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Information on EC 2.4.1.143 - alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
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EC Tree
2.4.1.143 alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferaseIUBMB 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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Word Map
- 2.4.1.143
- n-glycans
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carbohydrate-deficient
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complex-type
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dyserythropoietic
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oligomannose
- hempas
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schachter
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monoantennary
- phosphomannomutase
- synthesis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
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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beta-1,2-N-acetylglucosaminyltransferase II
EC 2.4.1.51
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formerly, part transferred
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GlcNAcT-II
GnT II
GnT-II
GnTII
Mgat2
N-acetylglucosaminyltransferase II
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II
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TbGnTII
TbGT15
UDP-GlcNAc:alpha6-D-mannoside beta1,2-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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N-acetylglucosaminyltransferase II
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein] = UDP + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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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.
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CAS REGISTRY NUMBER
COMMENTARY
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)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-D-Man-(1->6)-[beta-D-GlcNAc(1->2)-alpha-D-Man(1->3)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc + UDP-GlcNAc
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i.e. pyridylaminated MGn glycan, an intermediate during N-glycan processing
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?
UDP-alpha-D-GlcNAc + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
?
Gbeta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn glycan acceptor (GlcNAc-Man3-GlcNAc2-Asn) is used as acceptor substrate in enzyme assay, generated by enzymatic modification of a sialylglycopeptide (SGP) isolated from hen egg yolks and purified
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?
UDP-alpha-D-GlcNAc + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
UDP + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
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?
UDP-alpha-D-GlcNAc + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[VSG221 protein]
UDP + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[VSG221 protein]
UDP-GlcNAc + alpha-D-Man-(1->6)-[alpha-D-Man-(1->3)]-beta-D-Man(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc
UDP + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)-[alpha-D-Man-(1->3)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc
UDP-GlcNAc + GlcNAcMan3GlcNAc2-pyridylamine
UDP + GlcNAc2Man3GlcNAc2-pyridylamine
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?
UDP-N-acetyl-D-glucosamine + 3-deoxy-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta-octyl
UDP + GlcNAcbeta(1-2)3-deoxy-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta-octyl
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?
UDP-N-acetyl-D-glucosamine + 3-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-(3-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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?
UDP-N-acetyl-D-glucosamine + 3-O-methyl-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta-octyl
UDP + GlcNAcbeta(1-2)3-O-methyl-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta-octyl
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?
UDP-N-acetyl-D-glucosamine + 4-deoxy-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta-octyl
UDP + GlcNAcbeta(1-2)4-deoxy-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta-octyl
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?
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
UDP-N-acetyl-D-glucosamine + 4-O-methyl-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta-octyl
UDP + GlcNAcbeta(1-2)4-O-methyl-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta-octyl
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?
UDP-N-acetyl-D-glucosamine + 6-deoxy-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta-octyl
UDP + GlcNAcbeta(1-2)6-deoxy-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta-octyl
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?
UDP-N-acetyl-D-glucosamine + 6-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-(6-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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?
UDP-N-acetyl-D-glucosamine + 6-O-methyl-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta-octyl
UDP + GlcNAcbeta(1-2)6-O-methyl-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta-octyl
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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
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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
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-2-aminopyridine
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-2-aminopyridine
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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-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
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-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-R
the enzyme catalyzes an essential step in the biosynthetic pathway leading from high mannose to complex N-linked oligosaccharides
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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
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essential for biosynthesis of complex N-linked oligosaccharides
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?
UDP-N-acetyl-D-glucosamine + dideoxytetrasaccharide
UDP + dideoxypentasaccharide
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?
UDP-N-acetyl-D-glucosamine + Manalpha(1-6)(GlcNAcbeta(1-2)-6-deoxy-Manalpha(1-3))Manbeta-octyl
UDP + GlcNAcbeta(1-2)Manalpha(1-6)(GlcNAcbeta(1-2)-6-deoxy-Manalpha(1-3))Manbeta-octyl
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?
UDP-N-acetyl-D-glucosamine + Manalpha(1-6)(GlcNAcbeta(1-2)4-O-methyl-Manalpha(1-3))Manbeta-octyl
UDP + GlcNAcbeta(1-2)Manalpha(1-6)(GlcNAcbeta(1-2)4-O-methyl-Manalpha(1-3))Manbeta-octyl
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?
UDP-N-acetyl-D-glucosamine + Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))-4-deoxy-Manbeta-octyl
UDP + GlcNAcbeta(1-2)Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))-4-deoxy-Manbeta-octyl
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?
UDP-N-acetyl-D-glucosamine + Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta-octyl
UDP + GlcNAcbeta(1-2)Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta-octyl
UDP-N-acetyl-D-glucosamine + Manalpha(1->6)[GlcNAcbeta(1->2)-Manbeta(1->3)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridyl-aminoside
?
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the enzyme can transfer a second N-acetylglucosamine residue to the product of the first transferase reaction but in an extremely slow reaction that is unlikely to be biologically relevant
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?
UDP-alpha-D-GlcNAc + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[VSG221 protein]
UDP + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[VSG221 protein]
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?
UDP-alpha-D-GlcNAc + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[VSG221 protein]
UDP + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[VSG221 protein]
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?
UDP-GlcNAc + alpha-D-Man-(1->3)-alpha-D-Man-(1->6)-alpha-D-Man
?
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?
UDP-GlcNAc + alpha-D-Man-(1->3)-alpha-D-Man-(1->6)-alpha-D-Man
?
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?
UDP-GlcNAc + alpha-D-Man-(1->6)-[alpha-D-Man-(1->3)]-beta-D-Man(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc
UDP + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)-[alpha-D-Man-(1->3)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc
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?
UDP-GlcNAc + alpha-D-Man-(1->6)-[alpha-D-Man-(1->3)]-beta-D-Man(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc
UDP + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)-[alpha-D-Man-(1->3)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc
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?
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
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?
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
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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
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or 1,4-(+/-)-fucose-1,6-N-acetylglucosamine-pyridinylamine (with or without xylose in 1,2-beta-linkage to the beta-mannosyl residue)
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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
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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
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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
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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
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-
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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
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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
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-
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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
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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
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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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
R represents the remainder of the N-oligosaccharide core (n fucose), R: H or 1,4-(+/-)-fucose-1,6-N-acetylglucosaminyl-1-N-asparagine
-
?
