
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Substrates: does not act on alpha-mannosyl-1,2-alpha-mannosyl-, alpha-mannosyl-1,3-alpha-mannosyl-, alpha-mannosyl-1,6-alpha-mannosyl-termini
Products: R: (fucose-1,6)-1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: (fucose-1,6)-1,4-N-acetyl-D-glucosaminyl-Asn
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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
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Substrates: does not act on alpha-mannosyl-1,2-alpha-mannosyl-, alpha-mannosyl-1,3-alpha-mannosyl-, alpha-mannosyl-1,6-alpha-mannosyl-termini
Products: R: 1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: 1,4-N-acetyl-D-glucosaminyl-Asn
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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
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Substrates: R: (fucose-1,6)-1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: H
Products: R: H
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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
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Substrates: R: (fucose-1,6)-1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: (fucose-1,6)-1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: (fucose-1,6)-1,4-N-acetyl-D-glucosaminyl-Asn
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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
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Substrates: R: (fucose-1,6)-1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: 1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: 1,4-N-acetyl-D-glucosaminyl-Asn
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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
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Substrates: R: 1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: H
Products: R: H
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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
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Substrates: R: 1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: (fucose-1,6)-1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: (fucose-1,6)-1,4-N-acetyl-D-glucosaminyl-Asn
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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
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Substrates: R: 1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: 1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: 1,4-N-acetyl-D-glucosaminyl-Asn
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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
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Substrates: -
Products: -
Products: -
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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
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Substrates: -
Products: -
Products: -
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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
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Substrates: -
Products: -
Products: -
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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
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Substrates: -
Products: transfers an N-acetylglucosamine in beta-1,2-linkage to mannosyl-1,3-beta-mannosyl-terminus
Products: transfers an N-acetylglucosamine in beta-1,2-linkage to mannosyl-1,3-beta-mannosyl-terminus
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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
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Substrates: substrate specificity
Products: -
Products: -
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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
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Substrates: substrate specificity
Products: -
Products: -
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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
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Substrates: substrate specificity
Products: R: H
Products: R: H
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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
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Substrates: substrate specificity
Products: R: 1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: 1,4-N-acetyl-D-glucosaminyl-Asn
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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
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Substrates: R: H
Products: R: H
Products: R: H
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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
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Substrates: essential for activity: unsubstituted equatorial hydroxyl on C-4 of beta-linked mannosyl-residue
Products: R: 1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: 1,4-N-acetyl-D-glucosaminyl-Asn
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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
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Substrates: R: 1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: 1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: 1,4-N-acetyl-D-glucosaminyl-Asn
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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
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Substrates: -
Products: -
Products: -
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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
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Substrates: substrate specificity
Products: R: 1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: 1,4-N-acetyl-D-glucosaminyl-Asn
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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
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Substrates: substrate specificity
Products: transfers an N-acetylglucosamine in beta-1,2-linkage to mannosyl-1,3-beta-mannosyl-terminus
Products: transfers an N-acetylglucosamine in beta-1,2-linkage to mannosyl-1,3-beta-mannosyl-terminus
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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
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Substrates: pyridylaminated oligosaccharide
Products: -
Products: -
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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
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Substrates: essential for activity: unsubstituted equatorial hydroxyl on C-4 of beta-linked mannosyl-residue
Products: R: 1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: 1,4-N-acetyl-D-glucosaminyl-Asn
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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
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Substrates: essential for activity: unsubstituted equatorial hydroxyl on C-4 of beta-linked mannosyl-residue
Products: transfers an N-acetylglucosamine in beta-1,2-linkage to mannosyl-1,3-beta-mannosyl-terminus
Products: transfers an N-acetylglucosamine in beta-1,2-linkage to mannosyl-1,3-beta-mannosyl-terminus
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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
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Substrates: R: pyridinylamine
Products: -
Products: -
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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
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Substrates: R: 1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: 1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: 1,4-N-acetyl-D-glucosaminyl-Asn
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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
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Substrates: R: 1,4-N-acetyl-D-glucosaminyl-Asn
Products: transfers an N-acetylglucosamine in beta-1,2-linkage to mannosyl-1,3-beta-mannosyl-terminus
Products: transfers an N-acetylglucosamine in beta-1,2-linkage to mannosyl-1,3-beta-mannosyl-terminus
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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
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Substrates: R: 1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: 1,4-N-acetyl-D-glucosaminyl-1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: 1,4-N-acetyl-D-glucosaminyl-1,4-N-acetyl-D-glucosaminyl-Asn
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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
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Substrates: an axial 2-hydroxyl group on the beta-linked mannose of the substrate are essential for the enzyme
Products: R: 1,4-N-acetyl-D-glucosaminyl-Asn
Products: R: 1,4-N-acetyl-D-glucosaminyl-Asn
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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
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Substrates: an axial 2-hydroxyl group on the beta-linked mannose of the substrate are essential for the enzyme
Products: transfers an N-acetylglucosamine in beta-1,2-linkage to mannosyl-1,3-beta-mannosyl-terminus
Products: transfers an N-acetylglucosamine in beta-1,2-linkage to mannosyl-1,3-beta-mannosyl-terminus
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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
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Substrates: substrate specificity
Products: -
Products: -
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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
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Substrates: substrate specificity
Products: transfers an N-acetylglucosamine in beta-1,2-linkage to mannosyl-1,3-beta-mannosyl-terminus
Products: transfers an N-acetylglucosamine in beta-1,2-linkage to mannosyl-1,3-beta-mannosyl-terminus
?
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
-
Substrates: R: H
Products: R: H
Products: R: H
?
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
-
Substrates: absolute specificity for terminal branched mannosyl residues
Products: transfers an N-acetylglucosamine in beta-1,2-linkage to mannosyl-1,3-beta-mannosyl-terminus
Products: transfers an N-acetylglucosamine in beta-1,2-linkage to mannosyl-1,3-beta-mannosyl-terminus
?
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
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + Man5GlcNAc2
?
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + Man5GlcNAc2
?
-
Substrates: best substrate
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + Man5GlcNAc2-glycopeptide
UDP + GlcNAc(1-2)Man5GlcNAc2-glycopeptide
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + Man5GlcNAc2-glycopeptide
UDP + GlcNAc(1-2)Man5GlcNAc2-glycopeptide
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + Manalpha(1-3)Man
UDP + ?
-
Substrates: about 15% of the activity with Manalpha(1-3)Manalpha(1-6)Man
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + Manalpha(1-3)Man
UDP + ?
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + Manalpha(1-3)Manalpha(1-6)Man
UDP + ?
-
Substrates: about 30% of the activity with alpha1,3alpha1,6 mannopentaose
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + Manalpha(1-3)Manalpha(1-6)Man
UDP + ?
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: poor substrate
Products: -
Products: -
?
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
-
Substrates: no activity
Products: -
Products: -
?
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
-
Substrates: no activity
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + ovalbumin
?
-
Substrates: best substrate, recombinant enzyme expressed in SF9 cells, unmodified and as tagged fusion protein
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + ovalbumin
?
-
Substrates: substrate: glycopeptides prepared from ovalbumin
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + ovalbumin glycopeptide V
UDP + ovalbumin glycopeptide IIIA
-
Substrates: best substrate
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + ovalbumin glycopeptide V
UDP + ovalbumin glycopeptide IIIA
-
Substrates: physiological substrate
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + ovalbumin glycopeptide V
UDP + ovalbumin glycopeptide IIIA
-
Substrates: best substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essential for processing of high-mannose to hybrid and complex N-glycans
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the first step in the conversion of oligomannose to complex or hybrid N-glycans of glycoproteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with alpha1,6-mannobiose
Products: -
Products: -
?
additional information
?
