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

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
2.4.1.101
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RECOMMENDED NAME
GeneOntology No.
alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
UDP-N-acetyl-D-glucosamine + 3-(alpha-D-mannosyl)-beta-D-mannosyl-R = UDP + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
show the reaction diagram
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-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
mechanism
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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
show the reaction diagram
active site; DxD motif; ordered sequential bi bi mechanism; SGC domain of SGC superfamily
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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
show the reaction diagram
active site; D212 is the central residue of the DxD motif, conserved throughout all species; R303 is important for enzyme activity, conserved throughout all species
P70680
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
modeling study provides detailed insight into the mechanism of the GlcNAc transfer
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REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hexosyl group transfer
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PATHWAY
KEGG Link
MetaCyc Link
Metabolic pathways
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N-Glycan biosynthesis
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Various types of N-glycan biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-glucosamine:3-(alpha-D-mannosyl)-beta-D-mannosyl-glycoprotein 2-beta-N-acetyl-D-glucosaminyltransferase
R represents the remainder of the N-linked oligosaccharide in the glycoprotein acceptor. Note that this enzyme acts before N-acetylglucosaminyltransferases II, III, IV, V and VI (click here for diagram).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
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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alpha3-D-mannoside-beta-1,2-N-acetylglucosaminyltransferase I
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AtGnTI
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Arabidopsis enzyme
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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GlcNAc-T I
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GlcNAc-T I
P70680
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GlcNAc-T I
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GlcNAc-T I
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gly-12
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gene name
GLY-13
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gene name
gly-14
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gene name
GnT I
Q9ST97
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GnT1
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GnTI
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GnTI
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HuGnTI
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human enzyme
MGAT1
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gene name
MGAT1
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MGAT1
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N-acetylglucosaminyltransferase I
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N-acetylglucosaminyltransferase I
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N-acetylglucosaminyltransferase I
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N-acetylglucosaminyltransferase I
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N-acetylglucosaminyltransferase I
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N-acetylglucosaminyltransferase I
Q9ST97
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N-acetylglucosaminyltransferase I
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N-acetylglucosaminyltransferase I
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N-acetylglucosaminyltransferases I
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N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I
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pigGnT-I
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UDP-GlcNAc:alpha3-D-mannoside beta1,2-N-acetylglucosaminyltransferase
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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-Nacetylglucosaminyltransferase 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-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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CAS REGISTRY NUMBER
COMMENTARY
102576-81-8
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
a D144N muation in the GnTI of cgl mutant lacking GnTI activity is molecular basis of the defect
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Manually annotated by BRENDA team
constitutive single copy gene
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Manually annotated by BRENDA team
wild-type and cg/1 plants lacking an own active N-acetylglucosaminyltransferase Is
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Manually annotated by BRENDA team
1 difference to published sequence U65791: C1340 is A1340
SwissProt
Manually annotated by BRENDA team
wild-type and mutant cell lines
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Manually annotated by BRENDA team
recombinant enzyme as fusion protein with maltose-binding protein
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Manually annotated by BRENDA team
constitutive single copy gene
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Manually annotated by BRENDA team
expressed in alfalfa together with human beta 1,4-galacosyltransferase
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Manually annotated by BRENDA team
no activity in Saccharomyces cerevisiae
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Manually annotated by BRENDA team
male Donryu; transferases A and B
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Manually annotated by BRENDA team
constitutive single copy gene
Uniprot
Manually annotated by BRENDA team
2 isozymes A and B
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
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modulating N-acetylglucosaminyltransferase I activity in cells can influence antibody effector functions
malfunction
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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
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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
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Mgat1-null mouse embryos die at 9.5-10.5 days after fertilization
metabolism
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part of N-glycan pathway
metabolism
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the enzyme controls the synthesis of paucimannose N-glycans
physiological function
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plant N-glycan processing
physiological function
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N-glycan formation on glycoproteins
physiological function
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enzyme-dependent N-glycans are essential for cell-cell and cell-matrix interactions
physiological function
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Mgat1-dependent N-glycans are required for normal development
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-glucosamine + 2-deoxy-Manalpha6(Manalpha3)Man-beta-octyl
UDP + ?
show the reaction diagram
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-
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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
show the reaction diagram
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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
show the reaction diagram
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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-O-(4,4-azopentyl)-Manalpha6(Manalpha3)Man-beta-octyl
UDP + ?
show the reaction diagram
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-
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?
UDP-N-acetyl-D-glucosamine + 3-O-(4,5-epoxypentyl)-Manalpha6(Manalpha3)Man-beta-octyl
UDP + ?
show the reaction diagram
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-
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?
UDP-N-acetyl-D-glucosamine + 3-O-(5-iodoacetamidopentyl)-Manalpha6(Manalpha3)Man-beta-octyl
UDP + ?
show the reaction diagram
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-
-
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?
UDP-N-acetyl-D-glucosamine + 3-O-pentyl-Manalpha6(Manalpha3)Man-beta-octyl
UDP + ?
show the reaction diagram
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-
-
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?
UDP-N-acetyl-D-glucosamine + 4-O-methyl-Manalpha6(Manalpha3)Man-beta-octyl
UDP + ?
show the reaction diagram
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-
-
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?
