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Information on EC 2.4.1.101 - alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase and Organism(s) Oryctolagus cuniculus and UniProt Accession P27115

for references in articles please use BRENDA:EC2.4.1.101
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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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Oryctolagus cuniculus
UNIPROT: P27115
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The taxonomic range for the selected organisms is: Oryctolagus cuniculus
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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alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase
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N-acetylglucosaminyltransferase I
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I
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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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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-glucosamine + Man5GlcNAc2-[protein] = UDP + Man5GlcNAc3-[protein]
show the reaction diagram
UDP-N-acetyl-alpha-D-glucosamine + Man5GlcNAc2-[protein] = UDP + Man5GlcNAc3-[protein]
show the reaction diagram
mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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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
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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
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 + 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
?
show the reaction diagram
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-
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-
?
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
?
show the reaction diagram
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?
UDP + alpha-D-mannosyl-1,3-(alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-D-glucosamine
?
show the reaction diagram
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?
UDP-N-acetyl-alpha-D-glucosamine +
?
show the reaction diagram
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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
show the reaction diagram
UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,3-beta-D-mannosyl-1,4-N-acetyl-D-glucosamine
UDP + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-beta-D-mannosyl-1,4-N-acetyl-D-glucosamine
show the reaction diagram
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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 + dehexoso-orosomucoid
?
show the reaction diagram
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?
UDP-N-acetyl-D-glucosamine + Man5GlcNAc2-glycopeptide
UDP + GlcNAc(1-2)Man5GlcNAc2-glycopeptide
show the reaction diagram
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-
?
UDP-N-acetyl-D-glucosamine + Manalpha1,6(Manalpha1,3)Manbeta-1-O-octyl
UDP + GlcNAc(1-2)Manalpha(1-6)Manalpha(1-3)Manbeta-1-O-octyl
show the reaction diagram
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-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetylglucosamine-1,4-(fucose-1,6)-N-acetyl-glucosamine-Asn-peptide
UDP + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetylglucosamine-1,4-(fucose-1,6)-N-acetyl-glucosamine-Asn-peptide
show the reaction diagram
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no activity
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-
?
additional information
?
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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
GlcNAc transfer catalyzed by GnT-I is the first step in the conversion of high mannose oligosaccharides to complex and hybrid N-glycan structures
-
-
?
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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?
additional information
?
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the enzyme is essential for processing of high-mannose to hybrid and complex N-glycans
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
binds not independently of UDP-N-acetyl-D-glucose
Ca2+
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slight activation
Sn2+
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slight activation
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2'-dUDP
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weak
2'-O-Methyl-UDP
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weak
5-Bromo-UTP
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5-Mercury-UDP
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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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UDP-glucose
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weak
UDP-N-acetylgalactosamine
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weak
UDP-N-acetylglucosamine
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competitively to UDP
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Triton X-100
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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
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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
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2.03
alpha-D-mannosyl-1,3-(alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-D-glucosamine
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0.0384
alpha-D-mannosyl-1,3-(alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
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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
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0.0384 - 0.078
UDP-N-acetyl-D-glucosamine
additional information
additional information
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kinetic study
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.8
alpha-D-mannosyl-1,6-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
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0.034
UDP-N-acetylglucosamine
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19.8
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low-molecular weight form
2.51
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purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1 - 6.9
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about half-maximal activity at pH 5.1 and about 70% of maximal activity at pH 6.9
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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modulating N-acetylglucosaminyltransferase I activity in cells can influence antibody effector functions
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MGAT1_RABIT
447
1
51540
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
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x * 45000 + x * 50000 + x * 54000, low molecular weight form, SDS-PAGE, major band: MW 45000
46000
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x * 58000 + x * 46000, SDS-PAGE
50000
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x * 45000 + x * 50000 + x * 54000, low molecular weight form, SDS-PAGE, major band: MW 45000
54000
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x * 45000 + x * 50000 + x * 54000, low molecular weight form, SDS-PAGE, major band: MW 45000
58000
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x * 58000 + x * 46000, SDS-PAGE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D144N
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expression of D144N muatant enzyme of rabbit in cgl mutant of Arabidopsis thaliana lacking GnTI activity (caused by a D144N mutation in GnTI) can partially restore complex N-glycan formation
D291N
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inactive
more.
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deleting seven C-terminal amino acids of the enzyme reduces enzymatic activity by 40%
P138L
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inactive
R415K
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inactive
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
repeated freeze-thawing, stable to
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20% glycerol v/v, up to a year
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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
recombinant catalytic fragment from Sf9 insect cells
two molecular weight forms separable by gel filtration, purification of low-molecular weight form
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of catalytic fragment in Spodoptera frugiperda Sf9 cells via baculovirus infection
expressed in CHO-DUKX-Lec1 cells
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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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team