-
-
Substrates: the GnT I activity in the bovine oviduct may contribute to the induction of glycosylation and thereby contributing to the provision of the optimal microenvironment for fertilization and early development of embryos. Endocrine as well as local factors such as luteinizing hormone, vascular endothelial growth factor and tumor necrosis factor alpha increase the activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: GLY-13 plays an important role in the synthesis of N-glycans. Synthesis of paucimannose N-glycans by Caenorhabditis elegans requires prior actions of UDP-N-acetyl-D-glucosamine:alpha-3-D-mannoside beta1,2-N-acetylglucosaminyltransferase I, alpha3,6-mannosidase II and a specific membrane-bound beta-N-acetylglucosaminidase
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme initiates the biosynthesis of heparan sulfate
Products: -
Products: -
?
additional information
?
-
-
Substrates: transformant plants that exhibit specific reduction of GnTI activity below detection limit, do not exhibit significantly altered complex N-glycan structures. Even the undetectable residual GnTI activity is sufficient for the synthesis of complex N-glycans comparable to wild-type plants
Products: -
Products: -
?
additional information
?
-
-
Substrates: acts on synthetic substrate analogues
Products: -
Products: -
?
additional information
?
-
-
Substrates: no acceptor substrates are N-acetyl-D-glucosamine, 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-acetyl-D-glucosaminyl-1,4-N-acetyl-D-glucosaminyl-Asn
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essential for processing of high-mannose to hybrid and complex N-glycans
Products: -
Products: -
?
additional information
?
-
Substrates: high-level nonempirical calculations describe the mechanism, reaction pathway energetics, and structure of the transition state involved in the reaction catalyzed by GnT-I
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrates: dolichol phosphate, asialo-bovine submaxillary mucin or galactosylated asialo-bovine submaxillary mucin, different specificities of transferase A and B, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrates: free and protein-matrix-bound glycans
Products: -
Products: -
?
additional information
?
-
-
Substrates: specificity for several synthetic acceptor substrate analogues, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the first step in the conversion of oligomannose to complex or hybrid N-glycans of glycoproteins
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
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
UDP-N-acetyl-D-glucosamine + ovalbumin glycopeptide V
UDP + ovalbumin glycopeptide IIIA
-
Substrates: physiological substrate
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-glucosamine + Man5GlcNAc2-[protein]
UDP + Man5GlcNAc3-[protein]
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-glucosamine + Man5GlcNAc2-[protein]
UDP + Man5GlcNAc3-[protein]
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-glucosamine + Man5GlcNAc2-[protein]
UDP + Man5GlcNAc3-[protein]
Substrates: -
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
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
Substrates: GlcNAc transfer catalyzed by GnT-I is the first step in the conversion of high mannose oligosaccharides to complex and hybrid N-glycan structures
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: stimulates galactosyltransferase of bovine milk
Products: -
Products: -
?
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
-
Substrates: key enzyme of biosynthesis of complex and hybrid N-glycans
Products: -
Products: -
?
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
-
Substrates: key enzyme of biosynthesis of complex and hybrid N-glycans
Products: -
Products: -
?
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
-
Substrates: key enzyme of biosynthesis of complex and hybrid N-glycans
Products: -
Products: -
?
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
-
Substrates: key enzyme of biosynthesis of complex and hybrid N-glycans
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essential for processing of high-mannose to hybrid and complex N-glycans
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the first step in the conversion of oligomannose to complex or hybrid N-glycans of glycoproteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: GLY-13 plays an important role in the synthesis of N-glycans. Synthesis of paucimannose N-glycans by Caenorhabditis elegans requires prior actions of UDP-N-acetyl-D-glucosamine:alpha-3-D-mannoside beta1,2-N-acetylglucosaminyltransferase I, alpha3,6-mannosidase II and a specific membrane-bound beta-N-acetylglucosaminidase
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme initiates the biosynthesis of heparan sulfate
Products: -
Products: -
?
additional information
?
-
-
Substrates: transformant plants that exhibit specific reduction of GnTI activity below detection limit, do not exhibit significantly altered complex N-glycan structures. Even the undetectable residual GnTI activity is sufficient for the synthesis of complex N-glycans comparable to wild-type plants
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essential for processing of high-mannose to hybrid and complex N-glycans
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the first step in the conversion of oligomannose to complex or hybrid N-glycans of glycoproteins
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
Ca2+
Cd2+
Co2+
Fe2+
Mg2+
Mn2+
Ni2+
Zn2+
additional information
Ca2+
-
the enzyme in testicular fluid has an absolute requirement for either Co2+, or Mn2+, Mg2+ and ca2+. The activity is stimulated by the cations in the above order. The enzyme from cauda epididymal fluid has an absolute requirement for Mn2+ or Ca2+, with Co2+ and Mg2+ being ineffective
Co2+
-
the enzyme in testicular fluid has an absolute requirement for either Co2+, or Mn2+, Mg2+ and ca2+. The activity is stimulated by the cations in the above order. The enzyme from cauda epididymal fluid has an absolute requirement for Mn2+ or Ca2+, with Co2+ and Mg2+ being ineffective
Mg2+
-
the enzyme in testicular fluid has an absolute requirement for either Co2+, or Mn2+, Mg2+ and ca2+. The activity is stimulated by the cations in the above order. The enzyme from cauda epididymal fluid has an absolute requirement for Mn2+ or Ca2+, with Co2+ and Mg2+ being ineffective
Mn2+
-
the enzyme in testicular fluid has an absolute requirement for either Co2+, or Mn2+, Mg2+ and ca2+. The activity is stimulated by the cations in the above order. The enzyme from cauda epididymal fluid has an absolute requirement for Mn2+ or Ca2+, with Co2+ and Mg2+ being ineffective
additional information
not stimulated by Mg2+, Co2+, Ca2+, Zn2+ and C2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
-
additional information
-
several inhibitory synthetic acceptor substrate analogues, overview; strategies for inhibitor design based on substrate specificities of the enzyme
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
(n-acetylneuraminyl)-galactosylglucosylceramide n-acetylgalactosaminyltransferase deficiency
Essential roles of carbohydrate signals in development, immune response and tissue functions, as revealed by gene targeting.
alpha-1,3-mannosyl-glycoprotein 2-beta-n-acetylglucosaminyltransferase deficiency
An Arabidopsis thaliana cDNA complements the N-acetylglucosaminyltransferase I deficiency of CHO Lec1 cells.
alpha-1,3-mannosyl-glycoprotein 2-beta-n-acetylglucosaminyltransferase deficiency
Molecular basis of N-acetylglucosaminyltransferase I deficiency in Arabidopsis thaliana plants lacking complex N-glycans.
Carcinoma
Glycosyltransferase expression in human colonic tissue examined by oligonucleotide arrays.
Carcinoma, Hepatocellular
Processing of asparagine-linked oligosaccharides in insect cells. N-acetylglucosaminyltransferase I and II activities in cultured lepidopteran cells.
Glioma
N-acetylglucosaminyltransferase I promotes glioma cell proliferation and migration through increasing the stability of the glucose transporter GLUT1.
Herpes Simplex
N-acetylgalactosaminyltransferase activity involved in O-glycosylation of herpes simplex virus type 1 glycoproteins.
Infections
Blocking cellular N-glycosylation suppresses human cytomegalovirus entry in human fibroblasts.
Infections
Engineering the baculovirus genome to produce galactosylated antibodies in lepidopteran cells.
Infections
Hybrid- and complex-type N-glycans are not essential for Newcastle disease virus infection and fusion of host cells.
Infertility, Male
Essential roles of carbohydrate signals in development, immune response and tissue functions, as revealed by gene targeting.
Influenza, Human
Influenza virus entry and infection require host cell N-linked glycoprotein.
Muscular Dystrophies
The role of the GlcNAc(beta)1,2Man(alpha)- moiety in mammalian development. Null mutations of the genes encoding UDP-N-acetylglucosamine:alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I and UDP-N-acetylglucosamine:alpha-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I.2 cause embryonic lethality and congenital muscular dystrophy in mice and men, respectively.