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
-
acceptors are free and protein-matrix-bound glycans
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
best acceptor, high specificity
-
?
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
-
UDP-N-acetyl-D-glucosamine cannot be replaced by UDP-N-acetylgalactosamine, UDPgalactose, UDPxylose, UDPglucose or GDPfucose
-
?
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
-
no acceptor substrates: overview
-
?
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
-
-
-
-
?
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
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta-octyl
UDP + GlcNAcbeta(1-2)Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta-octyl
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta-octyl
UDP + GlcNAcbeta(1-2)Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta-octyl
-
-
-
?
additional information
?
-
-
the gene is alternatively spliced and developmmentally regulated
-
-
?
additional information
?
-
-
the enzyme is required for the chain initiation and elongation of the heparan sulfate backbone
-
-
?
additional information
?
-
binding structure of acceptor substrate and UDP, overview
-
-
-
additional information
?
-
-
binding structure of acceptor substrate and UDP, overview
-
-
-
additional information
?
-
the recombinant enzyme exhibits glycosyltransferase activity and strict substrate specificity. The acceptor substrate specificity of enzyme mutant HF-hGnTIIDELTA29 is examined using UDP-GlcNAc as a donor substrate and MM-PA, GnM-PA, GnGn-PA, and p-nitrophenyl-alpha-mannopyranoside as acceptor substrates instead of MGn-PA, overview
-
-
-
additional information
?
-
-
the recombinant enzyme exhibits glycosyltransferase activity and strict substrate specificity. The acceptor substrate specificity of enzyme mutant HF-hGnTIIDELTA29 is examined using UDP-GlcNAc as a donor substrate and MM-PA, GnM-PA, GnGn-PA, and p-nitrophenyl-alpha-mannopyranoside as acceptor substrates instead of MGn-PA, overview
-
-
-
additional information
?
-
-
the enzyme cannot use Man3GlcNAc2 and Manalpha(1->6)[Manbeta(1->3)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridyl-aminoside as substrate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-D-Man-(1->6)-[beta-D-GlcNAc(1->2)-alpha-D-Man(1->3)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc + UDP-GlcNAc
?
i.e. pyridylaminated MGn glycan, an intermediate during N-glycan processing
-
-
?
UDP-alpha-D-GlcNAc + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
UDP + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
-
-
-
?
UDP-alpha-D-GlcNAc + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[VSG221 protein]
UDP + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[VSG221 protein]
UDP-GlcNAc + alpha-D-Man-(1->6)-[alpha-D-Man-(1->3)]-beta-D-Man(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc
UDP + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)-[alpha-D-Man-(1->3)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc
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-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-R
the enzyme catalyzes an essential step in the biosynthetic pathway leading from high mannose to complex N-linked oligosaccharides
-
-
?
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
-
essential for biosynthesis of complex N-linked oligosaccharides
-
?
UDP-alpha-D-GlcNAc + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[VSG221 protein]
UDP + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[VSG221 protein]
-
-
-
?
UDP-alpha-D-GlcNAc + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[VSG221 protein]
UDP + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[VSG221 protein]
-
-
-
?
UDP-GlcNAc + alpha-D-Man-(1->3)-alpha-D-Man-(1->6)-alpha-D-Man
?
-
-
-
?
UDP-GlcNAc + alpha-D-Man-(1->3)-alpha-D-Man-(1->6)-alpha-D-Man
?
-
-
-
?
UDP-GlcNAc + alpha-D-Man-(1->6)-[alpha-D-Man-(1->3)]-beta-D-Man(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc
UDP + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)-[alpha-D-Man-(1->3)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc
-
-
-
?
UDP-GlcNAc + alpha-D-Man-(1->6)-[alpha-D-Man-(1->3)]-beta-D-Man(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc
UDP + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)-[alpha-D-Man-(1->3)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc
-
-
-
?
additional information
?
-
-
the gene is alternatively spliced and developmmentally regulated
-
-
?
additional information
?
-
-
the enzyme is required for the chain initiation and elongation of the heparan sulfate backbone
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
additional information
additional information
-
Ca2+, Co2+, Cu2+, Hg2+, Mg2+ or Zn2+ cannot replace Mn2+, at 1 or 2.5 mM each
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-deoxy-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-O-octyl
-
reversible inhibition
3-O-(4,4-azopentyl)-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Man-beta-octyl
-
-
3-O-(5-aminopentyl)-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Man-beta-octyl
-
-
6-deoxy-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-O-octyl
-
-
N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-beta-D-mannosyl-octyl
-
-
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
O-(5-amino)pentyl-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-O-octyl
-
reversible inhibition
O-(5-iodoacetamido)pentyl-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-O-octyl
-
irreversible inhibition
O-pentyl-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-O-octyl
-
reversible inhibition
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
-
irreversible inhibition
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
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
alpha-1,6-mannosyl-glycoprotein 2-beta-n-acetylglucosaminyltransferase deficiency
Carbohydrate-deficient glycoprotein syndrome type II. An autosomal recessive N-acetylglucosaminyltransferase II deficiency different from typical hereditary erythroblastic multinuclearity, with a positive acidified-serum lysis test (HEMPAS).
alpha-1,6-mannosyl-glycoprotein 2-beta-n-acetylglucosaminyltransferase deficiency
Hypoglycosylation of a brain glycoprotein (beta-trace protein) in CDG syndromes due to phosphomannomutase deficiency and N-acetylglucosaminyl-transferase II deficiency.
Anemia
Primary defect of congenital dyserythropoietic anemia type II. Failure in glycosylation of erythrocyte lactosaminoglycan proteins caused by lowered N-acetylglucosaminyltransferase II.
Anemia, Dyserythropoietic, Congenital
Defective glycosylation of erythrocyte membrane glycoconjugates in a variant of congenital dyserythropoietic anemia type II: association of low level of membrane-bound form of galactosyltransferase.
Anemia, Dyserythropoietic, Congenital
HEMPAS. Hereditary erythroblastic multinuclearity with positive acidified serum lysis test.
Anemia, Dyserythropoietic, Congenital
Incomplete synthesis of N-glycans in congenital dyserythropoietic anemia type II caused by a defect in the gene encoding alpha-mannosidase II.