UDP-N-acetyl-D-glucosamine + 6-O-methyl-Manalpha6(Manalpha3)Man-beta-octyl
UDP + ?
show the reaction diagram
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-
-
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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
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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
show the reaction diagram
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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
show the reaction diagram
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R: H
R: H
?
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
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R: H
R: H
?
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
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no activity with pyridylaminated substrate
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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
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recombinant isozyme A and B mutant T223A, 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
show the reaction diagram
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pyridylamine
R: pyridylamine
?
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
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pyridylamine
R: pyridylamine
?
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
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1,4-N-acetyl-D-glucosaminyl-Asn
R: H
?
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
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1,4-N-acetyl-D-glucosaminyl-R
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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
-
synthetic-beta-D-mannosyl-(1,6-anhydro)-derivative acts as substrate, too
R: H
?
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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-
-
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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
show the reaction diagram
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-
-
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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
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-1,4-N-acetyl-D-glucosaminyl-Asn-peptide
UDP + alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-alpha-D-mannosyl-1,6-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-Asn-peptide
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-1,4-N-acetyl-D-glucosaminyl-Asn-peptide
UDP + alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-alpha-D-mannosyl-1,6-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-Asn-peptide
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-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
-
stimulates galactosyltransferase of bovine milk
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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
-
key enzyme of biosynthesis of complex and hybrid N-glycans
-
-
?
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
-
key enzyme of biosynthesis of complex and hybrid N-glycans
-
-
?
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
-
key enzyme of biosynthesis of complex and hybrid N-glycans
-
-
?
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
-
key enzyme of biosynthesis of complex and hybrid N-glycans
-
-
?
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 + 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 + 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 + 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 + 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 + 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 + 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 + 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
-
-
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
show the reaction diagram
-
substrate specificity
-
?
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
-
substrate specificity
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
show the reaction diagram
-
substrate specificity
R: 1,4-N-acetyl-D-glucosaminyl-Asn
?
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
-
substrate specificity
R: 1,4-N-acetyl-D-glucosaminyl-Asn
?
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
-
substrate specificity
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
show the reaction diagram
-
substrate specificity
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
show the reaction diagram
-
pyridylaminated oligosaccharide
-
?
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
-
R: H
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
show the reaction diagram
-
R: H
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
show the reaction diagram
-
R: H
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
show the reaction diagram
-
R: H
R: (fucose-1,6)-1,4-N-acetyl-D-glucosaminyl-Asn, R: 1,4-N-acetyl-D-glucosaminyl-Asn
?
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
-
essential for activity: unsubstituted equatorial hydroxyl on C-4 of beta-linked mannosyl-residue
R: 1,4-N-acetyl-D-glucosaminyl-Asn
?
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
-
essential for activity: unsubstituted equatorial hydroxyl on C-4 of beta-linked mannosyl-residue
R: 1,4-N-acetyl-D-glucosaminyl-Asn
?
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
-
essential for activity: unsubstituted equatorial hydroxyl on C-4 of beta-linked mannosyl-residue
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
show the reaction diagram
-
R: pyridinylamine
-
?
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
-
R: pyridinylamine
pyridinylamine
?
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
-
R: 4-N-acetyl-D-glucosaminyl-Asn-peptide
R: H, R: (fucose-1,6)-1,4-N-acetyl-D-glucosaminyl-Asn, R: 1,4-N-acetyl-D-glucosaminyl-Asn
?
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
-
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
R: H, R: (fucose-1,6)-1,4-N-acetyl-D-glucosaminyl-Asn, R: 1,4-N-acetyl-D-glucosaminyl-Asn
?
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
-
does not act on alpha-mannosyl-1,2-alpha-mannosyl-, alpha-mannosyl-1,3-alpha-mannosyl-, alpha-mannosyl-1,6-alpha-mannosyl-termini
R: H, R: (fucose-1,6)-1,4-N-acetyl-D-glucosaminyl-Asn, R: 1,4-N-acetyl-D-glucosaminyl-Asn
?
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
-
R: (fucose-1,6)-1,4-N-acetyl-D-glucosaminyl-Asn
R: H, R: (fucose-1,6)-1,4-N-acetyl-D-glucosaminyl-Asn, R: 1,4-N-acetyl-D-glucosaminyl-Asn
?
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
-
R: 1,4-N-acetyl-D-glucosaminyl-Asn
R: H, R: (fucose-1,6)-1,4-N-acetyl-D-glucosaminyl-Asn
?
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
-
R: 1,4-N-acetyl-D-glucosaminyl-Asn
R: 1,4-N-acetyl-D-glucosaminyl-Asn
?
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
-
R: 1,4-N-acetyl-D-glucosaminyl-Asn
R: 1,4-N-acetyl-D-glucosaminyl-Asn
?
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
-
R: 1,4-N-acetyl-D-glucosaminyl-Asn
R: 1,4-N-acetyl-D-glucosaminyl-Asn
?
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
-
R: 1,4-N-acetyl-D-glucosaminyl-Asn
R: 1,4-N-acetyl-D-glucosaminyl-Asn
?
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
-
R: 1,4-N-acetyl-D-glucosaminyl-Asn
R: 1,4-N-acetyl-D-glucosaminyl-Asn
?