Neoplasms
N-acetylglucosaminyltransferase I activity of bovine oviduct epithelial cells: stimulation by luteinizing hormone, vascular endothelial growth factor and tumor necrosis factor alpha.
Neoplasms
N-acetylglucosaminyltransferase-I as a novel regulator of epithelial-mesenchymal transition.
Newcastle Disease
Hybrid- and complex-type N-glycans are not essential for Newcastle disease virus infection and fusion of host cells.
Pheochromocytoma
Comparison of the expression of cell surface poly-N-acetyllactosamine-type oligosaccharides in PC12 cells with those in its variant PC12D.
Teratocarcinoma
Cloning and expression of the murine gene and chromosomal location of the human gene encoding N-acetylglucosaminyltransferase I.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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 25°C
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
0.4
[Manalpha6(Manalpha3)Manalpha6][Manalpha3]Man-beta4-N-acetyl-D-glucosamine-beta4-N-acetyl-D-glucosamine-Asn
-
-
0.25
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
-
-
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
-
recombinant catalytic fragment
0.0384
alpha-D-mannosyl-1,3-(alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
-
0.2
alpha-D-mannosyl-1,3-(alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
immunoglobulin G glycopeptide
0.39
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
-
-
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
-
-
0.078
UDP-N-acetyl-D-glucosamine
-
with 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
additional information
additional information
-
Km-values for several synthetic acceptor substrate analogues, overview
-
additional information
additional information
-
interaction with bovine milk galactosyltransferase influences the Km-values
-
additional information
additional information
-
elimination of 4-hydroxyl of the alpha-1,3-linked mannose of the substrate increases the Km-value 20fold
-
additional information
additional information
-
kinetic data of free and protein-matrix-bound acceptor substrates
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
-
-
additional information
additional information
-
several inhibitory synthetic acceptor substrate analogues, overview
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
additional information
-
in vivo assay of recombinant enzyme expressed in Sf9 cells with coexpressed fowl plague virus HA as endogenous substrate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.3
6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 45
the activity decreases with increasing reaction temperature and is completely abolished at temperatures higher than 45°C. On the other hand, substantial GnTI activity is detected at low temperatures, even at 0°C (approximately 50% of the maximum)
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
expressing VSG variant 221 and transformed to stably express T7 polymerase and the tetracycline repressor protein under G418 antibiotic selection, gene TbGT11 or Tb427.3.5660
-
-
brenda
expressing VSG variant 221 and transformed to stably express T7 polymerase and the tetracycline repressor protein under G418 antibiotic selection, gene TbGT11 or Tb427.3.5660
-
-
brenda
a D144N muation in the GnTI of cgl mutant lacking GnTI activity is molecular basis of the defect
-
-
brenda
wild-type and cg/1 plants lacking an own active N-acetylglucosaminyltransferase Is
-
-
brenda
1 difference to published sequence U65791: C1340 is A1340
SwissProt
brenda
expressed in alfalfa together with human beta 1,4-galacosyltransferase
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
two forms of beta 2-N-acetylglucosaminyltransferase I in rat testicular and epididymal fluids
brenda
MGAT1 is highly expressed in glioblastoma tissues
brenda
-
diethylnitrosamine- or dimethylaminoazobenzene-induced hepatoma, Morris 5123D hepatoma or AH-109A, solid or ascitic
brenda
-
no significant difference between the GnT I activities from dominant follicles collected before and after surge of luteinizing hormone
brenda
-
two forms of beta 2-N-acetylglucosaminyltransferase I in rat testicular and cauda epididymal fluids
brenda
wild-type, Lec1 cells are deficient in enzyme activity, mutant Lec1A cells show weak enzyme activity, 2% compared to wild-type, and produce complex N-glycans
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
in recombinant Saccharomyces cerevisisae
brenda
additional information
-
Golgi-localized N-acetylglucosaminyltransferase I is a determinant of osmotic stress tolerance in Arabidopsis thaliana
brenda
-
medial Golgi enzyme, exists as high molecular weight complex, which do not require the transmembrane domain nor the cytoplasmic tail of the enzyme for complex formation
brenda
-
the enzyme is a Golgi-resident type-II membrane protein. The transmembrane domain of enzyme GnTI is the major determinant for its cis/medial-Golgi localization, while the stem region of GnTI contributes predominately to homomeric and heteromeric protein complex formation
brenda
additional information
-
mesophyll protoplasts are created to analyze differences in localization
-
brenda
additional information
-
mammalian Golgi retention signal does not function in Saccharomyces cerevisiae cells
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
sequence alignment reveals that the Trypanosoma brucei enzyme is far removed from the metazoan GnTI family and suggests that the parasite has adapted the beta3-glycosyltransferase family to catalyze beta1-2 linkages. It belongs to a family of putative UDP-sugar-dependent glycosyltransferases with similarity to the mammalian beta1-3-glycosyltransferase family. Enzyme TbGnTI transfers UDP-GlcNAc to biantennary Man3GlcNAc2, but not to triantennary Man5GlcNAc2, which is the preferred substrate for metazoan enzymes
evolution
the modification in the Golgi of N-glycans by N-acetylglucosaminyltransferase I (GlcNAc-TI, MGAT1) can be considered to be a hallmark of multicellular eukaryotes as it is found in all metazoans and plants, but rarely in unicellular organisms
evolution
-
sequence alignment reveals that the Trypanosoma brucei enzyme is far removed from the metazoan GnTI family and suggests that the parasite has adapted the beta3-glycosyltransferase family to catalyze beta1-2 linkages. It belongs to a family of putative UDP-sugar-dependent glycosyltransferases with similarity to the mammalian beta1-3-glycosyltransferase family. Enzyme TbGnTI transfers UDP-GlcNAc to biantennary Man3GlcNAc2, but not to triantennary Man5GlcNAc2, which is the preferred substrate for metazoan enzymes
-
malfunction
-
Mgat1-null flies are viable but exhibit pronounced defects in locomotion. Neuron-specific RNAi knockdown of Mgat1 in wild-type flies results in locomotory defects, reduced life span, and about 50% reduction in enzyme activity
malfunction
-
modulating N-acetylglucosaminyltransferase I activity in cells can influence antibody effector functions
malfunction
-
worms with either deletion or RNA-mediated down-regulation of the gly-14 gene are completely resistant to killing by bacteria on PGS medium
malfunction
-
the bloodstream-form TbGT11 null mutant exhibits significantly modified protein N-glycans but normal growth in vitro and infectivity to rodents
malfunction
downregulation of MGAT1 inhibits glioma cell proliferation and migration, overview. Glut1 protein expression is significantly decreased in MGAT1 knockdown cells, but there is no significant change in Glut3. Activation of EGFR signalling by HB-EGF can rescue the inhibitory effects of MGAT1 knockdown on the expression of Glut1, but downregulation of MGAT1 does not significantly change the level of Glut1 mRNA. Downregulation of MGAT1 decreases the complex N-glycan of Glut1. Ectopic expression of Glut1 rescues the inhibitory effects of MGAT1 knockdown on glioma cell proliferation and migration
malfunction