Anemia, Dyserythropoietic, Congenital
Primary defect of congenital dyserythropoietic anemia type II. Failure in glycosylation of erythrocyte lactosaminoglycan proteins caused by lowered N-acetylglucosaminyltransferase II.
Congenital Disorders of Glycosylation
Carbohydrate-deficient glycoprotein syndrome type II. An autosomal recessive N-acetylglucosaminyltransferase II deficiency different from typical hereditary erythroblastic multinuclearity, with a positive acidified-serum lysis test (HEMPAS).
Infections
Engineering the baculovirus genome to produce galactosylated antibodies in lepidopteran cells.
Neuroblastoma
Knockdown of N-Acetylglucosaminyltransferase-II Reduces Matrix Metalloproteinase 2 Activity and Suppresses Tumorigenicity in Neuroblastoma Cell Line.
phosphomannomutase deficiency
Hypoglycosylation of a brain glycoprotein (beta-trace protein) in CDG syndromes due to phosphomannomutase deficiency and N-acetylglucosaminyl-transferase II deficiency.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
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
-
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
-
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
-
37°C
0.0166 - 0.19
alpha-D-mannosyl-1,6-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetylglucosaminyl-R
0.062 - 0.557
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
0.0166
alpha-D-mannosyl-1,6-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetylglucosaminyl-R
-
pH 6.5
0.1
alpha-D-mannosyl-1,6-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetylglucosaminyl-R
-
37°C
0.19
alpha-D-mannosyl-1,6-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-1,4-N-acetylglucosaminyl-R
-
pH 6.5, 37°C
0.062
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
pH 7.0, 37°C, recombinant wild-type mutant expressed from HEK-293F cells
0.0782
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
pH 7.0, 37°C, recombinant wild-type mutant expressed from HEK-293S cells
0.115
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
pH 7.0, 37°C, recombinant mutant N318A
0.145
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
pH 7.0, 37°C, recombinant mutant Y294A
0.17
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
pH 7.0, 37°C, recombinant mutant W346A
0.223
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
pH 7.0, 37°C, recombinant mutant R198A
0.29
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
pH 7.0, 37°C, recombinant mutant E259A
0.557
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
pH 7.0, 37°C, recombinant mutant Y344A
0.295
UDP-alpha-D-GlcNAc
pH 7.0, 37°C, recombinant wild-type mutant expressed from HEK-293S cells
0.349
UDP-alpha-D-GlcNAc
pH 7.0, 37°C, recombinant wild-type mutant expressed from HEK-293F cells
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000083 - 1.003
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
0.000083
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
pH 7.0, 37°C, recombinant mutant E259A
0.0023
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
pH 7.0, 37°C, recombinant mutant Y344A
0.005
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
pH 7.0, 37°C, recombinant mutant W346A
0.05
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
pH 7.0, 37°C, recombinant mutant N318A
0.137
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
pH 7.0, 37°C, recombinant mutant R198A
0.167
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
pH 7.0, 37°C, recombinant mutant Y294A
0.682
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
pH 7.0, 37°C, recombinant wild-type mutant expressed from HEK-293S cells
1.003
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
pH 7.0, 37°C, recombinant wild-type mutant expressed from HEK-293F cells
0.593
UDP-alpha-D-GlcNAc
pH 7.0, 37°C, recombinant wild-type mutant expressed from HEK-293S cells
0.773
UDP-alpha-D-GlcNAc
pH 7.0, 37°C, recombinant wild-type mutant expressed from HEK-293F cells
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00029 - 16.18
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
0.00029
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
pH 7.0, 37°C, recombinant mutant E259A
0.0041
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
pH 7.0, 37°C, recombinant mutant Y344A
0.029
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
pH 7.0, 37°C, recombinant mutant W346A
0.435
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
pH 7.0, 37°C, recombinant mutant N318A
0.614
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
pH 7.0, 37°C, recombinant mutant R198A
1.152
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
pH 7.0, 37°C, recombinant mutant Y294A
8.72
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
pH 7.0, 37°C, recombinant wild-type mutant expressed from HEK-293S cells
16.18
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn
pH 7.0, 37°C, recombinant wild-type mutant expressed from HEK-293F cells
2.01
UDP-alpha-D-GlcNAc
pH 7.0, 37°C, recombinant wild-type mutant expressed from HEK-293S cells
2.22
UDP-alpha-D-GlcNAc
pH 7.0, 37°C, recombinant wild-type mutant expressed from HEK-293F cells
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
3-O-(4,4-azopentyl)-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Man-beta-octyl
-
-
2.5
3-O-(5-aminopentyl)-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Man-beta-octyl
-
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11.2
-
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 as substrate
21.4
-
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
-
alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-O-octyl as substrate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 6.5
6.5 - 7
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.7 - 8.1
-
the enzyme has an optimum pH of 6.7, with a broad shoulder of high activity from pH 7.1 to 8.1
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
Mgat2 enzymatic activity, but not mRNA transcript levels, differ significantly among the three strains (PL/J C57BL/6 129/Sv)
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
gene is expressed in the early stages of development mainly in the nervous system
brenda
additional information
-
reduction of N-acetylglucosaminyltransferase II in hyperkeratotic skin of ichthyosis patients
brenda
additional information
enzyme TbGT15 is predominantly expressed in bloodstream form parasites
brenda
additional information
-
enzyme TbGT15 is predominantly expressed in bloodstream form parasites
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GnTII is a Golgi-localized type II transmembrane enzyme
brenda
TbGT15 is a type II transmembrane protein and its sequence contains a dibasic motif, which functions as an endoplasmic reticulum exit signal
brenda
-
TbGT15 is a type II transmembrane protein and its sequence contains a dibasic motif, which functions as an endoplasmic reticulum exit signal
-
brenda
enzyme exhibits a type II transmembrane protein topology with a putative N-terminal cytoplasmic tail of 9 amino acids followed by transmembrane domain of 18 residues, and a C-terminal luminal domain of 405 residues