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
-
R: 1,4-N-acetyl-D-glucosaminyl-Asn
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
show the reaction diagram
-
R: 1,4-N-acetyl-D-glucosaminyl-Asn
R: 1,4-N-acetyl-D-glucosaminyl-1,4-N-acetyl-D-glucosaminyl-Asn
?
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
-
an axial 2-hydroxyl group on the beta-linked mannose of the substrate are essential for the enzyme
R: 1,4-N-acetyl-D-glucosaminyl-Asn, 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
show the reaction diagram
-
absolute specificity for terminal branched mannosyl residues
transfers an N-acetylglucosamine in beta-1,2-linkage to mannosyl-1,3-beta-mannosyl-terminus
?
UDP-N-acetyl-D-glucosamine + asialofetuin
?
show the reaction diagram
-
beta-galactosidase-, beta-N-acetylhexosamidase- and alpha-mannosidase-treated asialofetuin, beta-galactosidase- and beta-N-acetylhexosamidase-treated asialofetuin
-
-
?
UDP-N-acetyl-D-glucosamine + beta-galactosidase- and beta-N-acetylhexosamidase-treated asialotransferrin
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + dehexoso-orosomucoid
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + desialo-degalacto-dehexosamine-orosomucoid
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + fowl plague virus hemagglutinin
UDP + fowl plague virus hemagglutinin with terminal N-acetyl-D-glucosaminyl residues
show the reaction diagram
-
recombinant coexpression of enzyme and substrate in SF9 insect cells
-
?
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)[GlcNAbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
show the reaction diagram
-, Q9ST97
3.9% activity compared to Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
-
-
?
UDP-N-acetyl-D-glucosamine + GlcUAcbeta1-3Galbeta1-O-naphthalenemethanol
?
show the reaction diagram
-
synthetic substrate
-
-
?
UDP-N-acetyl-D-glucosamine + glycopeptides prepared from porcine IgC
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Man3Man-O-beta4-N-acetyl-D-glucosamine
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Man5-RNAse B
UDP + RNAse B-GlcNAc2-Man5-GlcNAc
show the reaction diagram
-
wild type hGnT1 and mutants C121A, C121S and R120A/C121H transfer GlcNAc from UDP-GlcNAc to the glycoprotein acceptor Man5-RNAse B, whereas mutants C121T and C121D are inactive. After 1 h, the wild-type MBP-hGnT1(D103) and C121A mutant convert more than 50% of RNAse BM5 to RNAse BM5Gn, while the C121S mutant shows less than 25% conversion. The wild-type MBP-hGnT1(D103) and both C121A and C121S mutants convert RNAse BM5 nearly completely to RNAse BM5Gn following overnight incubation. The R120A/C121H mutant is less active than the wild-type and the single mutants. It converts more than half of the RNAse BM5 into RNAse BM5Gn after 17 h
-
-
?
UDP-N-acetyl-D-glucosamine + Man5GlcNAc2
?
show the reaction diagram
P70680
-
-
-
?
UDP-N-acetyl-D-glucosamine + Man5GlcNAc2
?
show the reaction diagram
-
best substrate
-
-
?
UDP-N-acetyl-D-glucosamine + Man5GlcNAc2-glycopeptide
UDP + GlcNAc(1-2)Man5GlcNAc2-glycopeptide
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha(1-2)Manalpha(1-3)[Manalpha(1-6)]Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
UDP + Manalpha(1-2)Manalpha(1-3)[Manalpha(1-6)]Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
show the reaction diagram
-, Q9ST97
0.5% activity compared to Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha(1-3)Man
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha(1-3)Man
UDP + ?
show the reaction diagram
-
about 15% of the activity with Manalpha(1-3)Manalpha(1-6)Man
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha(1-3)Manalpha(1-6)Man
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha(1-3)Manalpha(1-6)Man
UDP + ?
show the reaction diagram
-
about 30% of the activity with alpha1,3alpha1,6 mannopentaose
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha(1-3)Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-R
UDP + Manalpha(1-3)Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-R
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha(1-3)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
UDP + GlcNAbeta(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
show the reaction diagram
-, Q9ST97
0.7% activity compared to Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha(1-6)Man
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
UDP + Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
show the reaction diagram
-, Q9ST97
100% activity
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-R
UDP + Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-R
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
UDP + Manalpha(1-6)[GlcNAbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
show the reaction diagram
-, Q9ST97
6.9% activity compared to Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-R
UDP + Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-R
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)[Fucalpha(1-3)]GlcNAc-pyridylaminoside
UDP + Manalpha(1-6)[GlcNAbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)[Fucalpha(1-3)]GlcNAc-pyridylaminoside
show the reaction diagram
-, Q9ST97
6.2% activity compared to Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha1,6(Manalpha1,3)Manbeta-1-O-octyl
UDP + GlcNAc(1-2)Manalpha(1-6)Manalpha(1-3)Manbeta-1-O-octyl
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha1,6(Manalpha1,3)Manbeta-1-O-octyl
UDP + GlcNAcalpha(1-2)Manalpha(1-6)Manalpha(1-3)Manbeta-1-O-octyl
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha6(4-deoxy-Manalpha3)Man-beta-octyl
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha6(4-O-(5-iodoacetamidopentyl)-Manalpha3)Man-beta-octyl
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha6(4-O-methyl-Manalpha3)Man-beta-octyl
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha6(Manalpha3)Man-O-beta hexyl
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha6(Manalpha3)Man-O-beta(8-methoxycarbonyl)octyl
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha6(Manalpha3)Man-O-beta-octyl
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha6(Manalpha3)Man-O-beta4-N-acetyl-D-glucosamine
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha6(Manalpha3)Man-O-beta4-N-acetyl-D-glucosamine-beta4(L-fucose-alpha6)-N-acetyl-D-glucosamine-Asn
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha6(Manalpha3)Man-O-beta4-N-acetyl-D-glucosamine-beta4-N-acetyl-D-glucosamine
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosamine-beta2-Manalpha6(Manalpha3)Man-beta4-N-acetyl-D-glucosamine
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetylglucosamine-1,4-(fucose-1,6)-N-acetyl-glucosamine-Asn-peptide
UDP + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetylglucosamine-1,4-(fucose-1,6)-N-acetyl-glucosamine-Asn-peptide
show the reaction diagram
-
no activity
-
-
-
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
-
no activity
-
-
-
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
-
poor substrate
-
?