enzyme-deficient Chlamydomonas reinhardtii cells expressing eukaryotic GnTI from Arabidopsis thaliana exhibit an altered phenotype with large vacuoles, increase of ROS production and accumulation of starch granules, suggesting the activation of stress responses likely due to the perturbation of the Golgi apparatus
malfunction
enzyme-deficient Chlamydomonas reinhardtii cells expressing eukaryotic GnTI from Phaeodactylum tricornutum exhibit an altered phenotype with large vacuoles, increase of ROS production and accumulation of starch granules, suggesting the activation of stress responses likely due to the perturbation of the Golgi apparatus
malfunction
-
the bloodstream-form TbGT11 null mutant exhibits significantly modified protein N-glycans but normal growth in vitro and infectivity to rodents
-
metabolism
-
the enzyme controls the synthesis of paucimannose N-glycans
metabolism
the enzyme is involved in the N-glycan-branching pathway, overview. Regulation of cellular metabolite levels by Mgat1, overview
metabolism
-
the first step in hybrid and complex N-glycan biosynthesis is initiated by N-acetylglucosaminyltransferase I (GnTI) through the addition of an N-acetylglucosamine (GlcNAc) residue to the alpha1-3-linked core mannose of Man5GlcNAc2
metabolism
eukaryotic N-glycosylation pathways are dependent of N-acetylglucosaminyltransferase I (GnTI), a key glycosyltransferase opening the door to the formation of complex-type N-glycans by transferring a N-acetylglucosamine residue onto the Man5GlcNAc2 intermediate
metabolism
eukaryotic N-glycosylation pathways are dependent of N-acetylglucosaminyltransferase I (GnTI), a key glycosyltransferase opening the door to the formation of complex-type N-glycans by transferring a N-acetylglucosamine residue onto the Man5GlcNAc2 intermediate
metabolism
the N-glycomic repertoire of Caenorhabditis exhibits a large degree of plasticity even in the absence of key glycan processing enzymes from the Golgi apparatus
metabolism
-
the first step in hybrid and complex N-glycan biosynthesis is initiated by N-acetylglucosaminyltransferase I (GnTI) through the addition of an N-acetylglucosamine (GlcNAc) residue to the alpha1-3-linked core mannose of Man5GlcNAc2
-
physiological function
-
enzyme-dependent N-glycans are essential for cell-cell and cell-matrix interactions
physiological function
-
Mgat1-dependent N-glycans are required for normal development
physiological function
-
Mgat1-dependent N-glycans are required for normal development
physiological function
-
Mgat1-dependent N-glycans are required for normal development
physiological function
-
in contrast to multicellular organisms, where the enzyme activity is essential for biosynthesis of both complex and hybrid N-glycans, Trypanosoma brucei TbGT11 null mutants produce atypical pseudohybrid glycans, indicating that the enzyme activity is not dependent on prior TbGnTI action. The enzyme GnTI reaction is essential for biosynthesis of both complex and hybridN-glycans. TbGnTII activity is not dependent on prior TbGnTI action
physiological function
AtGnTI (At4g38240) encodes for a Golgi enzyme that is responsible for the transfer of a terminal GlcNAc residue onto Man5GlcNAc2 N-glycan
physiological function
N-acetylglucosaminyltransferase I (MGAT1) is responsible for the conversion of high-mannose to hybrid and complex N-glycans. It promotes glioma cell proliferation and migration through increasing the stability of the glucose transporter GLUT1, MGAT1 interacted with Glut1 in U-87/MG cells, mechanism of MGAT1 promoting glioma cell proliferation, overview. MGAT1 regulates Glut1 N-glycosylation
physiological function
PtGnTI restores in vivo the biosynthesis of complex-type N-glycans in CHO Lec1 mutant that lacks endogenous GnTI activity
physiological function
the modification in the Golgi of N-glycans is catalyzed by N-acetylglucosaminyltransferase I (GlcNAc-TI, MGAT1). The enzyme is key for the normal processing of N-glycans to either complex or paucimannosidic forms, both of which are found in the model nematode Caenorhabditis elegans
physiological function
-
in contrast to multicellular organisms, where the enzyme activity is essential for biosynthesis of both complex and hybrid N-glycans, Trypanosoma brucei TbGT11 null mutants produce atypical pseudohybrid glycans, indicating that the enzyme activity is not dependent on prior TbGnTI action. The enzyme GnTI reaction is essential for biosynthesis of both complex and hybridN-glycans. TbGnTII activity is not dependent on prior TbGnTI action
-
additional information
-
steady-state distribution of the enzyme in the cis/medial-Golgi in plants is a prerequisite for efficient N-glycan processing in vivo
additional information
analysis of the diversity of wild-type and mutant Caenorhabditis elegans N-glycomes, profiled by MALDI-TOF MS, overview
additional information
analysis of the diversity of wild-type and mutant Caenorhabditis elegans N-glycomes, profiled by MALDI-TOF MS, overview
additional information
analysis of the diversity of wild-type and mutant Caenorhabditis elegans N-glycomes, profiled by MALDI-TOF MS, overview
additional information
-
analysis of the diversity of wild-type and mutant Caenorhabditis elegans N-glycomes, profiled by MALDI-TOF MS, overview
additional information
Glut1 N-glycan structure is evaluated by N-glycosidase digestion. Glut1 in U87/MG cells is sensitive to PNGase F but resistant to endo H digestion, suggesting that the type of Glut1 N-glycan in U87/MG cells are mainly complex type N-glycan
Show AA Sequence and Transmembrane Helices (2690 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45000
-
x * 45000 + x * 50000 + x * 54000, low molecular weight form, SDS-PAGE, major band: MW 45000
46000
50000
54000
-
x * 45000 + x * 50000 + x * 54000, low molecular weight form, SDS-PAGE, major band: MW 45000
78000
additional information
50000
-
x * 45000 + x * 50000 + x * 54000, low molecular weight form, SDS-PAGE, major band: MW 45000
78000
-
mass of the fusion protein, free YFP-marker is about 27000 Da, SDS-PAGE
additional information
2 domain protein, determination of acceptor substrate-, nucleotide sugar- and metal-binding sites
additional information
-
2 domain protein, determination of acceptor substrate-, nucleotide sugar- and metal-binding sites
additional information
-
two MW-species of pig liver enzyme: major MW 52000 and minor MW 59000, SDS-PAGE
additional information
-
enzyme exists as high molecular weight complex, which do not require the transmembrane domain nor the cytoplasmic tail of the enzyme for complex formation
additional information
-
shorter hydrophobic membrane anchor domain compared to animal enzymes, amino acid sequences alignment
additional information
-
shorter hydrophobic membrane anchor domain compared to animal enzymes, amino acid sequences alignment
additional information
shorter hydrophobic membrane anchor domain compared to animal enzymes, amino acid sequences alignment
additional information
-
shorter hydrophobic membrane anchor domain compared to animal enzymes, amino acid sequences alignment
additional information
-
type II membrane proteins: short N-terminal cytoplasmic tail of 4 amino acid residues, transmembrane domain of 22 residues, stem region of 81 residue for isozyme A and 77 residues for isozyme B, amino acid sequences alignment
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
-
the enzyme has cytoplasmic transmembrane and stem regions. The transmembrane domain of enzyme GnTI is the major determinant for its cis/medial-Golgi localization, while the stem region of GnTI contributes predominately to homomeric and heteromeric protein complex formation
?
-
x * 45000 + x * 50000 + x * 54000, low molecular weight form, SDS-PAGE, major band: MW 45000
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
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
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
more.
