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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
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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->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 + 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 + betaGlc-O(CH2)7CH3
?
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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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?
additional information
?
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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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?
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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?
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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?
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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R represents the remainder of the N-oligosaccharide core (n fucose), R: H or 1,4-(+/-)-fucose-1,6-N-acetylglucosaminyl-1-N-asparagine
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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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acceptors are free and protein-matrix-bound glycans
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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
-
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
-
-
?
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3.7
3-deoxy-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta-octyl
-
-
0.26
3-O-methyl-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta-octyl
-
-
0.22
4-deoxy-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta-octyl
-
-
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
0.26
4-O-methyl-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta-octyl
-
-
0.25
6-deoxy-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta-octyl
-
-
0.2
6-O-methyl-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta-octyl
-
-
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
0.55
Manalpha(1-6)(GlcNAcbeta(1-2)-6-deoxy-Manalpha(1-3))Manbeta-octyl
-
-
0.16
Manalpha(1-6)(GlcNAcbeta(1-2)4-O-methyl-Manalpha(1-3))Manbeta-octyl
-
-
0.48
Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))-4-deoxy-Manbeta-octyl
-
-
0.13
Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta-octyl
-
-
0.295 - 4.3
UDP-alpha-D-GlcNAc
0.018 - 0.96
UDP-N-acetylglucosamine
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
1.09
UDP-alpha-D-GlcNAc
pH 7.0, 37°C, recombinant mutant Y294A
1.4
UDP-alpha-D-GlcNAc
pH 7.0, 37°C, recombinant mutant N318A
1.49
UDP-alpha-D-GlcNAc
pH 7.0, 37°C, recombinant mutant R198A
2.14
UDP-alpha-D-GlcNAc
pH 7.0, 37°C, recombinant mutant Y344A
2.36
UDP-alpha-D-GlcNAc
pH 7.0, 37°C, recombinant mutant D217A
4.3
UDP-alpha-D-GlcNAc
pH 7.0, 37°C, recombinant mutant E259A
0.018
UDP-N-acetylglucosamine
-
pH 6.5
0.23
UDP-N-acetylglucosamine
-
pH 6.5, 37°C
0.96
UDP-N-acetylglucosamine
-
pH 6.5, 37°C
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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
-
part of N-glycan pathway
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
-
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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
5771-5774
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
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Zhang, W.; Revers, L.; Pierce, M.; Schachter, H.
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