UDP-N-acetyl-D-glucosamine + ovalbumin
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + ovalbumin
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + ovalbumin
?
show the reaction diagram
-
best substrate, recombinant enzyme expressed in SF9 cells, unmodified and as tagged fusion protein
-
-
?
UDP-N-acetyl-D-glucosamine + ovalbumin
?
show the reaction diagram
-
substrate: glycopeptides prepared from ovalbumin
-
-
?
UDP-N-acetyl-D-glucosamine + ovalbumin glycopeptide III A-C
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + ovalbumin glycopeptide IV
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + ovalbumin glycopeptide V
UDP + ovalbumin glycopeptide IIIA
show the reaction diagram
-
best substrate
-
-
?
UDP-N-acetyl-D-glucosamine + ovalbumin glycopeptide V
UDP + ovalbumin glycopeptide IIIA
show the reaction diagram
-
best substrate
-
?
UDP-N-acetyl-D-glucosamine + ovalbumin glycopeptide V
UDP + ovalbumin glycopeptide IIIA
show the reaction diagram
-
physiological substrate
-
-
?
UDP-N-acetyl-D-glucosamine + R-Manalpha6(Manalpha3)Man-beta-octyl
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + [Manalpha(1-6)Manalpha(1-3)Manalpha(1-6)][Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-Asn
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + [Manalpha1,6(Manalpha1,3)Manalpha1,6](Manalpha1,3)Manbeta1,4GlcAcbeta1,4GlcNAc-R
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetylglucosamine + 3-(alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2-(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D-mannosyl-R
show the reaction diagram
-
-
-
-
-
UDP-N-acetylglucosamine + alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-1,4-N-acetyl-D-glucosaminyl-Asn-peptide
UDP + alpha-D-mannosyl-1,6-(alpha-D-mannosyl-1,3)-alpha-D-mannosyl-1,6-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
show the reaction diagram
-
regioselective and stereoselective addition of beta-1,2-N-acetylglucosamine to a high mannose oligosaccharide from yeast, room temperature, 2.7fold excess of UDP-N-acetylglucosamine over the oligosaccharide substrate, 20 mM HEPES, pH 7.5, 150 mM NaCl, 20 mM MnCl2
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
substrates: dolichol phosphate, asialo-bovine submaxillary mucin or galactosylated asialo-bovine submaxillary mucin, different specificities of transferase A and B, overview
-
-
-
additional information
?
-
-
acts on synthetic substrate analogues
-
-
-
additional information
?
-
-
substrates: free and protein-matrix-bound glycans
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
specificity for several synthetic acceptor substrate analogues, overview
-
-
-
additional information
?
-
-
enzyme initiates the biosynthesis of heparan sulfate
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
the enzyme catalyzes the first step in the conversion of oligomannose to complex or hybrid N-glycans of glycoproteins
-
-
-
additional information
?
-
-
the enzyme catalyzes the first step in the conversion of oligomannose to complex or hybrid N-glycans of glycoproteins
-
-
-
additional information
?
-
-
the enzyme is essential for processing of high-mannose to hybrid and complex N-glycans
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
high-level nonempirical calculations describe the mechanism, reaction pathway energetics, and structure of the transition state involved in the reaction catalyzed by GnT-I
-
-
-
additional information
?
-
-
no activity with alpha1,6-mannobiose
-
-
-
additional information
?
-
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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 + 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
-
stimulates galactosyltransferase of bovine milk
-
-
?
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
-
key enzyme of biosynthesis of complex and hybrid N-glycans
-
-
?
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
-
key enzyme of biosynthesis of complex and hybrid N-glycans
-
-
?
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
-
key enzyme of biosynthesis of complex and hybrid N-glycans
-
-
?
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
-
key enzyme of biosynthesis of complex and hybrid N-glycans
-
-
?
UDP-N-acetyl-D-glucosamine + ovalbumin glycopeptide V
UDP + ovalbumin glycopeptide IIIA
show the reaction diagram
-
physiological substrate
-
-
?
UDP-N-acetylglucosamine + 3-(alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2-(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D-mannosyl-R
show the reaction diagram
-
-
-
-
-
additional information
?