-
deleting seven C-terminal amino acids of the enzyme reduces enzymatic activity by 40%
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
additional information
-
natural point mutation contains mRNA but no enzyme activity
additional information
-
AAA, ER steady-state location with little Golgi labelling
additional information
-
Elisa experiments show that cgl1-1 mutant of Arabidopsis lacking N-acetylglucosaminyltransferase I activity, is fully complemented by YFP-labeled Arabidopsis enzyme (similar level of proteins with complex glycans), but only partially complemented by human enzyme (lower levels of proteins with complex glycans), chimeric enzyme with similar levels compared to wild-type, sub-cellular localization of the human enzyme is partly distinct, the human enzyme is easily cleaved of its transmembrane anchor
additional information
-
RAA, localisation in ER and Golgi membrane, more pronounced labeling in the ER
additional information
-
site-directed mutagenesis of single arginine residues within cytoplasmic tail are sufficient to promote rapid Golgi targeting of Golgi-resident N-acetylglucosaminyltransferase I, an intact ER export motif is essential for proper in vivo function, transport is COPII-dependent, exchange of the cytoplasmic tail with the corresponding part of other plant glycosylation enzymes does not alter the Golgi targeting, complementation experiments with cg/1 Arabidopsis thaliana lacking an active N-acetylglucosaminyltransferase I
additional information
eukaryotic N-glycosylation pathways are dependent of N-acetylglucosaminyltransferase I (GnTI), a key glycosyltransferase opening the door to the formation of complex-type N-glycans by transferring a N-acetylglucosamine residue onto the Man5GlcNAc2 intermediate. In contrast, glycans N-linked to Chlamydomonas reinhardtii proteins arise from a GnTI-independent Golgi processing of oligomannosides giving rise to Man5GlcNAc2 substituted eventually with one or two xylose(s). Chlamydomonas reinhardtii proteins carry linear Man5GlcNAc2 instead of the branched structure usually found in eukaryotes. Moreover, characterization of the lipid-linked oligosaccharide precursor demonstrated that Chlamydomonas reinhardtii exhibit a Glc3Man5GlcNAc2 dolichol diphosphate precursor. This precursor is then trimmed into a linear Man5GlcNAc2 that is not substrate for GnTI. Expression of GnTI cDNAs originated from Arabidopsis and the diatom Phaeodactylum tricornutum cause no modification of the N-glycans in the GnTI transformed cells. Cells expressing GnTI exhibit an altered phenotype with large vacuoles, increase of ROS production and accumulation of starch granules, suggesting the activation of stress responses likely due to the perturbation of the Golgi apparatus
additional information
complete abolition of GlcNAc-TI activity requires the generation of a triple knock-out strain, knockoing out the three genes encoding the enzyme, i.e. gly-12, gly-13 and gly-14. The multiple hexose residues of the N-glycans of the gly-12/gly-13/gly-14 triple mutant are not just mannose, but include galactoses in three different positions (beta-intersecting, beta-bisecting and alpha-terminal) on isomeric forms of Hex4-8HexNAc2 structures, some of these structures are fucosylated and/or methylated, determination of the N-glycome of 12/gly-13/gly-14 triple GlcNAc-TI knock-out strain
additional information
complete abolition of GlcNAc-TI activity requires the generation of a triple knock-out strain, knockoing out the three genes encoding the enzyme, i.e. gly-12, gly-13 and gly-14. The multiple hexose residues of the N-glycans of the gly-12/gly-13/gly-14 triple mutant are not just mannose, but include galactoses in three different positions (beta-intersecting, beta-bisecting and alpha-terminal) on isomeric forms of Hex4-8HexNAc2 structures, some of these structures are fucosylated and/or methylated, determination of the N-glycome of 12/gly-13/gly-14 triple GlcNAc-TI knock-out strain
additional information
complete abolition of GlcNAc-TI activity requires the generation of a triple knock-out strain, knockoing out the three genes encoding the enzyme, i.e. gly-12, gly-13 and gly-14. The multiple hexose residues of the N-glycans of the gly-12/gly-13/gly-14 triple mutant are not just mannose, but include galactoses in three different positions (beta-intersecting, beta-bisecting and alpha-terminal) on isomeric forms of Hex4-8HexNAc2 structures, some of these structures are fucosylated and/or methylated, determination of the N-glycome of 12/gly-13/gly-14 triple GlcNAc-TI knock-out strain
additional information
-
complete abolition of GlcNAc-TI activity requires the generation of a triple knock-out strain, knockoing out the three genes encoding the enzyme, i.e. gly-12, gly-13 and gly-14. The multiple hexose residues of the N-glycans of the gly-12/gly-13/gly-14 triple mutant are not just mannose, but include galactoses in three different positions (beta-intersecting, beta-bisecting and alpha-terminal) on isomeric forms of Hex4-8HexNAc2 structures, some of these structures are fucosylated and/or methylated, determination of the N-glycome of 12/gly-13/gly-14 triple GlcNAc-TI knock-out strain
additional information
1 difference to published sequence with accession number U65791: C1340 is A1340
additional information
-
construction of chimeric proteins with different portions of the N-terminal ectodomain of the enzyme, modification to ectodomain of type II surface membrane protein, chimeras are retained in the Golgi apparatus
additional information
-
a truncated, soluble enzyme form, consisting of stem region and catalytic domain, is accumulated in the Golgi apparatus prior to secretion
additional information
-
Elisa experiments show that cgl1-1 mutant of Arabidopsis lacking N-acetylglucosaminyltransferase I activity, is fully complemented by YFP-labeled Arabidopsis enzyme (similar level of proteins with complex glycans), but only partially complemented by human enzyme (lower levels of proteins with complex glycans), chimeric enzyme with similar levels compared to wild-type, sub-cellular localization of the human enzyme is partly distinct, the human enzyme is easily cleaved of its transmembrane anchor
additional information
GlcNAc and tet-induced Mgat1 increases the levels of many metabolites in HeLa cells, and HEK293 cells, tet-induced Mgat1 changes in the N-glycan distributions, , N-glycans profiles of transgenic HeLa and HEK-293 cells, overview
additional information
-
GlcNAc and tet-induced Mgat1 increases the levels of many metabolites in HeLa cells, and HEK293 cells, tet-induced Mgat1 changes in the N-glycan distributions, , N-glycans profiles of transgenic HeLa and HEK-293 cells, overview
additional information
MGAT1 protein and mRNA levels are markedly reduced in cells infected with lentiviral expressing MGAT1 shRNA-1 or MGAT1-shRNA-2. Knockdown of MGAT1 leads to an increase in the G1-phase cells with a decrease in S-phase cells and G2/M-phase cells. Downregulation of MGAT1 significantly inhibits migration of GBM cells
additional information
-
construction of a series of chimeric N-acetylglucosaminyltransferase I (GnTI) mutants by to investigate the contribution of the cytoplasmic, transmembrane, and stem region the enzyme for its cis/medial-Golgi localization and for protein-protein interaction in the Golgi apparatus. The individual GnTI protein domains, i.e. cytoplasmic tail, transmembrane domain and luminal stem region, are replaced with those from the well-known trans-Golgi enzyme alpha2,6-sialyltransferase and transiently expressed in Nicotiana benthamiana. A chimeric GnTI variant with altered sub-Golgi localization is not able to complement the GnTI-dependent glycosylation defect. Generation of transgenic Arabdiopsis thaliana gntI plants expressing the chimeric CTS domai region fused to the catalytic domain of Arabidopsis thaliana GnTI enzyme and expression in enzyme activity-deficient Nicotiana benthamiana plants under control of the endogenous GnTI promoter. The Arabidopsis enzyme chimeric constructs can complement the inactive the N-glycan processing defect of tobacco mutant plants
additional information
-
transient transfection of isolated protoplasts of Arabidopsis thaliana defective mutant with cDNA in sense and antisense orientation
additional information
-
construction of antisense transgenic plants via Agrobacterium tumefaciens transfection of the own gene in antisense orientation, regulation analysis
additional information
-
the fusion of the human beta 1,4-galactosyltransferase with the targeting domain of Nicotiana N-acetylglucosaminyltransferase I does not increase the level of beta 1,4-galactosylation in alfalfa
additional information
