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Galbeta(1->4)GlcNAcbeta(1->3)[Galbeta(1->4)GlcNAcbeta(1->6)]GalNAcalpha-OCH(CH3)CH(NH2)CO2H
UDP + GlcNAcbeta(1->3)Galbeta(1->4)GlcNAcbeta(1->3)[Galbeta(1->4)GlcNAcbeta(1->6)]GalNAcalpha-OCH(CH3)CH(NH2)CO2H
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Substrates: 115% activity compared to Galbeta(1->4)GlcNAcbeta-O(CH2)3N3
Products: -
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UDP-N-acetyl-alpha-D-glucosamine + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-R
Substrates: -
Products: -
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UDP-N-acetyl-alpha-D-glucosamine + Galbeta(1->4)GlcNAcbeta(1->3)Galbeta(1->4)GlcNAc
UDP + GlcNAcbeta(1->3)Galbeta(1->4)GlcNAcbeta(1->3)Galbeta(1->4)GlcNAc
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Substrates: -
Products: -
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UDP-N-acetyl-D-glucosamine + asialo alpha1-acid glycoprotein
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Substrates: sialic acid depleted alpha1-acid glycoprotein, 30% of the activity with neolactotetraosylceramide
Products: -
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UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide
UDP + N-acetyl-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide
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Substrates: i.e. neolactotetraosylceramide, GlcNAcT-2, synthesis in vitro of Ii core glycosphingolipids
Products: -
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UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP-N-acetyl-D-glucosamine + Fucalpha(1->2)Galbeta(1->4)GlcNAcbeta-O(CH2)3N3
UDP + GlcNAcbeta(1->3)[Fucalpha(1->2)]Galbeta(1->4)GlcNAcbeta-O(CH2)3N3
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Substrates: 32% activity compared to Galbeta(1->4)GlcNAcbeta-O(CH2)3N3
Products: -
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UDP-N-acetyl-D-glucosamine + Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
UDP + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
UDP-N-acetyl-D-glucosamine + Galbeta(1-4)GlcNAcbeta(1-4)GlcNAc-2-aminopyridine
UDP + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-4)GlcNAc-2-aminopyridine
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Substrates: -
Products: -
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UDP-N-acetyl-D-glucosamine + Galbeta(1-4)GlcNAcbeta(1-6)(Galbeta(1-4)GlcNAcbeta(1-2))Manalpha(1-6)Manbeta-octyl
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Substrates: regioselectivity of enzyme, favored site of GlcNAc addition is the lower beta1,2-branch over the beta1,6-branch by a 3:1 ratio resulting in a mixture of heptasaccharides
Products: -
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UDP-N-acetyl-D-glucosamine + Galbeta(1-4)GlcNAcbeta-p-nitrophenol
UDP + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta-p-nitrophenol
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Substrates: -
Products: -
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UDP-N-acetyl-D-glucosamine + Galbeta(1->3)GalNAcalpha-OCH(CH3)CH(NH2)CO2H
UDP + GlcNAcbeta(1->3)Galbeta(1->3)GalNAcalpha-OCH(CH3)CH(NH2)CO2H
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Substrates: 48% activity compared to Galbeta(1->4)GlcNAcbeta-O(CH2)3N3
Products: -
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UDP-N-acetyl-D-glucosamine + Galbeta(1->3)GalNAcbeta-O(CH2)2NH2
UDP + GlcNAcbeta(1->3)Galbeta(1->3)GalNAcbeta-O(CH2)2NH2
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Substrates: 76% activity compared to Galbeta(1->4)GlcNAcbeta-O(CH2)3N3
Products: -
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UDP-N-acetyl-D-glucosamine + Galbeta(1->3)GalNAcbeta-pNP
UDP + GlcNAcbeta(1->3)Galbeta(1->3)GalNAcbeta-pNP
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Substrates: poor acceptor, 23% activity compared to Galbeta(1->4)GlcNAcbeta-O(CH2)3N3
Products: -
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UDP-N-acetyl-D-glucosamine + Galbeta(1->3)GlcNAcbeta-O(CH2)3N3
UDP + GlcNAcbeta(1->3)Galbeta(1->3)GlcNAcbeta-O(CH2)3N3
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Substrates: 48% activity compared to Galbeta(1->4)GlcNAcbeta-O(CH2)3N3
Products: -
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UDP-N-acetyl-D-glucosamine + Galbeta(1->3)[Galbeta(1->4)GlcNAcbeta(1->6)]GalNAcalpha-OCH(CH3)CH(NH2)CO2H
UDP + GlcNAcbeta(1->3)Galbeta(1->3)[Galbeta(1->4)GlcNAcbeta(1->6)]GalNAcalpha-OCH(CH3)CH(NH2)CO2H
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Substrates: 101% activity compared to Galbeta(1->4)GlcNAcbeta-O(CH2)3N3
Products: -
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UDP-N-acetyl-D-glucosamine + Galbeta(1->3)[GlcNAcbeta(1->6)]GalNAcalpha-OCH(CH3)CH(NH2)CO2H
UDP + GlcNAcbeta(1->3)Galbeta(1->3)[GlcNAcbeta(1->6)]GalNAcalpha-OCH(CH3)CH(NH2)CO2H
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Substrates: 28% activity compared to Galbeta(1->4)GlcNAcbeta-O(CH2)3N3
Products: -
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UDP-N-acetyl-D-glucosamine + Galbeta(1->4)Glcbeta-O(CH2)3N3
UDP + GlcNAcbeta(1->3)Galbeta(1->4)Glcbeta-O(CH2)3N3
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Substrates: 65% activity compared to Galbeta(1->4)GlcNAcbeta-O(CH2)3N3
Products: -
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UDP-N-acetyl-D-glucosamine + Galbeta(1->4)GlcNAc
UDP + GlcNAcbeta(1->3)Galbeta(1->4)GlcNAc
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Substrates: 73% activity compared to Galbeta(1->4)GlcNAcbeta-O(CH2)3N3
Products: -
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UDP-N-acetyl-D-glucosamine + Galbeta(1->4)GlcNAcbeta(1->3)Galbeta(1->4)GlcNAcbeta(1->3)Galbeta(1->4)GlcNAcbeta(1->3)Galbeta(1->4)GlcNAcbeta-O(CH2)3N3
UDP + GlcNAcbeta(1->3)Galbeta(1->4)GlcNAcbeta(1->3)Galbeta(1->4)GlcNAcbeta(1->3)Galbeta(1->4)GlcNAcbeta(1->3)Galbeta(1->4)GlcNAcbeta-O(CH2)3N3
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Substrates: 107% activity compared to Galbeta(1->4)GlcNAcbeta-O(CH2)3N3
Products: -
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UDP-N-acetyl-D-glucosamine + Galbeta(1->4)GlcNAcbeta(1->3)Galbeta(1->4)GlcNAcbeta(1->3)Galbeta(1->4)GlcNAcbeta-O(CH2)3N3
UDP + GlcNAcbeta(1->3)Galbeta(1->4)GlcNAcbeta(1->3)Galbeta(1->4)GlcNAcbeta(1->3)Galbeta(1->4)GlcNAcbeta-O(CH2)3N3
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Substrates: 101% activity compared to Galbeta(1->4)GlcNAcbeta-O(CH2)3N3
Products: -
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UDP-N-acetyl-D-glucosamine + Galbeta(1->4)GlcNAcbeta(1->3)Galbeta(1->4)GlcNAcbeta-O(CH2)3N3
UDP + GlcNAcbeta(1->3)Galbeta(1->4)GlcNAcbeta(1->3)Galbeta(1->4)GlcNAcbeta-O(CH2)3N3
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Substrates: 90% activity compared to Galbeta(1->4)GlcNAcbeta-O(CH2)3N3
Products: -
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UDP-N-acetyl-D-glucosamine + Galbeta(1->4)GlcNAcbeta(1->3)GalNAcalpha-OCH(CH3)CH(NH2)CO2H
UDP + GlcNAcbeta(1->3)Galbeta(1->4)GlcNAcbeta(1->3)GalNAcalpha-OCH(CH3)CH(NH2)CO2H
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Substrates: 57% activity compared to Galbeta(1->4)GlcNAcbeta-O(CH2)3N3
Products: -
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UDP-N-acetyl-D-glucosamine + Galbeta(1->4)GlcNAcbeta(1->6)GalNAcalpha-OCH(CH3)CH(NH2)CO2H
UDP + GlcNAcbeta(1->3)Galbeta(1->4)GlcNAcbeta(1->6)GalNAcalpha-OCH(CH3)CH(NH2)CO2H
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Substrates: 101% activity compared to Galbeta(1->4)GlcNAcbeta-O(CH2)3N3
Products: -