-
-
enzyme initiates the biosynthesis of heparan sulfate
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
the enzyme catalyzes the first step in the conversion of oligomannose to complex or hybrid N-glycans of glycoproteins
-
-
-
additional information
?
-
-
the enzyme catalyzes the first step in the conversion of oligomannose to complex or hybrid N-glycans of glycoproteins
-
-
-
additional information
?
-
-
the enzyme is essential for processing of high-mannose to hybrid and complex N-glycans
-
-
-
additional information
?
-
-
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ba2+
-
no activation
Ba2+
-
slight activation
Ca2+
-
slight activation
Ca2+
-
can substitute Mn2+
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
Cd2+
-
78% efficiency; activation
Cd2+
-
activation; can substitute for Mn2+ with 20%
Cd2+
-
activation
Co2+
-
91% efficiency; activation
Co2+
-
activation; can substitute for Mn2+ with 80%
Co2+
-
activation
Co2+
-
requirement
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
Co2+
-
Co2+, Mn2+ or Mg2+ required, Co2+ is most effective
Fe2+
-
activation; slight
Fe2+
-
activation; can substitute for Mn2+ with 65% efficiency
Fe2+
-
activation
Mg2+
-
61% efficiency; activation
Mg2+
-
activation; can substitute for Mn2+ with 40%
Mg2+
-
activation
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
Mg2+
-
Co2+, Mn2+ or Mg2+ required
Mn2+
-
requirement
Mn2+
-
18-26 mM; requirement
Mn2+
-
2 mM; requirement
Mn2+
-
requirement
Mn2+
-
requirement
Mn2+
-
requirement
Mn2+
-
25-100 mM; requirement
Mn2+
-
requirement
Mn2+
-
can also use Ca2+; requirement
Mn2+
-
20-80 mM; requirement
Mn2+
-
binds not independently of UDP-N-acetyl-D-glucose
Mn2+
-
requirement
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
Mn2+
-
Co2+, Mn2+ or Mg2+ required, optimal concentration is 50 mM
Mn2+
-
required for activity
Ni2+
-
34% efficiency; activation
Ni2+
-
activation; can substitute for Mn2+ with 20%
Ni2+
-
activation
Sn2+
-
slight activation
Zn2+
-
19% efficiency; activation
Zn2+
-
activation; can substitute for Mn2+ with 8%
Zn2+
-
activation
Mn2+
-, Q9ST97
maximal activity in the presence of 2 mM Mn2+
additional information
-
no activation by Cu2+; no activation by Hg2+
additional information
-
no activation by Cu2+; no activation by Sr2+, Pb2+
additional information
-, Q9ST97
not stimulated by Mg2+, Co2+, Ca2+, Zn2+ and C2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2'-O-Methyl-UDP
-
weak
alpha-D-Mannosyl-1,3-(alpha-D-mannosyl-1,6)-4-O-methyl-beta-D-mannosyl-1,4-N-acetyl-D-glucosamine
-
weak
alpha-D-mannosyl-1,6-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
-
Antibodies to pig liver N-acetylglucosaminyltransferase I
-
-
-
EDTA
-
3 mM
Manalpha6(6-O-(4,4-azopentyl)-Manalpha3)Man-beta-octyl
-
-
Manalpha6(6-O-(4,5-epoxypentyl)-Manalpha3)Man-beta-octyl
-
-
Manalpha6(6-O-(4-oxopentyl)-Manalpha3)Man-beta-octyl
-
-
Manalpha6(6-O-(5-pentanolyl)-Manalpha3)Man-beta-octyl
-
-
UDP-N-acetylgalactosamine
-
weak
UDP-N-acetylglucosamine
-
competitively to UDP
[Manalpha6(Manalpha3)][4-O-methyl-Man]-beta4-N-acetyl-D-glucosamine
-
-
Manalpha6(6-O-methyl-Manalpha3)Man-beta-octyl
-
-
additional information
-
high ionic strength, e.g. 0.1 M NaCl
-
additional information
-
no inhibitors are CDP, UDPhexanolamine, AMP
-
additional information
-
several inhibitory synthetic acceptor substrate analogues, overview; strategies for inhibitor design based on substrate specificities of the enzyme
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Triton X-100
-
-
Triton X-100
-
slight activation
Triton X-100
-
slight activation
Zwittergent 3-12
-
slight activation
CHAPS
-
slight activation
additional information
-
no activation by 2-mercaptoethanol
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.6
-
2-deoxy-Manalpha6(Manalpha3)Man-beta-octyl
-
-
1.2
-
3-O-(4,4-azopentyl)-Manalpha6(Manalpha3)Man-beta-octyl
-
-
1.8
-
3-O-(4,5-epoxypentyl)-Manalpha6(Manalpha3)Man-beta-octyl
-
-
1.4
-
3-O-(5-iodoacetamidopentyl)-Manalpha6(Manalpha3)Man-beta-octyl
-
-
3.5
-
3-O-pentyl-Manalpha6(Manalpha3)Man-beta-octyl
-
-
0.9
-
4-O-methyl-Manalpha6(Manalpha3)Man-beta-octyl
-
-
0.3
-
6-O-methyl-Manalpha6(Manalpha3)Man-beta-octyl
-
-
0.078
-