eukaryotic N-glycosylation pathways are dependent of N-acetylglucosaminyltransferase I (GnTI), a key glycosyltransferase opening the door to the formation of complex-type N-glycans by transferring a N-acetylglucosamine residue onto the Man5GlcNAc2 intermediate. In contrast, glycans N-linked to Chlamydomonas reinhardtii proteins arise from a GnTI-independent Golgi processing of oligomannosides giving rise to Man5GlcNAc2 substituted eventually with one or two xylose(s). Chlamydomonas reinhardtii proteins carry linear Man5GlcNAc2 instead of the branched structure usually found in eukaryotes. Moreover, characterization of the lipid-linked oligosaccharide precursor demonstrated that Chlamydomonas reinhardtii exhibit a Glc3Man5GlcNAc2 dolichol diphosphate precursor. This precursor is then trimmed into a linear Man5GlcNAc2 that is not substrate for GnTI. Expression of GnTI cDNAs originated from Arabidopsis and the diatom Phaeodactylum tricornutum cause no modification of the N-glycans in the GnTI transformed cells. Cells expressing GnTI exhibit an altered phenotype with large vacuoles, increase of ROS production and accumulation of starch granules, suggesting the activation of stress responses likely due to the perturbation of the Golgi apparatus
additional information
-
eukaryotic N-glycosylation pathways are dependent of N-acetylglucosaminyltransferase I (GnTI), a key glycosyltransferase opening the door to the formation of complex-type N-glycans by transferring a N-acetylglucosamine residue onto the Man5GlcNAc2 intermediate. In contrast, glycans N-linked to Chlamydomonas reinhardtii proteins arise from a GnTI-independent Golgi processing of oligomannosides giving rise to Man5GlcNAc2 substituted eventually with one or two xylose(s). Chlamydomonas reinhardtii proteins carry linear Man5GlcNAc2 instead of the branched structure usually found in eukaryotes. Moreover, characterization of the lipid-linked oligosaccharide precursor demonstrated that Chlamydomonas reinhardtii exhibit a Glc3Man5GlcNAc2 dolichol diphosphate precursor. This precursor is then trimmed into a linear Man5GlcNAc2 that is not substrate for GnTI. Expression of GnTI cDNAs originated from Arabidopsis and the diatom Phaeodactylum tricornutum cause no modification of the N-glycans in the GnTI transformed cells. Cells expressing GnTI exhibit an altered phenotype with large vacuoles, increase of ROS production and accumulation of starch granules, suggesting the activation of stress responses likely due to the perturbation of the Golgi apparatus
additional information
transient transfection of isolated protoplasts of Arabidopsis thaliana defective mutant with cDNA in sense and antisense orientation
additional information
-
transient transfection of isolated protoplasts of Arabidopsis thaliana defective mutant with cDNA in sense and antisense orientation
additional information
construction of antisense transgenic plants via Agrobacterium tumefaciens transfection of the own gene in antisense orientation, regulation analysis
additional information
-
construction of antisense transgenic plants via Agrobacterium tumefaciens transfection of the own gene in antisense orientation, regulation analysis
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 45
the activity is stable after a 2 h incubation at a temperature lower than 25°C, but it significantly decreases after incubation at 35°C and is completely abolished at temperatures higher than 45°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
repeated freeze-thawing, stable to
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 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
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
partial
recombinant glutathione S-transferase fusion isozymes and mutants from insect Sf21 cells
-
two molecular weight forms separable by gel filtration, purification of low-molecular weight form
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
expressed in Chinese hamster ovary Lec1 mutant cells defective in endogeneous N-acetylglucosaminyltransferase I
-
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 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 isozymes A and B in Spodoptera frugiperda Sf21 cells as glutathione-S-transferase fusion proteins via baculovirus infection, isozyme B is folded less efficiently
-
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
-
gene gene TbGT11, DNA and amino acid sequence determination and analysis, gene TbGT11 encodes a Golgi apparatus resident UDP-GlcNAc:alpha3-D-mannoside beta1-2-N-acetylglucosaminyltransferaseI activity (TbGnTI).overexpression of full-length TbGT11 with a C-terminal HA3 epitope tag from a plasmid based on the trypanosome expression vector pLEW82
-
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
-
recombinant nuclear expression of the enzyme sequences fused to a tag sequence encoding for a V5-epitope in Chlamydomonas reinhardtii
recombinant tet-inducible expression of Flag-tagged GlcNAcT-I in HeLa and HEK293 cells
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
-
the organism has three different GlcNAc-TI genes: gly-12, gly-13 and gly-14
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
-
transient expression of chimeric enzyme domain mutants in Nicotiana benthamiana
-
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
-
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
-
recombinant nuclear expression of the enzyme sequences fused to a tag sequence encoding for a V5-epitope in Chlamydomonas reinhardtii
recombinant nuclear expression of the enzyme sequences fused to a tag sequence encoding for a V5-epitope in Chlamydomonas reinhardtii
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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
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
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
biotechnology
-
immobilization of the enzyme as maltose-binding fusion protein on an amylose resin for production of high-mannose type oligosaccharides
biotechnology
-
production of glycoprotein therapeutics in recombinant Saccharomyces cerevisiae adapted to production of hybrid- and complex-type carbohydrates
biotechnology
-
the fusion of the human beta 1,4-galacosyltransferase with the targeting domain of Nicotiana N-acetylglucosaminyltransferase I does not increase the level of beta 1,4-galactosylation in alfalfa, the expression in alfalfa strongly reduces the biosynthesis of Lewis a glycoepitope responsible for plant N-glycan immunogenicity in mammals
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tezuka, K.; Hayashi, M.; Ishihara, H.; Akazawa, T.; Takahashi, N.
Studies on synthetic pathway of xylose-containing N-linked oligosaccharides deduced from substrate specificities of the processing enzymes in sycamore cells (Acer pseudoplatanus L.)
Eur. J. Biochem.
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1992
Acer pseudoplatanus
brenda
Mller, G.; Reck, F.; Paulsen, H.; Kaur, K.J.; Sarkar, M.; Schachter, H.; Brockhausen, I.
Control of glycoprotein synthesis: substrate specificity of rat liver UDP-GlcNAc: Man-alpha-3R-beta-2-N-acetylglucosaminyltransferase I using synthetic substrate analogs
Glycoconj. J.
9
180-190
1992
Rattus norvegicus
brenda
Oppenheimer, C.L.; Hill, R.L.
Purification and characterization of a rabbit liver alpha 1-3 mannoside beta 1-2 N-acetylglucosaminyltransferase
J. Biol. Chem.
256
799-804
1981
Oryctolagus cuniculus
brenda
Mendicino, J.; Chandrasekaran, E.V.; Rao Anumula, K.; Davila, M.
Isolation and properties of alpha-D-mannose: beta-1,2-N-acetylglucosaminyltransferase from trachea mucosa
Biochemistry
20
967-976
1981
Sus scrofa
brenda
Harpaz, N.; Schachter, H.
Control of glycoprotein synthesis. Bovine colostrum UDP-N-acetylglucosamine:alpha-D-mannoside beta 2-N-acetylglucosaminyltransferase I. Separation from UDP-N-acetylglucosamine:alpha-D-mannoside beta 2-N-acetylglucosaminyltransferase II, partial purification, and substrate specificity
J. Biol. Chem.
255
4885-4893
1980
Bos taurus
brenda
Miyagi, T.; Tsuiki, S.
Studies on UDP-N-acetylglucosamine: alpha-mannoside beta-N-acetylglucosaminyltransferase of rat liver and hepatomas
Biochim. Biophys. Acta
661
148-157
1981
Rattus norvegicus
brenda
Oppenheimer, C.L.; Eckhardt, A.E.; Hill, R.L.
The nonidentity of porcine N-acetylglucosaminyltransferases I and II
J. Biol. Chem.
256
11477-11482
1981
Sus scrofa
brenda
Shao, M.C.; Wold, F.
The effect of the protein matrix on glycan processing in glycoproteins. Kinetic analysis of three rat liver Golgi enzymes
J. Biol. Chem.
263
5771-5774
1988
Rattus norvegicus
brenda
Moscarello, M.A.; Mitranic, M.M.; Vella, G.
Stimulation of bovine milk galactosyltransferase activity by bovine colostrum N-acetylglucosaminyltransferase I
Biochim. Biophys. Acta
831
192-200
1985
Bos taurus
brenda
Nishikawa, Y.; Pegg, W.; Paulsen, H.; Schachter, H.
Control of glycoprotein synthesis. Purification and characterization of rabbit liver UDP-N-acetylglucosamine:alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I
J. Biol. Chem.
263
8270-8281
1988
Oryctolagus cuniculus
brenda
Tang, B.L.; Wong, S.H.; Low, S.H.; Hong, W.