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UDP-N-acetyl-D-glucosamine + Galbeta(1->4)GlcNAcbeta(1->6)[GlcNAcbeta(1->4)]Galbeta(1->4)GlcNAcbeta-pNP
UDP + GlcNAcbeta(1->3)Galbeta(1->4)GlcNAcbeta(1->6)[GlcNAcbeta(1->4)]Galbeta(1->4)GlcNAcbeta-pNP
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Substrates: 104% activity compared to Galbeta(1->4)GlcNAcbeta-O(CH2)3N3
Products: -
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UDP-N-acetyl-D-glucosamine + Galbeta(1->4)GlcNAcbeta-O(CH2)3N3
UDP + GlcNAcbeta(1->3)Galbeta(1->4)GlcNAcbeta-O(CH2)3N3
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Substrates: 100% activity
Products: -
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UDP-N-acetyl-D-glucosamine + Galbeta(1->4)[Fucalpha(1->3)]GlcNAcbeta-O(CH2)3N3
UDP + GlcNAcbeta(1->3)Galbeta(1->4)[Fucalpha(1->3)]GlcNAcbeta-O(CH2)3N3
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Substrates: 26% activity compared to Galbeta(1->4)GlcNAcbeta-O(CH2)3N3
Products: -
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UDP-N-acetyl-D-glucosamine + Galbeta1,4(SO3-,6)-GlcNAcbeta1,3(SO3-,6)-Galbeta1,4(SO3-,6)-GlcNAc
UDP + GlcNAcbeta1,3-Galbeta1,4(SO3-,6)-GlcNAcbeta1,3(SO3-,6)-Galbeta1,4(SO3-,6)-GlcNAc
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Substrates: i.e. L2L4, 72% activity compared to L2L2
Products: -
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UDP-N-acetyl-D-glucosamine + Galbeta1,4(SO3-,6)-GlcNAcbeta1,3-Galbeta1,4(SO3-,6)-GlcNAc
UDP + GlcNAcbeta1,3-Galbeta1,4(SO3-,6)GlcNAcbeta1,3-Galbeta1,4(SO3-,6)-GlcNAc
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Substrates: i.e. L2L2, a 6-O-sulfated keratan sulfate, best substrate
Products: -
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UDP-N-acetyl-D-glucosamine + Galbeta1,4(SO3-,6)-GlcNAcbeta1,3-Galbeta1,4(SO3-,6)-GlcNAc
UDP + GlcNAcbeta1,3-Galbeta1,4(SO3-,6)GlcNAcbeta1,3Galbeta1,4(SO3-,6)-GlcNAc
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Substrates: i.e. L2L2, a 6-O-sulfated keratan sulfate, best substrate
Products: -
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UDP-N-acetyl-D-glucosamine + GalNAcbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
UDP + GlcNAcbeta(1-3)GalNAcbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
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Substrates: -
Products: mixture of the pentasaccharide product, 27 mol%, and the unreacted tetrasaccharide, 73 mol%
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UDP-N-acetyl-D-glucosamine + GalNAcbeta(1-4)GlcNAcbeta(1-3)Galbeta1-OMe
UDP + GlcNAcbeta(1-3)GalNAcbeta(1-4)GlcNAcbeta(1-3)Galbeta1-OMe
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Substrates: -
Products: -
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UDP-N-acetyl-D-glucosamine + GalNAcbeta(1-4)GlcNAcbeta1-OMe
UDP + GlcNAcbeta(1-3)GalNAcbeta(1-4)GlcNAcbeta1-OMe
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Substrates: -
Products: -
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UDP-N-acetyl-D-glucosamine + GalNAcbeta(1-4)GlcNAcbeta1-OR
UDP + GlcNAcbeta(1-3)GalNAcbeta(1-4)GlcNAcbeta1-OR
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Substrates: i.e. N,N-diacetyllactosediamine-OR
Products: only 12.5% of the substrate is converted into the product, which is unusually resistant towards jackbean beta-N-acetylhexosaminidase
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UDP-N-acetyl-D-glucosamine + glycolipid
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Substrates: physiological acceptors: N-glycans, O-glycans, glycolipids and keratan sulfates
Products: -
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UDP-N-acetyl-D-glucosamine + keratan sulfate
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Substrates: physiological acceptors: N-glycans, O-glycans, glycolipids and keratan sulfates
Products: -
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UDP-N-acetyl-D-glucosamine + lactosylceramide
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Substrates: 15% of the activity with neolactotetraosylceramide
Products: -
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UDP-N-acetyl-D-glucosamine + N-acetyllactosamine
UDP + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
Substrates: -
Products: -
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UDP-N-acetyl-D-glucosamine + N-glycan
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UDP-N-acetyl-D-glucosamine + O-glycan
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Substrates: physiological acceptors: N-glycans, O-glycans, glycolipids and keratan sulfates
Products: -
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UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
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UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
UDP + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
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Substrates: poly-N-acetyllactosamine is biosynthesized by the alternating addition of N-acetyl-D-glucosamine by UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase and Gal by UDP-Gal:betaGlcNAc beta-1,4-galactosyltransferase
Products: -
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UDP-N-acetylglucosamine + asialo-alpha1-acid glycoprotein
UDP + N-acetylglucosaminylated asialo-alpha1-acid glycoprotein
UDP-N-acetylglucosamine + asialo-fetuin
UDP + N-acetylglucosaminylated asialo-fetuin
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Substrates: much less effective than asialo-alpha1-acid glycoprotein, transfer of GlcNAc to a terminal Gal in a beta1,3-linkage
Products: -
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UDP-N-acetylglucosamine + asialo-transferrin
UDP + N-acetylglucosaminylated asialo-transferrin
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Substrates: much less effective than asialo-alpha1-acid glycoprotein, transfer of GlcNAc to a terminal Gal in a beta1,3-linkage
Products: -
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UDP-N-acetylglucosamine + lactoneotetraosylceramide
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Substrates: lactoneotetraosylceramide from bovine erythrocytes, higher rate than with lactonorhexaosylceramide, efficiency decreases with growing acceptor chain length
Products: -
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UDP-N-acetylglucosamine + lactonorhexaosylceramide
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Substrates: lactonorhexaosylceramide from bovine erythrocytes, lower rate than with lactoneotetraosylceramide, efficiency decreases with growing acceptor chain length
Products: -
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UDP-N-acetylglucosamine + lactose
UDP + GlcNAcbeta(1-3)Galbeta(1-4)Glc
UDP-N-acetylglucosamine + lactosylceramide
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Substrates: lactosylceramide from human erythrocytes
Products: -
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UDP-N-acetylglucosamine + lactotetraosylceramide
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Substrates: lactotetraosylceramide from human meconium, poor substrate
Products: -
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UDP-N-acetylglucosamine + N-acetyllactosamine
UDP + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
UDP-N-acetylglucosamine + porcine submaxillary asialo-afuco-mucin
UDP + N-acetylglucosaminylated porcine submaxillary asialo-afuco-mucin
additional information
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UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R

UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
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Substrates: -
Products: -
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UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
Substrates: iGnT has a unique characteristic in binding to acceptor substrates, preferentially adding poly-N-acetyllactosamine to membrane glycoproteins
Products: -
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UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
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Substrates: involved in the biosynthesis of blood group precursors, enzyme might control the biosynthesis of the linear carbohydrate chain by adding a N-acetylglucosaminyl residue to a Galbeta(1-4)GlcNAc-R structure present on oligosaccharides, glycosylceramides and glycoproteins
Products: -
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UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
Substrates: enzyme is essential for the formation of poly-N-acetyllactosamines and the i-antigen, responsible for the formation of GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc-R structure and poly-N-acetyllactosamine extension
Products: -
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UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
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Substrates: B3GNT1 displays an in vitro preference for the GlcNAcbeta1->2Man branch
Products: -
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UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
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Substrates: acts on beta-galactosyl-1,4-N-acetylglucosaminyl termini on asialo-alpha1-acid glycoproteins and other glycoproteins and oligosaccharides, GlcNAc residues are introduced to position C-3 of the terminal galactose of the glycoprotein
Products: -
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UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
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Substrates: highly specific for acceptor oligosaccharides and glycoproteins carrying a terminal Galbeta(1-4)GlcNAcbeta1-R unit, catalyzes the formation of GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta-R sequence, Galbeta(1-4)GlcNAcbeta(1-2)(Galbeta(1-4)GlcNAcbeta(1-6))Man pentasaccharide in the acceptor structure is a requirement for optimal activity, branch specificity, branches of this pentasaccharide structure, when contained in tri- and tetraantennary oligosaccharides, are highly preferred over other branches for attachment of the 1st and 2nd mol of GlcNAc into the acceptor molecule, enzyme also shows activity towards oligosaccharides related to blood group I- and i-active polylactosaminoglycans
Products: -
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UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
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Substrates: might function in the biosynthesis of cell surface polylactosaminoglycans on Novikoff cells and blood group i antigenic structures, enzyme controls the synthesis of linear chain types by adding a N-acetylglucosaminyl residue to a Galbeta(1-4)GlcNAc-R primer structure present on glycoprotein or glycolipid yielding a GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc-R sequence
Products: -
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UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
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Substrates: enzyme functions in both the initiation and elongation of linear i-active polylactosaminoglycan chains of N-glycoproteins and possibly other glycoconjugates
Products: -
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UDP-N-acetyl-D-glucosamine + Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc

UDP + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
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Substrates: i.e. lacto-N-neotetraose, 117% of activity with N-acetyllactosamine
Products: -
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UDP-N-acetyl-D-glucosamine + Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
UDP + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
Substrates: -
Products: -
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UDP-N-acetyl-D-glucosamine + N-glycan

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Substrates: physiological acceptors: N-glycans, O-glycans, glycolipids and keratan sulfates
Products: -
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UDP-N-acetyl-D-glucosamine + N-glycan
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Substrates: polylactosamine extension occurs on both beta1,2- and beta1,6-branches of complex N-type glycans
Products: -
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UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine

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Substrates: involved in the initiation and extension of poly-N-acetyllactosamine biosynthesis, may act as a key enzyme
Products: -
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UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
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Substrates: synthesis of N-acetyllactosamine repeats in Asn-linked oligosaccharides is enhanced by an increase of enzyme
Products: -
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UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
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Substrates: -
Products: -
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UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
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Substrates: enzyme is capable of elongation of polylactosamine i-chains
Products: -
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UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
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Substrates: poly-N-acetyllactosamine biosynthesis, polylactosamine extension occurs on both beta1,2- and beta1,6-branches of complex N-type glycans
Products: -
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UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
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Substrates: -
Products: -
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UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
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Substrates: biosynthesis of poly-N-acetyllactosamine chains on N-linked oligosaccharides, catalyzes a rate-limiting reaction in the expression of poly-N-acetyllactosamine chains, especially in pheochromocytoma cells
Products: -
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UDP-N-acetylglucosamine + asialo-alpha1-acid glycoprotein

UDP + N-acetylglucosaminylated asialo-alpha1-acid glycoprotein
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Substrates: best acceptor among the glycoproteins that contain Galbeta(1-4)GlcNAc
Products: -
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UDP-N-acetylglucosamine + asialo-alpha1-acid glycoprotein
UDP + N-acetylglucosaminylated asialo-alpha1-acid glycoprotein
Substrates: -
Products: -
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UDP-N-acetylglucosamine + asialo-alpha1-acid glycoprotein
UDP + N-acetylglucosaminylated asialo-alpha1-acid glycoprotein
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Substrates: GlcNAc residues are introduced to position C-3 of the terminal galactose of the glycoprotein, relative high activity towards asialo-alpha1-acid glycoprotein in Novikoff ascites tumor cells
Products: -
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UDP-N-acetylglucosamine + asialo-alpha1-acid glycoprotein
UDP + N-acetylglucosaminylated asialo-alpha1-acid glycoprotein
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Substrates: much more effective than asialo-transferrin and asialo-fetuin, asialo-alpha1-acid glycoprotein from human plasma Cohn fraction V, transfer of GlcNAc to a terminal Gal in a beta1,3-linkage
Products: -
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UDP-N-acetylglucosamine + lactose

