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Information on EC 2.4.1.143 - alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase and Organism(s) Rattus norvegicus and UniProt Accession Q09326

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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 activity initiates the synthesis of the second antenna of di-antennary complex N-glycans. While the natural substrate (produced by EC 3.2.1.114, mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase) is described here, the minimal substrate recognized by the enzyme is alpha-D-Man-(1->6)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)]-beta-D-Man-R.
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Rattus norvegicus
UNIPROT: Q09326
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The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
Synonyms
gntii, n-acetylglucosaminyltransferase ii, gnt ii, glcnac-t ii, gnt-ii, beta-1,2-n-acetylglucosaminyltransferase ii, gnt ii-a, gnt ii-b, tbgntii, n-acetylglucosaminyltransferase-ii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylglucosaminyltransferase II
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alpha-1,6-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase
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alpha-1,6-mannosylglycoprotein beta-1-2-N-acetylglucosaminyltransferase
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N-acetylglucosaminyltransferase II
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N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II
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UDP-GlcNAc:mannoside alpha1-6 acetylglucosaminyltransferase
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uridine diphosphoacetylglucosamine-alpha-1,6-mannosylglycoprotein beta-1-2-N-acetylglucosaminyltransferase
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uridine diphosphoacetylglucosamine-alpha-D-mannoside beta1-2-acetylglucosaminyltransferase
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uridine diphosphoacetylglucosamine-mannoside alpha1->6-acetylglucosaminyltransferase
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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->6)-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 activity initiates the synthesis of the second antenna of di-antennary complex N-glycans. While the natural substrate (produced by EC 3.2.1.114, mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase) is described here, the minimal substrate recognized by the enzyme is alpha-D-Man-(1->6)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)]-beta-D-Man-R.
CAS REGISTRY NUMBER
COMMENTARY hide
105913-04-0
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202420-38-0
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91755-74-7
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91847-11-9
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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 + 4-O-methyl-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-O-octyl
UDP + N-acetyl-beta-D-glucosaminyl-1,2-(4-O-methyl-alpha-D-mannosyl)-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-O-octyl
show the reaction diagram
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?
UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-6-deoxy-alpha-D-mannosyl-1,3)-beta-D-mannosyl-O-octyl
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-6-deoxy-alpha-D-mannosyl-1,3)-beta-D-mannosyl-O-octyl
show the reaction diagram
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?
UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetylglucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetylglucosaminyl-R
show the reaction diagram
UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-O-octyl
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-O-octyl
show the reaction diagram
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?
UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetylglucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetylglucosaminyl-R
show the reaction diagram
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essential for biosynthesis of complex N-linked oligosaccharides
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?
UDP-N-acetyl-D-glucosamine + dideoxytetrasaccharide
UDP + dideoxypentasaccharide
show the reaction diagram
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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 + alpha-D-mannosyl-1,6-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetylglucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetylglucosaminyl-R
show the reaction diagram
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essential for biosynthesis of complex N-linked oligosaccharides
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-Hg-UDP
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reversible
5-Hg-UDP-N-acetylglucosamine
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reversible
6-deoxy-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-O-octyl
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N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-beta-D-mannosyl-octyl
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O-(4,4-azo)pentyl-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-O-octyl
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.16
4-O-methyl-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-O-octyl
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37°C
0.55
alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-6-deoxy-alpha-D-mannosyl-1,3)-beta-D-mannosyl-O-octyl
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37°C
0.13
alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-O-octyl
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37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11.2
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4-O-methyl-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-O-octyl as substrate
21.4
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5-deoxy-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-O-octyl as substrate
7.8
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alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-O-octyl as substrate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MGAT2_RAT
442
1
51110
Swiss-Prot
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
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x * 42000, SDS-PAGE
43000
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x * 43000, x * 48000, SDS-PAGE, one or both of these bands represent the enzyme
48000
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x * 43000, x * 48000, SDS-PAGE, one or both of these bands represent the enzyme
additional information
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rat enzyme in crude extract exists in 2 forms, high-molecular weight form: above MW 200000, low-molecular weight form: MW 43000-48000, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Triton X-100 stabilizes
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, at least 6 months in 20% glycerol, 10 mM EDTA and 0.1% Triton X-100
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
solubilized with Triton X-100/NaCl, enzyme in crude extract exists in 2 molecular weight forms: purification of low-molecular weight form, affinity chromatography on Hg-UDP-N-acetylglucosamine-thiopropyl-Sepharose
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
construction of a Gnt II-expressing alg3 mutant strain of Pichia pastoris. Engineering of an artificial glycosylation pathway in Pichia pastoris blocked in dolichol oligosaccharide assembly
transient expression in COS-7 cells, linked in frame to a cDNA segment encoding the cleavable signal sequence of the human IL-2 receptor
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shao, M.C.; Wold, F.
The effect of the protein matrix on glycan processing in glycoproteins. Kinetic analysis of three rat liver Golgi enzymes
J. Biol. Chem.
263
5771-5774
1988
Rattus norvegicus
Manually annotated by BRENDA team
Alton, G.; Srivastava, G.; Kaur, K.J.; Hindsgaul, O.
Use of N-acetylglucosaminyltransferases I and II in the synthesis of a dideoxypentasaccharide
Bioorg. Med. Chem.
2
675-680
1994
Rattus norvegicus
Manually annotated by BRENDA team
Bendiak, B.; Schachter, H.
Control of glycoprotein synthesis. Purification of UDP-N-acetylglucosamine:alpha-D-mannoside beta 1-2 N-acetylglucosaminyltransferase II from rat liver
J. Biol. Chem.
262
5775-5783
1987
Rattus norvegicus
Manually annotated by BRENDA team
Schachter, H.; Chen, S.H.; Zhou, S.; Tan, J.; Yip, B.; Sarkar, M.; Spence, A.
Structure and function of the genes encoding N-acetylglucosaminyltransferases which initiate N-glycan antennae
Biochem. Soc. Trans.
25
875-880
1997
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Reck, F.; Meinjohanns, E.; Springer, M.; Wilkens, R.; Van Dorst, J.A.; Paulsen, H.; Moller, G.; Brockhausen, I.; Schachter, H.
Synthetic substrate analogues for UDP-GlcNAc: Man alpha 1-6R beta(1-2)-N-acetylglucosaminyltransferase II. Substrate specificity and inhibitors for the enzyme
Glycoconj. J.
11
210-216
1994
Rattus norvegicus
Manually annotated by BRENDA team
D'Agostaro, G.A.F.; Zingoni, A.; Moritz, R.L.; Simpson, R.J.; Schachter, H.; Bendiak, B.
Molecular cloning and expression of cDNA encoding the rat UDP-N-acetylglucosamine:alpha-6-D-mannoside beta-1,2-N-acetylglucosaminyltransferase II
J. Biol. Chem.
270
15211-15221
1995
Rattus norvegicus
Manually annotated by BRENDA team
Bobrowicz, P.; Davidson, R.C.; Li, H.; Potgieter, T.I.; Nett, J.H.; Hamilton, S.R.; Stadheim, T.A.; Miele, R.G.; Bobrowicz, B.; Mitchell, T.; Rausch, S.; Renfer, E.; Wildt, S.
Engineering of an artificial glycosylation pathway blocked in core oligosaccharide assembly in the yeast Pichia pastoris: Production of complex humanized glycoproteins with terminal galactose
Glycobiology
14
757-766
2004
Rattus norvegicus (Q09326)
Manually annotated by BRENDA team