The transmembrane domain of N-glucosaminyltransferase I contains a Golgi retention signal
J. Biol. Chem.
267
10122-10126
1992
Homo sapiens
brenda
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
Bos taurus, Gallus gallus, Mesocricetus auratus, Oryctolagus cuniculus, Sus scrofa
brenda
Fritz, T.A.; Gabb, M.M.; Wei, G.; Esko, J.D.
Two N-acetylglucosaminyltransferases catalyze the biosynthesis of heparan sulfate
J. Biol. Chem.
269
28809-28814
1994
Cricetulus griseus
brenda
Nishiu, J.; Kioka, N.; Fukada, T.; Sakai, H.; Komano, T.
Characterization of rat N-acetylglucosaminyltransferase I expressed in Escherichia coli
Biosci. Biotechnol. Biochem.
59
1750-1752
1995
Rattus norvegicus
brenda
Reck, F.; Springer, M.; Meinjohanns, E.; Paulsen, H.; Brockhausen, I.; Schachter, H.
Synthetic substrate analogs for UDP-GlcNAc: manalpha1-3R beta1-2-N-acetylglucosaminyltransferase I. Substrate specificity and inhibitors for the enzyme
Glycoconj. J.
12
747-754
1995
Rattus norvegicus
brenda
Wagner, R.; Liedtke, S.; Kretzschmar, E.; Geyer, H.G.; Geyer, R.; Klenk, H.D.
Elongation of the N-glycans of fowl plague virus hemagglutinin expressed in Spodoptera frugiperda (Sf9) cells by coexpression of human beta1,2-N-acetylglucosaminyltransferase I
Glycobiology
6
165-175
1996
Homo sapiens
brenda
Yoshida, S.; Suzuki, M.; Yamano, S.; Takeuchi, M.; Ikenaga, H.; Kioka, N.; Sakai, H.; Komano, T.
Expression and characterization of rat UDP-N-acetylglucosamine: alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I in Saccharomyces cerevisiae
Glycobiology
9
53-58
1999
no activity in Saccharomyces cerevisiae, Rattus norvegicus
brenda
Unligil, U.M.; Zhou, S.; Yuwaraj, S.; Sarkar, M.; Schachter, H.; Rini, J.M.
X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: catalytic mechanism and a new protein superfamily
EMBO J.
19
5269-5280
2000
Oryctolagus cuniculus (P27115), Oryctolagus cuniculus
brenda
Opat, A.S.; Houghton, F.; Gleeson, P.A.
Medial Golgi but not late Golgi glycosyltransferases exist as high molecular weight complexes. Role of luminal domain in complex formation and localization
J. Biol. Chem.
275
11836-11845
2000
Homo sapiens
brenda
Wenderoth, I.; Von Schaewen, A.
Isolation and characterization of plant N-acetyl glucosaminyltransferase I (GntI) cDNA sequences. Functional analyses in the Arabidopsis cgl mutant and in antisense plants
Plant Physiol.
123
1097-1108
2000
Arabidopsis thaliana, Nicotiana tabacum, Solanum tuberosum (Q8VX56), Solanum tuberosum
brenda
Fujiyama, K.; Ido, Y.; Misaki, R.; Moran, D.G.; Yanagihara, I.; Honda, T.; Nishimura, S.I.; Yoshida, T.; Seki, T.
Human N-acetylglucosaminyltransferase I. Expression in Escherichia coli as a soluble enzyme, and application as an immobilized enzyme for the chemoenzymatic synthesis of N-linked oligosaccharides
J. Biosci. Bioeng.
92
569-574
2001
Homo sapiens
brenda
Chen, W.; Unligil, U.M.; Rini, J.M.; Stanley, P.
Independent Lec1A CHO glycosylation mutants arise from point mutations in N-acetylglucosaminyltransferase I that reduce affinity for both substrates. Molecular consequences based on the crystal structure of GlcNAc-TI
Biochemistry
40
8765-8772
2001
Mesocricetus auratus, Cricetulus griseus (P70680)
brenda
Mucha, J.; Svoboda, B.; Frohwein, U.; Strasser, R.; Mischinger, M.; Schwihla, H.; Altmann, F.; Hane, W.; Schachter, H.; Glossl, J.; Mach, L.
Tissues of the clawed frog Xenopus laevis contain two closely related forms of UDP-GlcNAc:alpha3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I
Glycobiology
11
769-778
2001
Spodoptera frugiperda, Xenopus laevis
brenda
Zhang, W.; Cao, P.; Chen, S.; Spence, A.M.; Zhu, S.; Staudacher, E.; Schachter, H.
Synthesis of paucimannose N-glycans by Caenorhabditis elegans requires prior actions of UDP-N-acetyl-D-glucosamine:alpha-3-D-mannoside beta1,2-N-acetylglucosaminyltransferase I, alpha3,6-mannosidase II and a specific membrane-bound beta-N-acetylglucosaminidase
Biochem. J.
372
53-64
2003
Caenorhabditis elegans
brenda
Strasser, R.; Stadlmann, J.; Svoboda, B.; Altmann, F.; Glossl, J.; Mach, L.
Molecular basis of N-acetylglucosaminyltransferase I deficiency in Arabidopsis thaliana plants lacking complex N-glycans
Biochem. J.
387
385-391
2005
Arabidopsis thaliana, Oryctolagus cuniculus
brenda
Nozaki, H.; Matsuzawa, T.; Nakamura, T.; Arai, I.; Urashima, T.
Are there two forms of beta 2-N-acetylglucosaminyltransferase I in rat testicular and epididymal fluids?
Biochim. Biophys. Acta
1649
140-145
2003
Rattus norvegicus
brenda
Tvaroska, I.; Andre, I.; Carver, J.P.
Catalytic mechanism of the inverting N-acetylglucosaminyltransferase I: DFT quantum mechanical model of the reaction pathway and determination of the transition state structure
Glycobiology
13
559-566
2003
Oryctolagus cuniculus (P27115)
brenda
Strasser, R.; Altmann, F.; Glossl, J.; Steinkellner, H.
Unaltered complex N-glycan profiles in Nicotiana benthamiana despite drastic reduction of beta1,2-N-acetylglucosaminyltransferase I activity
Glycoconj. J.
21
275-282
2004
Nicotiana benthamiana
brenda
Nozaki, H.; Miyamoto, A.; Hayashi, K.G.; Matsui, M.; Yoshida, T.; Nakamura, T.; Arai, I.; Urashima, T.
N-Acetylglucosaminyltransferase I activity in bovine ovarian follicular fluids from dominant and atretic follicles
J. Appl. Glycosci.
51
315-320
2004
Bos taurus
-
brenda
Nozaki, H.; Wijayagunawardane, M.P.; Kodituwakku, S.P.; Yoshida, T.; Nakamura, T.; Arai, I.; Urashima, T.; Miyamoto, A.
N-acetylglucosaminyltransferase I activity of bovine oviduct epithelial cells: stimulation by luteinizing hormone, vascular endothelial growth factor and tumor necrosis factor alpha
J. Reprod. Dev.
51
229-234
2005
Bos taurus
brenda
Schachter, H.; Reck, F.; Paulsen, H.
Use of synthetic oligosaccharide substrate analogs to map the active sites of N-acetylglucosaminyltransferases I and II
Methods Enzymol.
363
459-475
2003
Rattus norvegicus
brenda
Matsunami, K.; Miyagawa, S.; Nakagawa, K.; Otsuka, H.; Hideaki, O.; Shirakura, R.
Molecular cloning of pigGnT-I and I.2: an application to xenotransplantation
Biochem. Biophys. Res. Commun.
343
677-683
2006
Sus scrofa
brenda
Kasajima, Y.; Yamaguchi, M.; Hirai, N.; Ohmachi, T.; Yoshida, T.
In vivo expression of UDP-N-acetylglucosamine: alpha-3-D-Mannoside beta-1,2-N-acetylglucosaminyltransferase I (GnT-1) in Aspergillus oryzae and effects on the sugar chain of alpha-amylase
Biosci. Biotechnol. Biochem.