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
compared with the structure of human GnTII, the amino acid residues involved in catalytic activity and substrate recognition are almost fully conserved in Bombyx mori GnTII, which is consistent with its enzymatic properties
evolution
enzyme TbGT15 belongs to the trypanosome beta3-glycosyltransferase superfamily
evolution
MGAT2 has been characterized from mammalian, plant, and insect sources, enzyme structure comparisons, overview
evolution
-
enzyme TbGT15 belongs to the trypanosome beta3-glycosyltransferase superfamily
-
malfunction
deletion of TbGT15 is accompanied by the absence of complex N-glycans, as well as alterations in the biosynthesis of the giant poly-Lac-dently from prior TbGnTI action, which is in contrast to canonical GnTIIs that only use substrates after modification by GnTI, i.e. Manalpha1-6(GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc
malfunction
human deficiency in MGAT2 leads to carbohydrate-deficient glycoprotein syndrome type IIa (CDG IIa) characterized by facial dysmorphy, ventricular septal defects, and severely retarded psychomotor development. To date, five MGAT2 mutations have been identified in CDG IIa patients, all residing within the catalytic domain (H262R, S290F, N318D, C339ter, and K237N). Four of the mutations (H262R, S290F, N318D, C339ter) exhibit significantly reduced (compound heterozygote N318D:C339ter) or a complete absence of enzyme activity (H262R, S290F). Three of the residues are nonconserved (H262, N318, and K237), and N318 and K237 H-bond directly or indirectly with the UDP-GlcNAc donor. The S290 is a conserved residue that stabilizes the core of the GT-A fold through H-bonds to peptide bond backbone residues. The H262R, S290F, and K237N mutations break these critical hydrogen bonds and introduce steric clashes to destabilize the protein. The isosteric N318D mutation results in reduced activity similar to the 30 to 37fold reduction in kcat/Km for the N318A
malfunction
-
deletion of TbGT15 is accompanied by the absence of complex N-glycans, as well as alterations in the biosynthesis of the giant poly-Lac-dently from prior TbGnTI action, which is in contrast to canonical GnTIIs that only use substrates after modification by GnTI, i.e. Manalpha1-6(GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc
-
metabolism
-
the enzyme functions at the N-glycan processing branch point and is one of the major factors determining the net outcome of the insect cell N-glycosylation pathway
metabolism
Asn-linked oligosaccharides are extensively modified during transit through the secretory pathway, first by trimming of the nascent glycan chains and subsequently by initiating and extending multiple oligosaccharide branches from the trimannosyl glycan core. Trimming and branching pathway steps are highly ordered and hierarchal based on the precise substrate specificities of the individual biosynthetic enzymes. A key committed step in the synthesis of complex-type glycans is catalyzed by N-acetylglucosaminyltransferase II (MGAT2), an enzyme that generates the second GlcNAcbeta1,2- branch from the trimannosyl glycan core using UDPGlcNAc as the sugar donor. Enzymatic steps required for the synthesis of the complex-type structures, processing of N-glycans from Man9GlcNAc2 to complex-type structures includes GlcNAc addition by MGAT1, Man trimming by MAN2A1, and GlcNAc addition by MGAT2, pathway overview
metabolism
beta-1,2-N-acetylglucosaminyltransferase II is a key enzyme for complex-type N-glycan biosynthesis. Both insect and mammalian cells produce Man(alpha1->6)[GlcNAc(beta1->2)Man(alpha1->3)]Man(beta1->4)GlcNAc(beta1->4)GlcNAc (MGn) glycan as an intermediate during N-glycan processing. In insect cells, beta-N-acetylglucosaminidase (fused lobes, FDL) removes a GlcNAc residue of the alpha1-3 arm of MGn glycan to produce Man(alpha1->6)[Man(alpha1->3)]ManGlcNAc2 (MM), a core structure from paucimannose-type N-glycans
metabolism
N-acetylglucosaminyltransferase I or II initiate the elaboration of the Manalpha1-3 and Manalpha1-6 arms, respectively, of the conserved trimannosyl-N-acetylchitobiosyl core of N-linked glycans. Proposed scheme for poly-LacNAc-containing N-glycans of bloodstream form trypanosomes, overview
metabolism
-
N-acetylglucosaminyltransferase I or II initiate the elaboration of the Manalpha1-3 and Manalpha1-6 arms, respectively, of the conserved trimannosyl-N-acetylchitobiosyl core of N-linked glycans. Proposed scheme for poly-LacNAc-containing N-glycans of bloodstream form trypanosomes, overview
-
physiological function
beta-1,2-N-acetylglucosaminyltransferase II (GnTII) catalyzes the transfer of GlcNAc from a UDP-GlcNAc donor to the alpha1-6 arm of MGn glycan to produce biantennary complex-type glycans in mammalian cells
physiological function
beta-1,2-N-acetylglucosaminyltransferase II (GnTII) is a Golgi-localized type II transmembrane enzyme that catalyzes the transfer of N-acetylglucosamine to the 6-arm of the trimanosyl core of N-glycans, an essential step in the conversion of oligomannose-type to complex-type N-glycans
physiological function
TbGT15 is the glycosyltransferase responsible for the transfer of beta1-2-linked GlcNAc to the alpha1-6-linked alpha-D-mannopyranosyl residue of Manalpha1-6(Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc. The enzyme initiates the elaboration of the Manalpha1-6 arms of the conserved trimannosyl-N-acetylchitobiosyl core of N-linked glycans, structure and biosynthesis of complex N-glycans in the human pathogen are analyzed, and the adaptation by trypanosomes of beta3-glycosyltransferase family members to catalyze beta-1-2 glycosidic linkages is demonstrated. TbGT15 is a non-essential gene in Trypanosoma brucei bloodstream form cells
physiological function
-
TbGT15 is the glycosyltransferase responsible for the transfer of beta1-2-linked GlcNAc to the alpha1-6-linked alpha-D-mannopyranosyl residue of Manalpha1-6(Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc. The enzyme initiates the elaboration of the Manalpha1-6 arms of the conserved trimannosyl-N-acetylchitobiosyl core of N-linked glycans, structure and biosynthesis of complex N-glycans in the human pathogen are analyzed, and the adaptation by trypanosomes of beta3-glycosyltransferase family members to catalyze beta-1-2 glycosidic linkages is demonstrated. TbGT15 is a non-essential gene in Trypanosoma brucei bloodstream form cells
-
additional information