UDP + GlcNAcbeta(1-3)Galbeta(1-4)Glc
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Substrates: transfer of one GlcNAc to position C-3 of the terminal Gal residue of lactose or N-acetyllactosamine in the beta linkage, 51% of activity with N-acetyllactosamine
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UDP-N-acetylglucosamine + lactose
UDP + GlcNAcbeta(1-3)Galbeta(1-4)Glc
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Substrates: less physiological acceptor than N-acetyllactosamine
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UDP-N-acetylglucosamine + lactose
UDP + GlcNAcbeta(1-3)Galbeta(1-4)Glc
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Substrates: less effective acceptor than N-acetyllactosamine
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UDP-N-acetylglucosamine + lactose
UDP + GlcNAcbeta(1-3)Galbeta(1-4)Glc
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Substrates: 70% of activity with N-acetyllactosamine
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UDP-N-acetylglucosamine + N-acetyllactosamine

UDP + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
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Substrates: transfer of one GlcNAc to position C-3 of the terminal Gal residue of lactose or N-acetyllactosamine in the beta linkage
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UDP-N-acetylglucosamine + N-acetyllactosamine
UDP + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
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Substrates: -
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UDP-N-acetylglucosamine + N-acetyllactosamine
UDP + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
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Substrates: more physiological acceptor than lactose
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UDP-N-acetylglucosamine + N-acetyllactosamine
UDP + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
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Substrates: more effective acceptor than lactose
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UDP-N-acetylglucosamine + N-acetyllactosamine
UDP + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
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Substrates: -
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UDP-N-acetylglucosamine + N-acetyllactosamine
UDP + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
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Substrates: more effective acceptor than lactose
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UDP-N-acetylglucosamine + porcine submaxillary asialo-afuco-mucin

UDP + N-acetylglucosaminylated porcine submaxillary asialo-afuco-mucin
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Substrates: very poor substrate
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UDP-N-acetylglucosamine + porcine submaxillary asialo-afuco-mucin
UDP + N-acetylglucosaminylated porcine submaxillary asialo-afuco-mucin
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Substrates: poor acceptor, Galbeta(1-3)GalNAc as terminal acceptor structure
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additional information

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Substrates: terminal Galbeta(1-4)Glc(NAc) sequences, i.e. type II chains, are preferred substrates, no substrates: terminal Galbeta(1-3)GlcNAc sequences, i.e. type I chains, Lewis X trisaccharides, i.e. Galbeta(1-4)(Fucalpha(1-3))GlcNAc, monosaccharides, e.g. galactose, asialo-bovine submaxillary mucin that contains GalNAcalpha1-Ser/Thr and Galbeta(1-3)GalNAcalpha1-Ser/Thr
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additional information
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Substrates: the enzyme shows no activity on a terminal Gal with Neu5Acalpha(2->6) substitution. Terminal galactose with alpha-linkage, Galalpha(1->3)Gal or Galalpha(1->4)Gal is not an acceptor substrate for the enzyme
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additional information
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Substrates: no acceptors: melibiose, gentiobiose, galactose, glucose, N-acetylgalactosamine, N-acetylglucosamine
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additional information
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Substrates: transfer of GlcNAc occurs mainly to type 2 chain nonfucosylated structures, elongation of type 1 chain structure Lc4 is also detectable, no transfer to any fucosylated derivative of either type 1 or 2 chains, transfer of GlcNAc to a terminal Gal residue on a lacto-series core chain
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additional information
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Substrates: no acceptor: Galbeta(1-3)GlcNAcbeta(1-3)Galbeta(1-4)Glc
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additional information
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Substrates: biosynthesis of lacto-series core chains, enzyme is activated in association with oncogenesis in colonic epithelia
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additional information
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Substrates: the enzyme together with N-acetyllactosamine synthase, EC 2.4.1.90, catalyzes formation of linear glycans containing alternating beta-3-O-substituted residues of D-galactose and beta-4-O-substituted residues of N-acetyl-D-glucosamine, structures are present among others in glycosphingolipids or H-II type, polyglycosylceramides and polyglycosylpeptides, e.g. erythroglycan
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additional information
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Substrates: enzyme is in volved in biosynthesis of keratan sulfate, overview, enzyme is an anti-migration factor for a lung cancer cell line
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additional information
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Substrates: substrate specificity, enzyme acts efficiently on keratan sulfate-related glycans, while lacto-N-tetraose and lacto-N-neo-tetraose are poor substrates, overview, product analysis
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additional information
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Substrates: transglycosylation reaction follows a sequential mechanism
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additional information
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Substrates: transglycosylation reaction follows a sequential mechanism. Kd values of UDP-GlcNAc and UDP are around 0.14 and 0.26 mM, respectively
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additional information
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Substrates: beta3GnT7 may play a role in preventing cells from migrating out of the original tissues and invading surrounding tissues
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additional information
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Substrates: beta3GnT7 may play a role in preventing cells from migrating out of the original tissues and invading surrounding tissues
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additional information
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Substrates: biosynthesis of Ii core glycosphingolipids
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additional information
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Substrates: B3gnt1 null females are fertile, the B3gnt1 null males are not able to sire litters at the expected rate when mated to either wild type or B3gnt1-null females
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additional information
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Substrates: beta3GnT7 may play a role in preventing cells from migrating out of the original tissues and invading surrounding tissues
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additional information
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Substrates: asialo-serum glycoproteins are much more effective than O-glycoproteins as acceptors, overview over oligosaccharide substrates
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UDP-N-acetyl-alpha-D-glucosamine + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-R
Substrates: -
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UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP-N-acetyl-D-glucosamine + glycolipid
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Substrates: physiological acceptors: N-glycans, O-glycans, glycolipids and keratan sulfates
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UDP-N-acetyl-D-glucosamine + keratan sulfate
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Substrates: physiological acceptors: N-glycans, O-glycans, glycolipids and keratan sulfates
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UDP-N-acetyl-D-glucosamine + N-glycan
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UDP-N-acetyl-D-glucosamine + O-glycan
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Substrates: physiological acceptors: N-glycans, O-glycans, glycolipids and keratan sulfates
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UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
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additional information
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UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R

UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
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Substrates: involved in the biosynthesis of blood group precursors, enzyme might control the biosynthesis of the linear carbohydrate chain by adding a N-acetylglucosaminyl residue to a Galbeta(1-4)GlcNAc-R structure present on oligosaccharides, glycosylceramides and glycoproteins
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UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
Substrates: enzyme is essential for the formation of poly-N-acetyllactosamines and the i-antigen, responsible for the formation of GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc-R structure and poly-N-acetyllactosamine extension
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UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
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Substrates: might function in the biosynthesis of cell surface polylactosaminoglycans on Novikoff cells and blood group i antigenic structures, enzyme controls the synthesis of linear chain types by adding a N-acetylglucosaminyl residue to a Galbeta(1-4)GlcNAc-R primer structure present on glycoprotein or glycolipid yielding a GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc-R sequence
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UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
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Substrates: enzyme functions in both the initiation and elongation of linear i-active polylactosaminoglycan chains of N-glycoproteins and possibly other glycoconjugates
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UDP-N-acetyl-D-glucosamine + N-glycan

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Substrates: physiological acceptors: N-glycans, O-glycans, glycolipids and keratan sulfates
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UDP-N-acetyl-D-glucosamine + N-glycan
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Substrates: polylactosamine extension occurs on both beta1,2- and beta1,6-branches of complex N-type glycans
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UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine

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Substrates: involved in the initiation and extension of poly-N-acetyllactosamine biosynthesis, may act as a key enzyme
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UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
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Substrates: synthesis of N-acetyllactosamine repeats in Asn-linked oligosaccharides is enhanced by an increase of enzyme
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UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
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Substrates: -
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UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
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Substrates: enzyme is capable of elongation of polylactosamine i-chains
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UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
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Substrates: poly-N-acetyllactosamine biosynthesis, polylactosamine extension occurs on both beta1,2- and beta1,6-branches of complex N-type glycans
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UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
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Substrates: -
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UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
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Substrates: biosynthesis of poly-N-acetyllactosamine chains on N-linked oligosaccharides, catalyzes a rate-limiting reaction in the expression of poly-N-acetyllactosamine chains, especially in pheochromocytoma cells
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additional information

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Substrates: biosynthesis of lacto-series core chains, enzyme is activated in association with oncogenesis in colonic epithelia
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additional information
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Substrates: the enzyme together with N-acetyllactosamine synthase, EC 2.4.1.90, catalyzes formation of linear glycans containing alternating beta-3-O-substituted residues of D-galactose and beta-4-O-substituted residues of N-acetyl-D-glucosamine, structures are present among others in glycosphingolipids or H-II type, polyglycosylceramides and polyglycosylpeptides, e.g. erythroglycan
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additional information
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Substrates: enzyme is in volved in biosynthesis of keratan sulfate, overview, enzyme is an anti-migration factor for a lung cancer cell line
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additional information
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Substrates: beta3GnT7 may play a role in preventing cells from migrating out of the original tissues and invading surrounding tissues
Products: -
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additional information
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Substrates: beta3GnT7 may play a role in preventing cells from migrating out of the original tissues and invading surrounding tissues
Products: -
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additional information
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Substrates: biosynthesis of Ii core glycosphingolipids
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additional information
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Substrates: B3gnt1 null females are fertile, the B3gnt1 null males are not able to sire litters at the expected rate when mated to either wild type or B3gnt1-null females
Products: -
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additional information
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Substrates: beta3GnT7 may play a role in preventing cells from migrating out of the original tissues and invading surrounding tissues
Products: -
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1-[(2R)-3,3-dimethylbutan-2-yl]-6-(5-methyl-5-phenyl-4,5-dihydro-1,2,4-oxadiazol-3-yl)-1,3-dihydro-2H-benzimidazol-2-one
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1-[(2R)-3,3-dimethylbutan-2-yl]-6-(morpholine-4-carbonyl)-1,3-dihydro-2H-benzimidazol-2-one
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1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(2S)-2-(1H-indol-2-yl)-2-methyl-5-oxo-2,5-dihydro-1H-imidazol-4-yl]-1,3-dihydro-2H-benzimidazol-2-one
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1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(2S)-2-(2,3-dimethyl-1H-indol-5-yl)-2-methyl-5-oxo-2,5-dihydro-1H-imidazol-4-yl]-1,3-dihydro-2H-benzimidazol-2-one
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1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(2S)-2-(imidazo[1,2-a]pyridin-6-yl)-2-methyl-5-oxo-2,5-dihydro-1H-imidazol-4-yl]-1,3-dihydro-2H-benzimidazol-2-one
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1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(2S)-2-methyl-5-oxo-2-[2-(trifluoromethyl)pyrimidin-5-yl]-2,5-dihydro-1H-imidazol-4-yl]-1,3-dihydro-2H-benzimidazol-2-one
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1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(2S)-5-oxo-2-(pyridin-3-yl)-2-(4H-1,2,4-triazol-3-yl)-2,5-dihydro-1H-imidazol-4-yl]-1,3-dihydro-2H-benzimidazol-2-one
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1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(5S)-5-methyl-2-oxo-5-[2-(trifluoromethyl)pyrimidin-5-yl]-2,5-dihydrofuran-3-yl]-1,3-dihydro-2H-benzimidazol-2-one
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1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(5S)-5-methyl-4-oxo-5-phenyl-4,5-dihydro-1H-imidazol-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
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1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(5S)-5-methyl-4-oxo-5-[2-(trifluoromethyl)pyrimidin-5-yl]-4,5-dihydro-1H-imidazol-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
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1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(5S)-5-methyl-4-oxo-5-[5-(trifluoromethyl)pyridin-2-yl]-4,5-dihydro-1H-imidazol-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
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1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(5S)-5-methyl-4-oxo-5-[6-(trifluoromethyl)pyridin-3-yl]-4,5-dihydro-1H-imidazol-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
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1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(5S)-5-methyl-5-(5-methylpyridin-2-yl)-4-oxo-4,5-dihydro-1H-imidazol-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
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1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(5S)-5-methyl-5-(5-methylpyrimidin-2-yl)-4-oxo-4,5-dihydro-1H-imidazol-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
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1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(5S)-5-methyl-5-(6-methylpyridin-3-yl)-4-oxo-4,5-dihydro-1H-imidazol-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
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3-(2-methylpropyl)-2-oxo-2,3-dihydro-1H-1,3-benzimidazole-5-carboxylic acid
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3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-2,3-dihydro-1H-1,3-benzimidazole-5-carboxylic acid
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3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxylic acid
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3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-N-(propan-2-yl)-2,3-dihydro-1H-benzimidazole-5-carboxamide
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3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-N-phenyl-2,3-dihydro-1H-benzimidazole-5-carboxamide
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3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-N-[(1S)-1-[2-(trifluoromethyl)pyrimidin-5-yl]ethyl]-2,3-dihydro-1H-benzimidazole-5-carboxamide
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3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-N-[(1S)-1-[5-(trifluoromethyl)pyridin-2-yl]ethyl]-2,3-dihydro-1H-benzimidazole-5-carboxamide
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3-[(2R)-3,3-dimethylbutan-2-yl]-N-(2,3-dimethyl-1H-indol-6-yl)-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide
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3-[(2R)-3,3-dimethylbutan-2-yl]-N-[(1S)-1-(2-methylpyrimidin-5-yl)ethyl]-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide
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3-[(2R)-3,3-dimethylbutan-2-yl]-N-[(1S)-1-(5-methylpyridin-2-yl)ethyl]-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide
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4-Thiouridine diphosphate
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inhibits in a concentration-dependent manner
6-[(2R)-2-(2-chloropyrimidin-5-yl)-5-oxo-2-(pyridin-2-yl)-2,5-dihydro-1H-imidazol-4-yl]-1-[(2R)-3,3-dimethylbutan-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
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6-[(2R)-2-(5-chloropyridin-2-yl)-2-(6-chloropyridin-3-yl)-5-oxo-2,5-dihydro-1H-imidazol-4-yl]-1-[(2R)-3,3-dimethylbutan-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
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6-[(2S)-2-(5-chloropyridin-2-yl)-2-methyl-5-oxo-2,5-dihydro-1H-imidazol-4-yl]-1-[(2R)-3,3-dimethylbutan-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
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6-[(2S)-2-benzyl-5-oxo-2-[2-(trifluoromethyl)pyrimidin-5-yl]-2,5-dihydro-1H-imidazol-4-yl]-1-[(2R)-3,3-dimethylbutan-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
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6-[(5R)-5-(5-chloropyridin-2-yl)-5-methyl-4-oxo-4,5-dihydro-1H-imidazol-2-yl]-1-[(2R)-3,3-dimethylbutan-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
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6-[(5S)-5-(5-chloropyridin-2-yl)-5-methyl-4-oxo-4,5-dihydro-1H-imidazol-2-yl]-1-[(2R)-3,3-dimethylbutan-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
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6-[(5S)-5-(5-chloropyrimidin-2-yl)-5-methyl-4-oxo-4,5-dihydro-1H-imidazol-2-yl]-1-[(2R)-3,3-dimethylbutan-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
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N-acetyllactosamine
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strong product inhibition
N-[(1R)-1-(4-chlorophenyl)ethyl]-3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide
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N-[(1S)-1-(2-chloropyrimidin-5-yl)ethyl]-3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide
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N-[(1S)-1-(4-chlorophenyl)ethyl]-3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide
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N-[(1S)-1-(5-bromopyridin-2-yl)ethyl]-3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide
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N-[(1S)-1-(5-chloropyrazin-2-yl)ethyl]-3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide
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N-[(1S)-1-(5-chloropyridin-2-yl)ethyl]-3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide
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N-[(1S)-1-(5-chloropyrimidin-2-yl)ethyl]-3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide
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N-[(4-chlorophenyl)methyl]-3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide
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N-[2-(4-chlorophenyl)propan-2-yl]-3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide
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UDP
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1 mM, 70% inhibition
additional information
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nerve growth factor stimulated PC-12 cells with reduced GnT-i activity compared to unstimulated cells, no effect in PC-12D cells
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CaCl2

