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Information on EC 2.4.1.101 - alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase and Organism(s) Homo sapiens

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EC Tree
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-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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Homo sapiens
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylglucosaminyltransferase, uridine diphosphoacetylglucosamine-alpha-1,3-mannosylglycoprotein beta-1,2-N-
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-
-
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alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase
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-
-
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beta-1-2 GlcNAc transferase
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ChGnTI
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chimeric Arabidopsis-human enzyme
GlcNAc transferase I
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GlcNAcT-I
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GnT1
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GnTI
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Golgi N-glycan branching N-acetylglucosaminyltransferase I
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HuGnTI
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human enzyme
MGAT1
N-acetylglucosaminyltransferase I
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I
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-
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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-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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uridine diphosphoacetylglucosamine-alpha-1,3-mannosylglycoprotein beta-1,2-N-acetylglucosaminyltransferase
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-
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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-
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-
PATHWAY SOURCE
PATHWAYS
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
102576-81-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-glucosamine + 3-(alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
show the reaction diagram
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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
show the reaction diagram
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key enzyme of biosynthesis of complex and hybrid N-glycans
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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
show the reaction diagram
UDP-N-acetyl-D-glucosamine + fowl plague virus hemagglutinin
UDP + fowl plague virus hemagglutinin with terminal N-acetyl-D-glucosaminyl residues
show the reaction diagram
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recombinant coexpression of enzyme and substrate in SF9 insect cells
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?
UDP-N-acetyl-D-glucosamine + Man5-RNAse B
UDP + RNAse B-GlcNAc2-Man5-GlcNAc
show the reaction diagram
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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
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-
?
UDP-N-acetyl-D-glucosamine + Man5GlcNAc2
?
show the reaction diagram
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best substrate
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-
?
UDP-N-acetyl-D-glucosamine + ovalbumin
?
show the reaction diagram
UDP-N-acetylglucosamine + alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-1,4-N-acetyl-D-glucosaminyl-Asn-peptide
UDP + alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-alpha-D-mannosyl-1,6-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
show the reaction diagram
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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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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-glucosamine + 3-(alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-1,4-N-acetyl-D-glucosaminyl-Asn-peptide
UDP + alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-alpha-D-mannosyl-1,6-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-Asn-peptide
show the reaction diagram
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key enzyme of biosynthesis of complex and hybrid N-glycans
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
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requirement
Mn2+
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requirement
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
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Zn2+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.483
Man5GlcNAc2
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recombinant fusion protein
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.48
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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
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in vivo assay of recombinant enzyme expressed in Sf9 cells with coexpressed fowl plague virus HA as endogenous substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
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recombinant fusion protein
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
40
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recombinant fusion protein
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 70
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recombinant fusion protein
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MGAT1 is highly expressed in glioblastoma tissues
Manually annotated by BRENDA team
cell proliferation and migration analysis, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
metabolism
physiological function
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MGAT1_HUMAN
445
1
50878
Swiss-Prot
Secretory Pathway (Reliability: 1)
B3KQW5_HUMAN
197
0
23241
TrEMBL
Secretory Pathway (Reliability: 5)
D6RAK2_HUMAN
104
1
11187
TrEMBL
Secretory Pathway (Reliability: 1)
D6RB69_HUMAN
127
1
13803
TrEMBL
Secretory Pathway (Reliability: 1)
D6RBS3_HUMAN
103
1
11116
TrEMBL
Secretory Pathway (Reliability: 1)
D6RF69_HUMAN
199
1
22016
TrEMBL
Secretory Pathway (Reliability: 1)
Q8NBL8_HUMAN
302
1
34972
TrEMBL
Secretory Pathway (Reliability: 1)
B3KQ18_HUMAN
445
1
50866
TrEMBL
Secretory Pathway (Reliability: 1)
B7Z7F2_HUMAN
517
0
58765
TrEMBL
other Location (Reliability: 2)
D6R9U2_HUMAN
111
1
11935
TrEMBL
Secretory Pathway (Reliability: 1)
Q59G70_HUMAN
473
1
53504
TrEMBL
Mitochondrion (Reliability: 5)
D6RA48_HUMAN
95
1
10298
TrEMBL
Secretory Pathway (Reliability: 1)
D6RHZ8_HUMAN
153
1
16631
TrEMBL
Secretory Pathway (Reliability: 1)
D6RD15_HUMAN
115
1
12381
TrEMBL
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
-
x * 50000, recombinant enzyme, SDS-PAGE
53000
x * 53000, SDS-PAGE
78000
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mass of the fusion protein, free YFP-marker is about 27000 Da, 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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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O-glycosylated
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C121A
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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
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mutant enzyme shows no transfer of GlcNAc from UDP-GlcNAc to the glycoprotein acceptor Man5-RNAse B
C121S
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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
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mutant enzyme shows no transfer of GlcNAc from UDP-GlcNAc to the glycoprotein acceptor Man5-RNAse B
D77N
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exchange mutation in chimera TfR/GnT1myc, no effect on Golgi localization and inclusion into high molecular weight complexes, no catalytic activity
R120A/C121H
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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
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exchange mutation in chimera TfR/GnT1myc, no effect on Golgi localization and inclusion into high molecular weight complexes, no catalytic activity
R85S
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exchange mutation in chimera TfR/GnT1myc, no effect on Golgi localization and inclusion into high molecular weight complexes, no catalytic activity
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
large scale, recombinant maltose-binding fusion protein
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one Ni2+-NTA chromatography step is sufficient for oligosaccharide synthesis
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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
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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
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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
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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
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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
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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
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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
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recombinant tet-inducible expression of Flag-tagged GlcNAcT-I in HeLa and HEK293 cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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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limited enzyme expression after anti-CD3 stimulation
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
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immobilization of the enzyme as maltose-binding fusion protein on an amylose resin for production of high-mannose type oligosaccharides
molecular biology
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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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team