alpha-D-mannosyl-1,3-(alpha-D-mannosyl-1,6)-alpha-D-mannosyl-1,3-(alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-D-glucosamine
-
-
0.25
-
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
2.03
-
alpha-D-mannosyl-1,3-(alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-D-glucosamine
-
-
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
-
-
7.4
-
alpha-mannosyl-1,3-beta-mannosyl-1,4-N-acetylglucosamine
-
-
0.26
-
Man5GlcNAc2
P70680
wild-type CHO
0.483
-
Man5GlcNAc2
-
recombinant fusion protein
5.43
-
Man5GlcNAc2
P70680
mutant Lec1A
0.5
-
Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside
-, Q9ST97
recombinant enzyme, pH not specified in the publication, at 25C
-
22
-
Manalpha6(4-deoxy-Manalpha3)Man-beta-octyl
-
-
5
-
Manalpha6(4-O-(5-iodoacetamidopentyl)-Manalpha3)Man-beta-octyl
-
-
2.6
-
Manalpha6(4-O-methyl-Manalpha3)Man-beta-octyl
-
-
1.7
-
Manalpha6(Manalpha3)Man-O-beta hexyl
-
-
1.5
-
Manalpha6(Manalpha3)Man-O-beta(8-methoxycarbonyl)octyl
-
-
0.7
-
Manalpha6(Manalpha3)Man-O-beta-octyl
-
-
2.7
-
Manalpha6(Manalpha3)Man-O-beta4-N-acetyl-D-glucosamine
-
-
4.5
-
Manalpha6(Manalpha3)Man-O-beta4-N-acetyl-D-glucosamine
-
-
0.4
-
Manalpha6(Manalpha3)Man-O-beta4-N-acetyl-D-glucosamine-beta4(L-fucose-alpha6)-N-acetyl-D-glucosamine-Asn
-
-
1.9
-
N-acetyl-D-glucosamine-beta2-Manalpha6(Manalpha3)Man-beta4-N-acetyl-D-glucosamine
-
-
0.43
-
N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-pyridinylamine
-
-
-
10
-
N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
immunoglobulin G glycopeptide
0.44
-
ovalbumin
-
transferase A
-
4.5
-
ovalbumin
-
transferase B
-
0.12
-
ovalbumin glycopeptide V
-
-
-
0.33
-
ovalbumin glycopeptide V
-
transferase A
-
1.6
-
pyridylaminated Man3GlcNAc2
-
recombinant isozyme A
0.036
-
UDP-N-acetyl-D-glucosamine
-
-
0.0384
-
UDP-N-acetyl-D-glucosamine
-
-
0.046
-
UDP-N-acetyl-D-glucosamine
-
recombinant catalytic fragment
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
0.1
-
UDP-N-acetyl-D-glucosamine
-
-
0.17
-
UDP-N-acetyl-D-glucosamine
P70680
wild-type CHO
7.56
-
UDP-N-acetyl-D-glucosamine
P70680
mutant Lec1A
0.4
-
[Manalpha6(Manalpha3)Manalpha6][Manalpha3]Man-beta4-N-acetyl-D-glucosamine-beta4-N-acetyl-D-glucosamine-Asn
-
-
1.8
-
Manalpha6(Manalpha3)Man-O-beta4-N-acetyl-D-glucosamine-beta4-N-acetyl-D-glucosamine
-
-
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
-
additional information
-
additional information
-
interaction with bovine milk galactosyltransferase influences the Km-values
-
additional information
-
additional information
-
kinetic study
-
additional information
-
additional information
-
Km-values for several synthetic acceptor substrate analogues, overview
-
additional information
-
additional information
-
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
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
-
-
1.1
-
Manalpha6(6-O-(4,4-azopentyl)-Manalpha3)Man-beta-octyl
-
-
2.6
-
Manalpha6(6-O-(4,5-epoxypentyl)-Manalpha3)Man-beta-octyl
-
-
8.8
-
Manalpha6(6-O-(4-oxopentyl)-Manalpha3)Man-beta-octyl
-
-
10.2
-
Manalpha6(6-O-(5-pentanolyl)-Manalpha3)Man-beta-octyl
-
-
0.034
-
UDP-N-acetylglucosamine
-
-
13
-
[Manalpha6(Manalpha3)][4-O-methyl-Man]-beta4-N-acetyl-D-glucosamine
-
-
0.8
-
Manalpha6(6-O-methyl-Manalpha3)Man-beta-octyl
-
-
additional information
-
additional information
-
several inhibitory synthetic acceptor substrate analogues, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0000002
-
-
wild-type S49 cell
0.00000084
-
-
wild-type CHO cell
0.000015
-
-
transferase A, liver
0.00065
-
-
transferase B, hepatoma
0.079
-
-
alpha-D-mannosyl-1,3-(alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R immunoglobulin G glycopeptide
0.106
-
-
alpha1-acid glycoprotein treated with mild acid, beta-galactosidase and beta-N-acetylglucosamidase
0.48
-
-
room temperature, 2.7fold excess of UDP-N-acetylglucosamine over the oligosaccharide substrate, 20 mM HEPES, pH 7.5, 150 mM NaCl, 20 mM MnCl2
0.6
-
-
recombinant isozyme A
2.51
-
-
purified enzyme
3.37
-
-
purified enzyme
4.8
-
-
liver
19.8
-
-
low-molecular weight form
20
-
-
purified enzyme
additional information
-
-
in vivo assay of recombinant enzyme expressed in Sf9 cells with coexpressed fowl plague virus HA as endogenous substrate