Rossmann-like fold that employs conserved divalent cation-dependent substrate interactions with the UDP-GlcNAc donor. MGAT2 interactions with the extended glycan acceptor are distinct from other related glycosyltransferases. These interactions are composed of a catalytic subsite that binds the Man-(alpha1,6)- monosaccharide acceptor and a distal exosite pocket that binds the GlcNAc-beta1,2Man-alpha1,3Manbeta- substrate recognition arm. Substrate binding by MGAT2 employs both conserved and convergent catalytic subsite modules to provide substrate selectivity and catalysis. More broadly, the MGAT2 active-site architecture demonstrates how glycosyltransferases create complementary modular templates for regiospecific extension of glycan structures in mammalian cells. The enzyme MGAT2 employs a UDP-GlcNAc donor in a Mn2+-dependent inverting catalytic mechanism. structural basis for substrate recognition by MGAT2, structure-function analysis, structure comparisons, catalytic mechanism, detailed overview
additional information
-
Rossmann-like fold that employs conserved divalent cation-dependent substrate interactions with the UDP-GlcNAc donor. MGAT2 interactions with the extended glycan acceptor are distinct from other related glycosyltransferases. These interactions are composed of a catalytic subsite that binds the Man-(alpha1,6)- monosaccharide acceptor and a distal exosite pocket that binds the GlcNAc-beta1,2Man-alpha1,3Manbeta- substrate recognition arm. Substrate binding by MGAT2 employs both conserved and convergent catalytic subsite modules to provide substrate selectivity and catalysis. More broadly, the MGAT2 active-site architecture demonstrates how glycosyltransferases create complementary modular templates for regiospecific extension of glycan structures in mammalian cells. The enzyme MGAT2 employs a UDP-GlcNAc donor in a Mn2+-dependent inverting catalytic mechanism. structural basis for substrate recognition by MGAT2, structure-function analysis, structure comparisons, catalytic mechanism, detailed overview
additional information
the enzyme sequence contains a DXD motif, which is generally involved in catalytic activity of known GTs
additional information
-
the enzyme sequence contains a DXD motif, which is generally involved in catalytic activity of known GTs
-
Show AA Sequence and Transmembrane Helices (2043 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
43000
-
x * 43000, x * 48000, SDS-PAGE, one or both of these bands represent the enzyme
48000
-
x * 43000, x * 48000, SDS-PAGE, one or both of these bands represent the enzyme
additional information
-
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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
-
x * 43000, x * 48000, SDS-PAGE, one or both of these bands represent the enzyme
additional information
modular architecture for GT substrate interactions, overview
additional information
-
modular architecture for GT substrate interactions, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
analysis of N-glycan attached to HF-hGnTIIDELTA29 mutant enzyme recombinantly expressed in silkworm using Endoglycosidase H (Endo H) and peptide:N-glycanase F (PNGase F)
glycoprotein
N-glycosylation and the binding of UDP, Mn2+, and GlcNAcMan3GlcNAc2 in the MGAT2 structure, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant catalytic domain of MGAT2 at 20 mg/ml in 5 mM MnCl2, 10 mM HEPES, pH 7.0, 50 mM NaCl, 200 mM betaine, and 10% glycerol is crystallized using hanging drop vapor diffusion method from a reservoir of 1.4 M ammonium sulfate. Crystals grow in 8-12 weeks and are derivatized with uranium oxide for phasing. The crystals are transferred to the reservoir solution supplemented with 20% cryoprotectant (2:2:1 ratio of ethylene glycol:DMSO:glycerol). MGAT2:UO2 crystallizes in space group P43212. For the UDP complex (MGAT2:UDP), 20 mg/ml of protein containing 5 mM UDP, 5 mM MnCl2, 10 mM HEPES, pH 7.0, 50 mM NaCl, 200 mM betaine and 10% glycerol produces multinucleated crystals from a reservoir containing 1.9 M ammonium sulfate, 100 mM HEPES at pH 7.5. Crystal seeding and optimization produce single crystals from a reservoir containing 1.7 M ammonium sulfate, 100 mM HEPES, pH 7.5, 5 mM UDP, and 5 mM MnCl2. Crystals are transferred to a reservoir solution supplemented with 20% cryoprotectant (2:2:1 ratio of ethylene glycol, DMSO, and glycerol). MGAT2:UDP crystallizes in P21. For the acceptor complex (MGAT2:Acc), 20 mg/ml of protein in 5 mM acceptor (GlcNAc-Man3-GlcNAc2-Asn), 10 mM HEPES, pH 7.0, 50 mM NaCl, 200 mM betaine and 10% glycerol, is crystallized from 1.6 M ammonium sulfate, 100 mM HEPES, pH 7.5, using the MGAT2:UDP crystals as the initial seed stock and MGAT2:Acc crystals as the final seed stock. The crystals are cryoprotected with the reservoir solution supplemented with 5 mM acceptor, 1.6 M ammonium sulfate, 100 mM HEPES, pH 7.5, and 20% cryoprotectant (2:2:1 ratio of ethylene glycol, DMSO and glycerol). MGAT2:Acc crystallizes in P22121. X-ray diffraction structure determination and analysis at 2.0 A, 1.6 A, and 2.8 A resolution, respectively
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D217A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
E259
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
N318A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
R198A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
W346A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
Y294A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
Y344A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
additional information
additional information
construction of a vector including the N-terminally FLAG (DYKDDDDK)-tagged lumenal region (Leu27eAla498) including the stem domain and the catalytic domain of BmGnTII together with a signal peptide sequence from bombyxin and transformed into Escherichia coli BmDH10Bac-CP--Chi- competent cells, which contain the cysteine protease- and chitinase-deficient BmNPV bacmid. RT-PCR expression analysis. The cDNA templates are synthesized from total RNAs extracted from whole bodies of first to fifth-instar larvae and pupa and tissues of fifth-instar larvae. Tissues used are as follows: fat body, midgut, silk gland, epidermis, and Malpighian tubule. To produce the soluble form of BmGnTII n hemolymph, chitosan/BmNPV bacmid nanocomplexes are prepared and then injected into fifth-instar silkworm larvae. The bacmid-injected larvae are reared on an artificial diet
additional information
-
construction of a vector including the N-terminally FLAG (DYKDDDDK)-tagged lumenal region (Leu27eAla498) including the stem domain and the catalytic domain of BmGnTII together with a signal peptide sequence from bombyxin and transformed into Escherichia coli BmDH10Bac-CP--Chi- competent cells, which contain the cysteine protease- and chitinase-deficient BmNPV bacmid. RT-PCR expression analysis. The cDNA templates are synthesized from total RNAs extracted from whole bodies of first to fifth-instar larvae and pupa and tissues of fifth-instar larvae. Tissues used are as follows: fat body, midgut, silk gland, epidermis, and Malpighian tubule. To produce the soluble form of BmGnTII n hemolymph, chitosan/BmNPV bacmid nanocomplexes are prepared and then injected into fifth-instar silkworm larvae. The bacmid-injected larvae are reared on an artificial diet
additional information
construction of an enzyme mutant HF-hGnTIIDELTA29 lacking the N-terminal cytosolic tail and transmembrane region