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EDTA

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10 mM, complete inhibition
EDTA
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slightly, 12% inhibition at 10 mM
ZnCl2

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0.0009
1-[(2R)-3,3-dimethylbutan-2-yl]-6-(5-methyl-5-phenyl-4,5-dihydro-1,2,4-oxadiazol-3-yl)-1,3-dihydro-2H-benzimidazol-2-one
Homo sapiens
pH and temperature not specified in the publication
0.0266
1-[(2R)-3,3-dimethylbutan-2-yl]-6-(morpholine-4-carbonyl)-1,3-dihydro-2H-benzimidazol-2-one
Homo sapiens
pH and temperature not specified in the publication
0.000053 - 0.000055
1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(2S)-2-(1H-indol-2-yl)-2-methyl-5-oxo-2,5-dihydro-1H-imidazol-4-yl]-1,3-dihydro-2H-benzimidazol-2-one
0.00101
1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(2S)-2-(2,3-dimethyl-1H-indol-5-yl)-2-methyl-5-oxo-2,5-dihydro-1H-imidazol-4-yl]-1,3-dihydro-2H-benzimidazol-2-one
Homo sapiens
pH and temperature not specified in the publication
0.00037
1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(2S)-2-(imidazo[1,2-a]pyridin-6-yl)-2-methyl-5-oxo-2,5-dihydro-1H-imidazol-4-yl]-1,3-dihydro-2H-benzimidazol-2-one
Homo sapiens
pH and temperature not specified in the publication
0.000024
1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(2S)-2-methyl-5-oxo-2-[2-(trifluoromethyl)pyrimidin-5-yl]-2,5-dihydro-1H-imidazol-4-yl]-1,3-dihydro-2H-benzimidazol-2-one
Homo sapiens
pH and temperature not specified in the publication
0.000026
1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(2S)-5-oxo-2-(pyridin-3-yl)-2-(4H-1,2,4-triazol-3-yl)-2,5-dihydro-1H-imidazol-4-yl]-1,3-dihydro-2H-benzimidazol-2-one
Homo sapiens
pH and temperature not specified in the publication
0.000028
1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(5S)-5-methyl-2-oxo-5-[2-(trifluoromethyl)pyrimidin-5-yl]-2,5-dihydrofuran-3-yl]-1,3-dihydro-2H-benzimidazol-2-one
Homo sapiens
pH and temperature not specified in the publication
0.0006
1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(5S)-5-methyl-4-oxo-5-phenyl-4,5-dihydro-1H-imidazol-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
Homo sapiens
pH and temperature not specified in the publication
0.000009
1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(5S)-5-methyl-4-oxo-5-[2-(trifluoromethyl)pyrimidin-5-yl]-4,5-dihydro-1H-imidazol-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
Homo sapiens
pH and temperature not specified in the publication
0.00003
1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(5S)-5-methyl-4-oxo-5-[5-(trifluoromethyl)pyridin-2-yl]-4,5-dihydro-1H-imidazol-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
Homo sapiens
pH and temperature not specified in the publication
0.000008
1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(5S)-5-methyl-4-oxo-5-[6-(trifluoromethyl)pyridin-3-yl]-4,5-dihydro-1H-imidazol-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
Homo sapiens
pH and temperature not specified in the publication
0.000096
1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(5S)-5-methyl-5-(5-methylpyridin-2-yl)-4-oxo-4,5-dihydro-1H-imidazol-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
Homo sapiens
pH and temperature not specified in the publication
0.000024
1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(5S)-5-methyl-5-(5-methylpyrimidin-2-yl)-4-oxo-4,5-dihydro-1H-imidazol-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
Homo sapiens
pH and temperature not specified in the publication
0.000029
1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(5S)-5-methyl-5-(6-methylpyridin-3-yl)-4-oxo-4,5-dihydro-1H-imidazol-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
Homo sapiens
pH and temperature not specified in the publication
0.0091
3-(2-methylpropyl)-2-oxo-2,3-dihydro-1H-1,3-benzimidazole-5-carboxylic acid
Homo sapiens
pH and temperature not specified in the publication
0.00026
3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-2,3-dihydro-1H-1,3-benzimidazole-5-carboxylic acid
Homo sapiens
pH and temperature not specified in the publication
0.122
3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxylic acid
Homo sapiens
pH and temperature not specified in the publication
-
0.0029
3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-N-(propan-2-yl)-2,3-dihydro-1H-benzimidazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.00082
3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-N-phenyl-2,3-dihydro-1H-benzimidazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.00007
3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-N-[(1S)-1-[2-(trifluoromethyl)pyrimidin-5-yl]ethyl]-2,3-dihydro-1H-benzimidazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.00023
3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-N-[(1S)-1-[5-(trifluoromethyl)pyridin-2-yl]ethyl]-2,3-dihydro-1H-benzimidazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.00006 - 0.165
3-[(2R)-3,3-dimethylbutan-2-yl]-N-(2,3-dimethyl-1H-indol-6-yl)-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide
0.00012
3-[(2R)-3,3-dimethylbutan-2-yl]-N-[(1S)-1-(2-methylpyrimidin-5-yl)ethyl]-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000093
3-[(2R)-3,3-dimethylbutan-2-yl]-N-[(1S)-1-(5-methylpyridin-2-yl)ethyl]-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000039
6-[(2R)-2-(2-chloropyrimidin-5-yl)-5-oxo-2-(pyridin-2-yl)-2,5-dihydro-1H-imidazol-4-yl]-1-[(2R)-3,3-dimethylbutan-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
Homo sapiens
pH and temperature not specified in the publication
0.0002
6-[(2R)-2-(5-chloropyridin-2-yl)-2-(6-chloropyridin-3-yl)-5-oxo-2,5-dihydro-1H-imidazol-4-yl]-1-[(2R)-3,3-dimethylbutan-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
Homo sapiens
pH and temperature not specified in the publication
0.000069
6-[(2S)-2-(5-chloropyridin-2-yl)-2-methyl-5-oxo-2,5-dihydro-1H-imidazol-4-yl]-1-[(2R)-3,3-dimethylbutan-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
Homo sapiens
pH and temperature not specified in the publication
0.000013
6-[(2S)-2-benzyl-5-oxo-2-[2-(trifluoromethyl)pyrimidin-5-yl]-2,5-dihydro-1H-imidazol-4-yl]-1-[(2R)-3,3-dimethylbutan-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
Homo sapiens
pH and temperature not specified in the publication
0.00051
6-[(5R)-5-(5-chloropyridin-2-yl)-5-methyl-4-oxo-4,5-dihydro-1H-imidazol-2-yl]-1-[(2R)-3,3-dimethylbutan-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
Homo sapiens
pH and temperature not specified in the publication
0.000066
6-[(5S)-5-(5-chloropyridin-2-yl)-5-methyl-4-oxo-4,5-dihydro-1H-imidazol-2-yl]-1-[(2R)-3,3-dimethylbutan-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
Homo sapiens
pH and temperature not specified in the publication
0.000082
6-[(5S)-5-(5-chloropyrimidin-2-yl)-5-methyl-4-oxo-4,5-dihydro-1H-imidazol-2-yl]-1-[(2R)-3,3-dimethylbutan-2-yl]-1,3-dihydro-2H-benzimidazol-2-one
Homo sapiens
pH and temperature not specified in the publication
0.00272
N-[(1R)-1-(4-chlorophenyl)ethyl]-3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000076
N-[(1S)-1-(2-chloropyrimidin-5-yl)ethyl]-3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.00029
N-[(1S)-1-(4-chlorophenyl)ethyl]-3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0001 - 0.169
N-[(1S)-1-(5-bromopyridin-2-yl)ethyl]-3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide
0.00089
N-[(1S)-1-(5-chloropyrazin-2-yl)ethyl]-3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.00023
N-[(1S)-1-(5-chloropyridin-2-yl)ethyl]-3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.00043
N-[(1S)-1-(5-chloropyrimidin-2-yl)ethyl]-3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.00061
N-[(4-chlorophenyl)methyl]-3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.00084
N-[2-(4-chlorophenyl)propan-2-yl]-3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000053
1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(2S)-2-(1H-indol-2-yl)-2-methyl-5-oxo-2,5-dihydro-1H-imidazol-4-yl]-1,3-dihydro-2H-benzimidazol-2-one

Homo sapiens
pH and temperature not specified in the publication
0.000055
1-[(2R)-3,3-dimethylbutan-2-yl]-6-[(2S)-2-(1H-indol-2-yl)-2-methyl-5-oxo-2,5-dihydro-1H-imidazol-4-yl]-1,3-dihydro-2H-benzimidazol-2-one
Homo sapiens
pH and temperature not specified in the publication
0.00006
3-[(2R)-3,3-dimethylbutan-2-yl]-N-(2,3-dimethyl-1H-indol-6-yl)-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide

Homo sapiens
pH and temperature not specified in the publication
0.165
3-[(2R)-3,3-dimethylbutan-2-yl]-N-(2,3-dimethyl-1H-indol-6-yl)-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0001
N-[(1S)-1-(5-bromopyridin-2-yl)ethyl]-3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide

Homo sapiens
pH and temperature not specified in the publication
0.169
N-[(1S)-1-(5-bromopyridin-2-yl)ethyl]-3-[(2R)-3,3-dimethylbutan-2-yl]-2-oxo-2,3-dihydro-1H-benzimidazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
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Van den Eijnden, D.H.; Winterwerp, H.; Smeeman, P.; Schiphorst, W.E.C.M.
Novikoff ascites tumor cells contain N-acetyllactosaminide beta 1-3 and beta 1-6 N-acetylglucosaminyltransferase activity
J. Biol. Chem.
258
3435-3437
1983
Rattus norvegicus
brenda
Zielenski, J.; Koscielak, J.
The occurrence of two novel N-acetylglucosaminyltransferase activities in human serum
FEBS Lett.
158
164-168
1983
Homo sapiens
brenda
Hosomi, O.; Takeya, A.; Kogure, T.
Human serum contains N-acetyllactosamine: beta 1-3 N-acetylglucosaminyltransferase activity
J. Biochem.
95
1655-1659
1984
Homo sapiens
brenda
Holmes, E.H.
Characterization of a beta 1-->3-N-acetylglucosaminyltransferase associated with synthesis of type 1 and type 2 lacto-series tumor-associated antigens from the human colonic adenocarcinoma cell line SW403
Arch. Biochem. Biophys.
260
461-468
1988
Homo sapiens
brenda
van den Eijnden, D.H.; Koenderman, A.H.L.; Schiphorst, W.E.C.M.
Biosynthesis of blood group i-active polylactosaminoglycans. Partial purification and properties of an UDP-GlcNAc:N-acetyllactosaminide beta 1-->3-N-acetylglucosaminyltransferase from Novikoff tumor cell ascites fluid
J. Biol. Chem.
263
12461-12471
1988
Rattus norvegicus
brenda
Kawashima, H.; Yamamoto, K.; Osawa, T.; Irimura, T.
Purification and characterization of UDP-GlcNAc:Galbeta 1-4Glc(NAc)beta-1,3-N-acetylglucosaminyltransferase (poly-N-acetyllactosamine extension enzyme) from calf serum
J. Biol. Chem.
268
27118-27126
1993
Bos taurus
brenda
McAuliffe, J.C.; Ujita, M.; Fukuda, M.; Hindsgaul, O.
Synthesis of selectively radiolabeled hexasaccharides for the determination of enzymatic regioselectivity
Glycoconjugate J.
16
767-772
1999
Homo sapiens
brenda
Fukuzumi, M.; Maruyama, S.; Sano, M.; Fukui, S.
Comparison of the expression of cell surface poly-N-acetyllactosamine-type oligosaccharides in PC12 cells with those in its variant PC12D
Glycobiology
11
481-494
2001
Rattus norvegicus
brenda
Kataoka, K.; Huh, N.h.
A novel beta1,3-N-acetylglucosaminyltransferase involved in invasion of cancer cells as assayed in vitro
Biochem. Biophys. Res. Commun.
294
843-848
2002
Homo sapiens (Q8NFL0), Homo sapiens, Mus musculus (Q8K0J2), Mus musculus, Mus musculus beta3GnT7 (Q8K0J2)
brenda
Sasaki, K.; Kurata-Miura, K.; Ujita, M.; Angata, K.; Nakagawa, S.; Sekine, S.; Nishi, T.; Fukuda, M.
Expression cloning of cDNA encoding a human beta-1,3-N-acetylglucosaminyltransferase that is essential for poly-N-acetyllactosamine synthesis
Proc. Natl. Acad. Sci. USA
94
14294-14299
1997
Homo sapiens (O43505)
brenda
Salo, H.; Aitio, O.; Ilves, K.; Bencomo, E.; Toivonen, S.; Penttil, L.; Niemel, R.; Salminen, H.; Grabenhorst, E.; Renkonen, R.; Renkonen, O.
Several polylactosamine-modifying glycosyltransferases also use internal GalNAcbeta1-4GlcNAc units of synthetic saccharides as acceptors
Glycobiology
12
217-228
2002
Homo sapiens
brenda
Hummel, M.; Hedrich, H.C.; Hasilik, A.
Elongation of N-acetyllactosamine repeats in diantennary oligosaccharides
Eur. J. Biochem.
245
428-433
1997
Cricetulus griseus
brenda
Basu, M.; Basu, S.
Biosynthesis in vitro of Ii core glycosphingolipids from neolactotetraosylceramide by beta1-3- and beta1-6-N-acetylglucosaminyltransferases from mouse T-lymphoma
J. Biol. Chem.
259
12557-12562
1984
Mus musculus
brenda
Seko, A.; Yamashita, K.
beta1,3-N-Acetylglucosaminyltransferase-7 (beta3Gn-T7) acts efficiently on keratan sulfate-related glycans
FEBS Lett.
556
216-220
2004
Homo sapiens
brenda
Biellmann, F.; Henion, T.R.; Burki, K.; Hennet, T.
Impaired sexual behavior in male mice deficient for the beta 1-3 N-acetylglucosaminyltransferase-I gene
Mol. Reprod. Dev.
75
699-706
2008
Mus musculus
brenda
Lee, P.L.; Kohler, J.J.; Pfeffer, S.R.
Association of beta-1,3-N-acetylglucosaminyltransferase 1 and beta-1,4-galactosyltransferase 1, trans-Golgi enzymes involved in coupled poly-N-acetyllactosamine synthesis
Glycobiology
19
655-664
2009
Homo sapiens
brenda
Bao, X.; Kobayashi, M.; Hatakeyama, S.; Angata, K.; Gullberg, D.; Nakayama, J.; Fukuda, M.; Fukuda, M.
Tumor suppressor function of laminin-binding alpha-dystroglycan requires a distinct beta3-N-acetylglucosaminyltransferase
Proc. Natl. Acad. Sci. USA
106
12109-12114
2009
Homo sapiens
brenda
Peng, W.; Pranskevich, J.; Nycholat, C.; Gilbert, M.; Wakarchuk, W.; Paulson, J.C.; Razi, N.
Helicobacter pylori beta1,3-N-acetylglucosaminyltransferase for versatile synthesis of type 1 and type 2 poly-LacNAcs on N-linked, O-linked and I-antigen glycans
Glycobiology
22
1453-1464
2012
Helicobacter pylori
brenda
Gao, L.; Zhang, H.; Zhang, B.; Zhu, J.; Chen, C.; Liu, W.
B3GNT3 overexpression is associated with unfavourable survival in non-small cell lung cancer
J. Clin. Pathol.
71
642-647
2018
Homo sapiens (Q9Y2A9), Homo sapiens
brenda
Wang, J.S.; Ruan, F.; Guo, L.Z.; Wang, F.G.; Wang, F.L.; An, H.M.
B3GNT3 acts as a carcinogenic factor in endometrial cancer via facilitating cell growth, invasion and migration through regulating RhoA/RAC1 pathway-associated markers
Genes Genomics
43
447-457
2021
Homo sapiens (Q9Y2A9)
brenda
Hao, Y.; Crequer-Grandhomme, A.; Javier, N.; Singh, A.; Chen, H.; Manzanillo, P.; Lo, M.C.; Huang, X.
Structures and mechanism of human glycosyltransferase beta1,3-N-acetylglucosaminyltransferase 2 (B3GNT2), an important player in immune homeostasis
J. Biol. Chem.
296
100042
2021
Homo sapiens (Q9NY97)
brenda
Jackson, J.J.; Siegmund, A.C.; Bai, W.J.; Reed, A.B.; Birkholz, A.B.; Campuzano, I.D.G.; Crequer-Grandhomme, A.; Hu, R.; Modak, R.V.; Sudom, A.; Javier, N.; Sanders, C.; Lo, M.C.; Xie, F.; Cee, V.J.; Manzanillo, P.; Allen, J.G.
Imidazolone as an amide bioisostere in the development of beta-1,3-N-acetylglucosaminyltransferase 2 (B3GNT2) inhibitors
J. Med. Chem.
66
16120-16140
2023
Homo sapiens (Q9NY97), Homo sapiens (Q9C0J1)
brenda