additional information
-
P70680
wild-type and mutant cell lines
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
8
-
broad optimum
5.8
-
-
-
6
-
-
-
6
-
-
enzyme from testicular fluid
6.3
-
-
assay at
6.3
-
-, Q9ST97
-
6.5
-
-
recombinant fusion protein
7
-
-
recombinant catalytic fragment
7
-
-
enzyme from epididymal fluid
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
8.5
-, Q9ST97
activity decreases to less than 15% of the maximum at pH values lower than 5.0 and higher than 8.5
5.1
6.9
-
about half-maximal activity at pH 5.1 and about 70% of maximal activity at pH 6.9
6.5
9
-
recombinant fusion protein
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-, Q9ST97
-
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
40
-
-
recombinant fusion protein
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
45
-, Q9ST97
the activity decreases with increasing reaction temperature and is completely abolished at temperatures higher than 45C. On the other hand, substantial GnTI activity is detected at low temperatures, even at 0C (approximately 50% of the maximum)
0
70
-
recombinant fusion protein
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
two forms of beta 2-N-acetylglucosaminyltransferase I in rat testicular and epididymal fluids
Manually annotated by BRENDA team
-
wild-type and mutant F6 and F8
Manually annotated by BRENDA team
P70680
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
Manually annotated by BRENDA team
-
isozyme B, low content of isozyme A
Manually annotated by BRENDA team
-
diethylnitrosamine- or dimethylaminoazobenzene-induced hepatoma, Morris 5123D hepatoma or AH-109A, solid or ascitic
Manually annotated by BRENDA team
-
isozyme B, low content of isozyme A
Manually annotated by BRENDA team
-
isozymes A and B
Manually annotated by BRENDA team
-
isozymes A and B
Manually annotated by BRENDA team
-
no significant difference between the GnT I activities from dominant follicles collected before and after surge of luteinizing hormone
Manually annotated by BRENDA team
-
isozymes A and B
Manually annotated by BRENDA team
-
two forms of beta 2-N-acetylglucosaminyltransferase I in rat testicular and cauda epididymal fluids
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
transferase B, hepatoma
Manually annotated by BRENDA team
-
in recombinant Saccharomyces cerevisisae
Manually annotated by BRENDA team
-
resident type II transmembrane protein
Manually annotated by BRENDA team
-
in recombinant Saccharomyces cerevisisae
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
Golgi-localized N-acetylglucosaminyltransferase I is a determinant of osmotic stress tolerance in Arabidopsis thaliana
Manually annotated by BRENDA team
-
membrane-bound recombinant chimeras
Manually annotated by BRENDA team
-
in recombinant Saccharomyces cerevisisae
Manually annotated by BRENDA team
additional information
-
mammalian Golgi retention signal does not function in Saccharomyces cerevisiae cells
-
Manually annotated by BRENDA team
additional information
-
mesophyll protoplasts are created to analyze differences in localization
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
52000
-
-
SDS-PAGE
59000
-
-
SDS-PAGE
78000
-
-
mass of the fusion protein, free YFP-marker is about 27000 Da, SDS-PAGE
additional information
-
-
two MW-species
additional information
-
-
two MW-species of pig liver enzyme: major MW 52000 and minor MW 59000, SDS-PAGE
additional information
-
-
separable by gel filtration; two MW-species
additional information
-
-
-
additional information
-
-
2 domain protein, determination of acceptor substrate-, nucleotide sugar- and metal-binding sites
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
-
Q8VX56, -
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
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 58000 + x * 46000, SDS-PAGE
?
-
x * 45000 + x * 50000 + x * 54000, low molecular weight form, SDS-PAGE, major band: MW 45000
?
-
x * 46000, recombinant catalytic fragment, SDS-PAGE
?
-
x * 50000, recombinant enzyme, SDS-PAGE
?
-
x * 51000, recombinant, tagged protein, SDS-PAGE
?
-
x * 65000, recombinant isozyme B, SDS-PAGE
?