additional information
-
construction of an enzyme mutant HF-hGnTIIDELTA29 lacking the N-terminal cytosolic tail and transmembrane region
additional information
MGAT2 catalytic domain expression construct (residues 29-447) is generated by replacement of the NH2-terminal membrane anchor with a fusion peptide cassette to target the secretion of the recombinant fusion protein product in mammalian cells
additional information
-
MGAT2 catalytic domain expression construct (residues 29-447) is generated by replacement of the NH2-terminal membrane anchor with a fusion peptide cassette to target the secretion of the recombinant fusion protein product in mammalian cells
additional information
gene replacement strategy is used to create TbGT15 null mutant cells and subsequent insertion of tetracycline-inducible ectopic copy. Constructs for gene replacement and ectopic expression are stably transformed into Trypanosoma brucei bloodstream form cells (strain 427, variant 221). Mouse infectivity studies with wild-type and TbGT15 null mutant bloodstream form trypanosomes. No morphological differences between the wild-type and TbGT15 null mutant parasites are ascertained by light microscopy or by scanning electron microscopy. Compared with wild-type cells, the TbGT15 null mutant parasites exhibit slightly slower growth kinetics in vitro, and this mild growth phenotype is partially reversed in TbGT15 conditional null cells grown under permissive conditions. In addition, no difference in its ability to infect mice can be detected for the TbGT15 null mutant. Mutant phenotype, overview
additional information
-
gene replacement strategy is used to create TbGT15 null mutant cells and subsequent insertion of tetracycline-inducible ectopic copy. Constructs for gene replacement and ectopic expression are stably transformed into Trypanosoma brucei bloodstream form cells (strain 427, variant 221). Mouse infectivity studies with wild-type and TbGT15 null mutant bloodstream form trypanosomes. No morphological differences between the wild-type and TbGT15 null mutant parasites are ascertained by light microscopy or by scanning electron microscopy. Compared with wild-type cells, the TbGT15 null mutant parasites exhibit slightly slower growth kinetics in vitro, and this mild growth phenotype is partially reversed in TbGT15 conditional null cells grown under permissive conditions. In addition, no difference in its ability to infect mice can be detected for the TbGT15 null mutant. Mutant phenotype, overview
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 50
-
splice variants GNTII-A, -B, -C, and -D show 70.3%, 81.9%, 44.4% and 91.9% relative activity after 1 h at 30, 50, 40 and 50°C, respectively
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, several weeks in 20% glycerol, 0.0005 mM DTT and 0.1% Triton X-100
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant soluble His-FLAG-tagged hGnTII from silkworm larval hemolymph in tandem affinity purification and ultrafiltration
recombinant wild-type and mutant His-tagged MGAT2 catalytic domains from HEK293 cells by nickel affinity chromatography, cleavage of fusion tags by recombinant TEV protease, and trimming of glycan structures to a single GlcNAc residue by EndoF1, followed by gel filtration, and ultrafiltration
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
a transformed insect cell line (Tn5beta4GalT) constitutively expresses a mammalian beta-1,4-galactosyltransferase and human beta-1,2-N-acetylglucosaminyltransferase II under the control of an immediate-early promoter. The baculovirus-host system can be used to produce a recombinant glycoprotein with fully galactosylated, biantennary N-glycans
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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
construction of a silkworm-based Bombyx mori nucleopolyhedrovirus bacmid expression system, and functional expression of His-FLAG-tagged human GnTII (hGnTII) lacking the N-terminal cytosolic tail and transmembrane region. The enzyme is secreted. The enzyme expressed in silkworm is glycosylated, the structure of N-glycans in the recombinant hGnTII is suggested to be of the complex type, pauci-mannosidic-type glycans, and the removal of the glycans does not affect the enzymatic activity
DNA and amino acid sequence determination and analysis, TbGT15 is present as a single copy per haploid genome, recombinant overexpression of full-length TbGT15 with a C-terminal 3x HA epitope tag, semi-quantitative RT-PCR enzyme expression analysis
expressed in Spodoptera frugiperda and Trichoplusia ni cells by using a baculovirus expression vector
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expression as fusion protein vHis-GlcNAc-TII in Spodoptera frugiperda Sf-9 cells
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gene GnTII, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, functional expression of the enzyme using a silkworm-based Bombyx mori nucleopolyhedrovirus bacmid expression system, the enzyme is secreted. The recombinant enzyme exhibits similar pH and temperature dependency and the same substrate specificity as human GnTII expressed by the same system, but deglycosylation with peptide:N-glycanase F does not affect its enzymatic activity. Construction of a vector including the N-terminally FLAG (DYKDDDDK)-tagged lumenal region (Leu27eAla498) including the stem domain and the catalytic domain of BmGnTII together with a signal peptide sequence from bombyxin and transformed into Escherichia coli BmDH10Bac-CP-/Chi- competent cells, which contain the cysteine protease- and chitinase-deficient BmNPV bacmid. RT-PCR expression analysis. The cDNA templates are synthesized from total RNAs extracted from whole bodies of first to fifth-instar larvae and pupa and tissues of fifth-instar larvae. Tissues used are as follows: fat body, midgut, silk gland, epidermis, and Malpighian tubule. To produce the soluble form of BmGnTII n hemolymph, chitosan/BmNPV bacmid nanocomplexes are prepared and then injected into fifth-instar silkworm larvae. The bacmid-injected larvae are reared on an artificial diet
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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transient recombinant expression of wild-type and mutant His-tagged MGAT2s' catalytic domain (residues 29-447) in HEK293S (GnTI-) or HEK293F (wild-type) cells. The fusion protein construct encodes an NH2-terminal signal sequence, His8-tag, AviTag, superfolder GFP, the TEV protease recognition site, and the truncated MGAT2 coding region behind a CMV promoter
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
the baculoviris-host system constitutively expressing beta-1,4-galactosyltransferase and beta-1,2-N-acetylglucosaminyltransferase II can be used to produce a recombinant glycoprotein with fully galactosylated, biantennary N-glycans
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tezuka, K.; Hayashi, M.; Ishihara, H.; Akazawa, T.; Takahashi, N.