70
2662-2668
2006
Rattus norvegicus
brenda
Kozmon, S.; Tvaroska, I.
Catalytic mechanism of glycosyltransferases: hybrid quantum mechanical/molecular mechanical study of the inverting N-acetylglucosaminyltransferase I
J. Am. Chem. Soc.
128
16921-16927
2006
Oryctolagus cuniculus (P27115)
brenda
Kainz, E.; Gallmetzer, A.; Hatzl, C.; Nett, J.H.; Li, H.; Schinko, T.; Pachlinger, R.; Berger, H.; Reyes-Dominguez, Y.; Bernreiter, A.; Gerngross, T.; Wildt, S.; Strauss, J.
N-glycan modification in Aspergillus species
Appl. Environ. Microbiol.
74
1076-1086
2008
Homo sapiens
brenda
Saribas, A.S.; Johnson, K.; Liu, L.; Bezila, D.; Hakes, D.
Refolding of human beta-1-2 GlcNAc transferase (GnT1) and the role of its unpaired Cys121
Biochem. Biophys. Res. Commun.
362
381-386
2007
Homo sapiens
brenda
Kang, J.S.; Frank, J.; Kang, C.H.; Kajiura, H.; Vikram, M.; Ueda, A.; Kim, S.; Bahk, J.D.; Triplett, B.; Fujiyama, K.; Lee, S.Y.; von Schaewen, A.; Koiwa, H.
Salt tolerance of Arabidopsis thaliana requires maturation of N-glycosylated proteins in the Golgi apparatus
Proc. Natl. Acad. Sci. USA
105
5933-5938
2008
Arabidopsis thaliana
brenda
Sourrouille, C.; Marquet-Blouin, E.; DAoust, M.A.; Kiefer-Meyer, M.C.; Seveno, M.; Pagny-Salehabadi, S.; Bardor, M.; Durambur, G.; Lerouge, P.; Vezina, L.; Gomord, V.
Down-regulated expression of plant-specific glycoepitopes in alfalfa
Plant Biotechnol. J.
6
702-721
2008
Nicotiana tabacum
brenda
Chen, H.L.; Li, C.F.; Grigorian, A.; Tian, W.; Demetriou, M.
T cell receptor signaling co-regulates multiple Golgi genes to enhance N-glycan branching
J. Biol. Chem.
284
32454-32461
2009
Homo sapiens
brenda
Chen, R.; Pawlicki, M.; Hamilton, B.; Tolbert, T.
Enzyme-catalyzed synthesis of a hybrid N-linked oligosaccharide using N-acetylglucosaminyltransferase I
Adv. Synth. Catal.
350
1689-1695
2008
Homo sapiens
-
brenda
Schoberer, J.; Vavra, U.; Stadlmann, J.; Hawes, C.; Mach, L.; Steinkellner, H.; Strasser, R.
Arginine/lysine residues in the cytoplasmic tail promote ER export of plant glycosylation enzymes
Traffic
10
101-115
2009
Arabidopsis thaliana
brenda
Henquet, M.; Heinhuis, B.; Borst, J.; Eigenhuijsen, J.; Schreuder, M.; Bosch, D.; van der Krol, A.
Differential effects of human and plant N-acetylglucosaminyltransferase I (GnTI) in plants
Transgenic Res.
19
535-547
2009
Arabidopsis thaliana, Homo sapiens
brenda
Zhong, X.; Cooley, C.; Seth, N.; Juo, Z.S.; Presman, E.; Resendes, N.; Kumar, R.; Allen, M.; Mosyak, L.; Stahl, M.; Somers, W.; Kriz, R.
Engineering novel Lec1 glycosylation mutants in CHO-DUKX cells: molecular insights and effector modulation of N-acetylglucosaminyltransferase I
Biotechnol. Bioeng.
109
1723-1734
2012
Oryctolagus cuniculus
brenda
Schachter, H.; Boulianne, G.
Life is sweet! A novel role for N-glycans in Drosophila lifespan
Fly
5
18-24
2011
Drosophila melanogaster
brenda
Baiet, B.; Burel, C.; Saint-Jean, B.; Louvet, R.; Menu-Bouaouiche, L.; Kiefer-Meyer, M.C.; Mathieu-Rivet, E.; Lefebvre, T.; Castel, H.; Carlier, A.; Cadoret, J.P.; Lerouge, P.; Bardor, M.
N-glycans of Phaeodactylum tricornutum diatom and functional characterization of its N-acetylglucosaminyltransferase I enzyme
J. Biol. Chem.
286
6152-6164
2011
Phaeodactylum tricornutum
brenda
Dohi, K.; Isoyama-Tanaka, J.; Tokuda, T.; Fujiyama, K.
Recombinant expression and characterization of N-acetylglucosaminyltransferase I derived from Nicotiana tabacum
J. Biosci. Bioeng.
109
388-391
2010
Nicotiana tabacum (Q9ST97), Nicotiana tabacum
brenda
Schachter, H.
Mgat1-dependent N-glycans are essential for the normal development of both vertebrate and invertebrate metazoans
Semin. Cell Dev. Biol.
21
609-615
2010
Caenorhabditis elegans, Drosophila melanogaster, Mus musculus
brenda
Abdel Rahman, A.; Ryczko, M.; Nakano, M.; Pawling, J.; Rodrigues, T.; Johswich, A.; Taniguchi, N.; Dennis, J.
Golgi N-glycan branching N-acetylglucosaminyltransferases I, V and VI promote nutrient uptake and metabolism
Glycobiology
25
225-240
2015
Homo sapiens (P26572), Homo sapiens
brenda
Damerow, M.; Rodrigues, J.A.; Wu, D.; Guether, M.L.; Mehlert, A.; Ferguson, M.A.
Identification and functional characterization of a highly divergent N-acetylglucosaminyltransferase I (TbGnTI) in Trypanosoma brucei
J. Biol. Chem.
289
9328-9339
2014
Trypanosoma brucei brucei, Trypanosoma brucei brucei 427
brenda
Schoberer, J.; Liebminger, E.; Vavra, U.; Veit, C.; Castilho, A.; Dicker, M.; Maresch, D.; Altmann, F.; Hawes, C.; Botchway, S.; Strasser, R.
The transmembrane domain of N-acetylglucosaminyltransferase I is the key determinant for its Golgi subcompartmentation
Plant J.
80
809-822
2014
Nicotiana benthamiana
brenda
Yan, S.; Wang, H.; Schachter, H.; Jin, C.; Wilson, I.B.H.; Paschinger, K.
Ablation of N-acetylglucosaminyltransferases in Caenorhabditis induces expression of unusual intersected and bisected N-glycans
Biochim. Biophys. Acta
1862
2191-2203
2018
Caenorhabditis elegans (G5EBG7), Caenorhabditis elegans (G5EFK6), Caenorhabditis elegans (Q11068), Caenorhabditis elegans
brenda
Li, Y.; Liu, Y.; Zhu, H.; Chen, X.; Tian, M.; Wei, Y.; Gong, Y.; Jiang, J.
N-acetylglucosaminyltransferase I promotes glioma cell proliferation and migration through increasing the stability of the glucose transporter GLUT1
FEBS Lett.
594
358-366
2020
Homo sapiens (P26572)
brenda
Vanier, G.; Lucas, P.L.; Loutelier-Bourhis, C.; Vanier, J.; Plasson, C.; Walet-Balieu, M.L.; Tchi-Song, P.C.; Remy-Jouet, I.; Richard, V.; Bernard, S.; Driouich, A.; Afonso, C.; Lerouge, P.; Mathieu-Rivet, E.; Bardor, M.
Heterologous expression of the N-acetylglucosaminyltransferase I dictates a reinvestigation of the N-glycosylation pathway in Chlamydomonas reinhardtii
Sci. Rep.
7
10156
2017
Arabidopsis thaliana (Q9XGM8), Phaeodactylum tricornutum (G0WVT5), Phaeodactylum tricornutum
brenda
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