-
x * 56000, recombinant enzyme, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
one glycosylation site
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
glycoprotein
-
O-glycosylated
glycoprotein
-
one glycosylation site
no glycoprotein
-
recombinant catalytic fragment, no glycosylation sites
glycoprotein
Q8VX56, -
one glycosylation site
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
catalytic enzyme fragment in presence and absence of UDP-N-acetyl-D-glucosamine and Mn2+, hanging drop vapour diffusion method, protein 10 mg/ml + 10 mM MES, pH 5.5, + 270 mM KCl + 2 mM MnCl2, 10 mM UDP-N-acetyl-D-glucosamine, well-solution: 100 mM Tris-HCl, pH 7.9, 15-20% polyethylene glycol , X-ray structure determination and analysis
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
10
-, Q9ST97
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
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
45
-, Q9ST97
the activity is stable after a 2 h incubation at a temperature lower than 25C, but it significantly decreases after incubation at 35C and is completely abolished at temperatures higher than 45C
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
repeated freeze-thawing, stable to
-
freeze-thawing, solubilized enzyme, unstable to
-
repeated freeze-thawing, stable to
-
Triton X-100, 0.1%, and albumin, 0.01%, stabilize solubilized enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, in dilute solution, t1/2: 1 day
-
4C, in the presence of albumin, at least a month
-
-20C, 20% glycerol v/v, up to a year
-
4C, in 20% glycerol, 0.1% Triton X-100, 25 mM MES-buffer, pH 6.5, 10 mM MnCl2, 1 mM PMSF, 0.1 mM 6-aminocaproic acid and 0.02% NaN3, several months
-
-20C, at least 6 months
-
3C, at least a month
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
mutant enzyme D144N
-
partial
-
large scale, recombinant maltose-binding fusion protein
-
one Ni2+-NTA chromatography step is sufficient for oligosaccharide synthesis
-
amylose resin column chromatography, gel filtration
-, Q9ST97
recombinant catalytic fragment from Sf9 insect cells
-
two molecular weight forms separable by gel filtration, purification of low-molecular weight form
-
partial; two forms: transferase A and B, the latter only in hepatoma
-
recombinant N-terminally His-tagged protein from Escherichia coli
-
affinity chromatography
-
liver
-
recombinant glutathione S-transferase fusion isozymes and mutants from insect Sf21 cells
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cloning and DNA sequence determination and analysis
-
expression of the mutant enzyme D144N in insect cells
-
expression of YFP or CFP fusion enzyme of Arabidopsis and human N-acetylglucosaminyltransferase I, and the chimeric enzyme of Arabidopsis CTS region and human catalytic domain in mutant cgl1-1 Arabidopsis (lacking N-acetylglucosaminyltransferase I), transformed by Agrobacterium tumefaciens
-
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
-
cDNA clone, constructed type-II-surface membrane-protein/human transferase chimeras are transfected into Madin-Darby canine kidney cells
-
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 unmodified enzyme and as tagged fusion protein in Spodoptera frugiperda Sf9 cells via baculovirus infection, coexpression of fowl plague virus hemagglutinin HA as endogenous substrate for in vivo activity assay
-
human beta-1-2-N-acetylglucosaminyltransferase (hGnT1) lacking the first 103 amino acids is expressed as a maltose binding protein (MBP) fusion protein in inclusion bodies in Escherichia coli and refolded using an oxido-shuffling method. Cloning and expression of MBP-hGnT1(D103) and mutant MBP-hGnT1 (D103) enzymes
-
in one construct, the catalytic domain of human GNT I (abbreviated as NA) is fused to the MNN9 leader (abbreviated as 15) from Saccharomyces cerevisiae to yield construct NA15. In a second construct, a fungal codon-optimized form is combined with the same MNN9 leader to yield construct coNA15. Expression in Aspergillus nidulans and Aspergillus niger
-
Agrobacterium-mediated transformation of alfalfa
-
cloning and DNA sequence determination and analysis
-
the enzyme fused to maltose-binding protein is expressed in Escherichia coli Rosetta-gami B(DE3) cells
-, Q9ST97
expressed in CHO-DUKX-Lec1 cells
-
expression of catalytic fragment in Spodoptera frugiperda Sf9 cells via baculovirus infection
-
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
-
expressed in Chinese hamster ovary Lec1 mutant cells defective in endogeneous N-acetylglucosaminyltransferase I
-
expression in Saccharomyces cerevisiae, tagged with c-Myc epitope
-
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
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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
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cloning and DNA sequence determination and analysis
Q8VX56, -
cloning of isozymes A and B, 2 separate genes, DNA sequence determination and analysis; functional expression of isozymes A and B in Spodoptera frugiperda Sf21 cells as glutathione-S-transferase fusion proteins via baculovirus infection, isozyme B is folded less efficiently
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EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
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
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limited enzyme expression after anti-CD3 stimulation
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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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ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C907T
P70680
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
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
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
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
-
inactive
more.
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deleting seven C-terminal amino acids of the enzyme reduces enzymatic activity by 40%
P138L
-
inactive
C123R
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mutant enzyme does not show any activity in an HPLC analysis
G320D
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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
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isozyme B, improvement of properties of isozyme B to the level of isozyme A
D144N
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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
additional information
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natural point mutation contains mRNA but no enzyme activity
additional information
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AAA, ER steady-state location with little Golgi labelling; AAR, similar Golgi-targeting as wild-type; RAA, localisation in ER and Golgi membrane, more pronounced labeling in the ER; 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
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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
G634A
P70680
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
additional information
P70680
1 difference to published sequence with accession number U65791: C1340 is A1340
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
additional information
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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
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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
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
-
construction of antisense transgenic plants via Agrobacterium tumefaciens transfection of the own gene in antisense orientation, regulation analysis; transient transfection of isolated protoplasts of Arabidopsis thaliana defective mutant with cDNA in sense and antisense orientation
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
R415K
-
inactive
additional information
Q8VX56, -
construction of antisense transgenic plants via Agrobacterium tumefaciens transfection of the own gene in antisense orientation, regulation analysis; transient transfection of isolated protoplasts of Arabidopsis thaliana defective mutant with cDNA in sense and antisense orientation
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
biotechnology
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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
biotechnology
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production of glycoprotein therapeutics in recombinant Saccharomyces cerevisiae adapted to production of hybrid- and complex-type carbohydrates
medicine
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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