Studies on synthetic pathway of xylose-containing N-linked oligosaccharides deduced from substrate specificities of the processing enzymes in sycamore cells (Acer pseudoplatanus L.)
Eur. J. Biochem.
203
401-413
1992
Acer pseudoplatanus
brenda
Harpaz, N.; Schachter, H.
Control of glycoprotein synthesis. Bovine colostrum UDP-N-acetylglucosamine:alpha-D-mannoside beta 2-N-acetylglucosaminyltransferase I. Separation from UDP-N-acetylglucosamine:alpha-D-mannoside beta 2-N-acetylglucosaminyltransferase II, partial purification, and substrate specificity
J. Biol. Chem.
255
4885-4893
1980
Bos taurus
brenda
Oppenheimer, C.L.; Eckhardt, A.E.; Hill, R.L.
The nonidentity of porcine N-acetylglucosaminyltransferases I and II
J. Biol. Chem.
256
11477-11482
1981
Sus scrofa
brenda
Shao, M.C.; Wold, F.
The effect of the protein matrix on glycan processing in glycoproteins. Kinetic analysis of three rat liver Golgi enzymes
J. Biol. Chem.
263
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1988
Rattus norvegicus
brenda
Schachter, H.; Brockhausen, I.; Hull, E.
High-performance liquid chromatography assays for N-acetylglucosaminyltransferases involved in N- and O-glycan synthesis
Methods Enzymol.
179
351-397
1989
Gallus gallus, Mesocricetus auratus
brenda
Fritz, T.A.; Gabb, M.M.; Wei, G.; Esko, J.D.
Two N-acetylglucosaminyltransferases catalyze the biosynthesis of heparan sulfate
J. Biol. Chem.
269
28809-28814
1994
Oncorhynchus mykiss
brenda
Altmann, F.; Kornfeld, G.; Dalik, T.; Staudacher, E.; Glossl, J.
Processing of asparagine-linked oligosaccharides in insect cells. N-acetylglucosaminyltransferase I and II activities in cultured lepidopteran cells
Glycobiology
3
619-625
1993
Bombyx mori, Mamestra brassicae, Spodoptera frugiperda, Mamestra brassicae IZD-Mb-0503, Bombyx mori Bm-N
brenda
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
brenda
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
brenda
Rogers, G.N.; Paulsen, J.C.; Daniels, R.S.; Skehel, J.J.; Wilson, I.A.; Wiley, D.C.
Single amino acid substitutions in influenza haemagglutinin change receptor binding specificity
Nature
304
76-78
1983
Bos taurus
brenda
Szumilo, T.; Kaushal, G.P.; Elbein, A.D.
Purification and properties of the glycoprotein processing N-acetylglucosaminyltransferase II from plants
Biochemistry
26
5498-5505
1987
Vigna radiata var. radiata
brenda
Strasser, R.; Steinkellner, H.; Boren, M.; Altmann, F.; Mach, L.; Glssl, J.; Mucha, J.
Molecular cloning of cDNA encoding N-acetylglucosaminyltransferase II from Arabidopsis thaliana
Glycoconj. J.
16
787-791
2000
Arabidopsis thaliana
brenda
Tan, J.; D'Agostaro, G.A.F.; Bendiak, B.; Reck, F.; Sarkar, M.; Squire, J.A.; Leong, P.; Schachter, H.
The human UDP-N-acetylglucosamine:alpha-6-D-mannoside-beta-1,2-N-acetylglucosaminyltransferase II gene (MGAT2). Cloning of genomic DNA, localization to chromosome 14q21, expression in insect cells and purification of the recombinant protein
Eur. J. Biochem.
231
317-328
1995
Homo sapiens
brenda
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
brenda
Chen, S.H.; Zhou, S.; Tan, J.; Schachter, H.
Transcriptional regulation of the human UDP-GlcNAc: alpha-6lpha-D-mannoside beta-1-2-N-acetylglucosaminyltransferase II gene (MGAT2) which controls complex N-glycan synthesis
Glycoconj. J.
15
301-308
1998
Homo sapiens
brenda
Zhang, W.; Revers, L.; Pierce, M.; Schachter, H.
Regulation of expression of the human beta-1,2-N-acetylglucosaminyltransferase II gene (MGAT2) by Ets transcription factors
Biochem. J.
347
511-518
2000
Homo sapiens
brenda
Wang, Y.; Schachter, H.; Marth, J.D.
Mice with a homozygous deletion of the Mgat2 gene encoding UDP-N-acetylglucosamine:alpha-6-D-mannoside beta1,2-N-acetylglucosaminyltransferase II: a model for congenital disorder of glycosylation type IIa
Biochim. Biophys. Acta
1573
301-311
2002
Mus musculus
brenda
Reck, F.; Springer, M.; Paulsen, H.; Brockhausen, I.; Sarkar, M.; Schachter, H.
Synthesis of tetrasaccharide analogs of the N-glycan substrate of beta-(1->2)-N-acetylglucosaminyltransferase II using trisaccharide precursors and recombinant beta-(1->2)-N-acetylglucosaminyltransferase I
Carbohydr. Res.
259
93-101
1994
Oryctolagus cuniculus
brenda
Leeb, T.; Kriegesmann, B.; Baumgartner, B.G.; Klett, C.; Yerle, M.; Hameister, H.; Brenig, B.
Molecular cloning of the porcine beta-1,2-N-acetylglucosaminyltransferase II gene and assignment to chromosome 1q23-q27
Biochim. Biophys. Acta
1336
361-366
1997
Sus scrofa
brenda
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
brenda
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
brenda
Tsitilou, S.G.; Grammenoudi, S.
Evidence for alternative splicing and developmental regulation of the Drosophila melanogaster Mgat2 (N-acetylglucosaminyltransferase II) gene
Biochem. Biophys. Res. Commun.
312
1372-1376
2003
Drosophila melanogaster
brenda
Takamatsu, S.; Inoue, N.; Katsumata, T.; Nakamura, K.; Fujibayashi, Y.; Takeuchi, M.
The relationship between the branch-forming glycosyltransferases and cell surface sugar chain structures
Biochemistry
44
6343-6349
2005
Homo sapiens
brenda
Tomiya, N.; Howe, D.; Aumiller, J.J.; Pathak, M.; Park, J.; Palter, K.B.; Jarvis, D.L.; Betenbaugh, M.J.; Lee, Y.C.
Complex-type biantennary N-glycans of recombinant human transferrin from Trichoplusia ni insect cells expressing mammalian beta-1,4-galactosyltransferase and beta-1,2-N-acetylglucosaminyltransferase II
Glycobiology
13
23-34
2003
Homo sapiens
brenda
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)
brenda
Schachter, H.
The joys of HexNAc. The synthesis and function of N- and O-glycan branches
Glycoconj. J.
17
465-483
2000
Homo sapiens
brenda
Mucha, J.; Svoboda, B.; Kappel, S.; Strasser, R.; Bencur, P.; Froehwein, U.; Schachter, H.; Mach, L.; Gloessl, J.
Two closely related forms of UDP-GlcNAc:alpha6-D-mannoside beta1,2-N-acetylglucosaminyltransferase II occur in the clawed frog Xenopus laevis
Glycoconj. J.
19
187-195
2003
Xenopus laevis (Q7ZZX7), Xenopus laevis
brenda
Schachter, H.; Reck, F.; Paulsen, H.
Use of synthetic oligosaccharide substrate analogs to map the active sites of N-acetylglucosaminyltransferases I and II
Methods Enzymol.
363
459-475
2003
Homo sapiens
brenda
Hanneman, A.J.; Rosa, J.C.; Ashline, D.; Reinhold, V.N.
Isomer and glycomer complexities of core GlcNAcs in Caenorhabditis elegans
Glycobiology
16
874-890
2006
Caenorhabditis elegans
brenda
Izumikawa, T.; Egusa, N.; Taniguchi, F.; Sugahara, K.; Kitagawa, H.
Heparan sulfate polymerization in Drosophila
J. Biol. Chem.
281
1929-1934
2006
Drosophila melanogaster
brenda
Ito, H.; Akiyama, M.; Nakagawa, H.; Uematsu, R.; Deguchi, K.; McMillan, J.R.; Nishimura, S.; Shimizu, H.
N-Linked neutral oligosaccharides in the stratum corneum of normal and ichthyotic skin
Arch. Dermatol. Res.
298
403-407
2007
Homo sapiens
brenda
Lee, S.; Grigorian, A.; Pawling, J.; Chen, I.; Gao, G.; Mozaffar, T.; McKerlie, C.; Demetriou, M.
N-Glycan processing deficiency promotes spontaneous inflammatory demyelination and neurodegeneration
J. Biol. Chem.
282
33725-33734
2007
Mus musculus
brenda
Kim, N.Y.; Kim, H.G.; Kim, Y.H.; Chung, I.S.; Yang, J.M.
Expression and characterization of human N-acetylglucosaminyltransferases and alpha2,3-sialyltransferase in insect cells for in vitro glycosylation of recombinant erythropoietin
J. Microbiol. Biotechnol.
18
383-391
2008
Homo sapiens
brenda
Chen, H.L.; Li, C.F.; Grigorian, A.; Tian, W.; Demetriou, M.
T cell receptor signaling co-regulates multiple Golgi genes to enhance N-glycan branching
J. Biol. Chem.
284
32454-32461
2009
Homo sapiens
brenda
Geisler, C.; Jarvis, D.L.
Substrate specificities and intracellular distributions of three N-glycan processing enzymes functioning at a key branch point in the insect N-glycosylation pathway
J. Biol. Chem.
287
7084-7097
2012
Spodoptera frugiperda
brenda
Damerow, M.; Graalfs, F.; Guether, M.L.; Mehlert, A.; Izquierdo, L.; Ferguson, M.A.
A gene of the beta3-glycosyltransferase family encodes N-acetylglucosaminyltransferase II function in Trypanosoma brucei
J. Biol. Chem.
291
13834-13845
2016
Trypanosoma brucei brucei (Q57U24), Trypanosoma brucei brucei 927/4 GUTat10.1 (Q57U24)
brenda
Miyazaki, T.; Kato, T.; Park, E.Y.
Heterologous expression, purification and characterization of human beta-1,2-N-acetylglucosaminyltransferase II using a silkworm-based Bombyx mori nucleopolyhedrovirus bacmid expression system
J. Biosci. Bioeng.
126
15-22
2018
Homo sapiens (Q10469), Homo sapiens
brenda
Miyazaki, T.; Miyashita, R.; Mori, S.; Kato, T.; Park, E.Y.
Expression and characterization of silkworm Bombyx mori beta-1,2-N-acetylglucosaminyltransferase II, a key enzyme for complex-type N-glycan biosynthesis
J. Biosci. Bioeng.
127
273-280
2019
Bombyx mori (A0A451FEC8), Bombyx mori
brenda
Kadirvelraj, R.; Yang, J.Y.; Sanders, J.H.; Liu, L.; Ramiah, A.; Prabhakar, P.K.; Boons, G.J.; Wood, Z.A.; Moremen, K.W.
Human N-acetylglucosaminyltransferase II substrate recognition uses a modular architecture that includes a convergent exosite
Proc. Natl. Acad. Sci. USA
115
4637-4642
2018
Homo sapiens (Q10469), Homo sapiens
brenda
Kajiura, H.; Nakamura, Y.; Nishimura, M.; Ohashi, T.; Misaki, R.; Fujiyama, K.
Characterization of Bombyx mori N-acetylglucosaminyltransferase II splicing variants
Biochem. Biophys. Res. Commun.
529
404-410
2020
Bombyx mori
brenda
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