Pub. Date : 2012 Jan
PMID : 22024534
22 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | However, the specificity of XYLT for N-glycans has not yet been completely clarified. | n-glycans | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 2 | To gain insights into the function of XYLT in the plant N-glycosylation pathway, we examined the acceptor substrate specificity of recombinant Arabidopsis XYLT (AtXYLT) using 2-aminopyridine-labeled N-glycans as the substrates and confirmed the N-glycans of Arabidopsis xylt mutant. | Nitrogen | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 3 | To gain insights into the function of XYLT in the plant N-glycosylation pathway, we examined the acceptor substrate specificity of recombinant Arabidopsis XYLT (AtXYLT) using 2-aminopyridine-labeled N-glycans as the substrates and confirmed the N-glycans of Arabidopsis xylt mutant. | Nitrogen | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 4 | To gain insights into the function of XYLT in the plant N-glycosylation pathway, we examined the acceptor substrate specificity of recombinant Arabidopsis XYLT (AtXYLT) using 2-aminopyridine-labeled N-glycans as the substrates and confirmed the N-glycans of Arabidopsis xylt mutant. | alpha-aminopyridine | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 5 | To gain insights into the function of XYLT in the plant N-glycosylation pathway, we examined the acceptor substrate specificity of recombinant Arabidopsis XYLT (AtXYLT) using 2-aminopyridine-labeled N-glycans as the substrates and confirmed the N-glycans of Arabidopsis xylt mutant. | alpha-aminopyridine | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 6 | To gain insights into the function of XYLT in the plant N-glycosylation pathway, we examined the acceptor substrate specificity of recombinant Arabidopsis XYLT (AtXYLT) using 2-aminopyridine-labeled N-glycans as the substrates and confirmed the N-glycans of Arabidopsis xylt mutant. | n-glycans | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 7 | To gain insights into the function of XYLT in the plant N-glycosylation pathway, we examined the acceptor substrate specificity of recombinant Arabidopsis XYLT (AtXYLT) using 2-aminopyridine-labeled N-glycans as the substrates and confirmed the N-glycans of Arabidopsis xylt mutant. | n-glycans | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 8 | To gain insights into the function of XYLT in the plant N-glycosylation pathway, we examined the acceptor substrate specificity of recombinant Arabidopsis XYLT (AtXYLT) using 2-aminopyridine-labeled N-glycans as the substrates and confirmed the N-glycans of Arabidopsis xylt mutant. | n-glycans | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 9 | To gain insights into the function of XYLT in the plant N-glycosylation pathway, we examined the acceptor substrate specificity of recombinant Arabidopsis XYLT (AtXYLT) using 2-aminopyridine-labeled N-glycans as the substrates and confirmed the N-glycans of Arabidopsis xylt mutant. | n-glycans | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 10 | Recombinant AtXYLT expressed in insect cells required the beta1,2-linked N-acetylglucosamine (GlcNAc) residue at the nonreducing terminus of the alpha1,3-branched mannose (Man) residue (GlcNAcbeta1,2-Manalpha1,3-Man; GNM3B) for activity. | 2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 11 | Recombinant AtXYLT expressed in insect cells required the beta1,2-linked N-acetylglucosamine (GlcNAc) residue at the nonreducing terminus of the alpha1,3-branched mannose (Man) residue (GlcNAcbeta1,2-Manalpha1,3-Man; GNM3B) for activity. | glcnacbeta1 | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 12 | Recombinant AtXYLT expressed in insect cells required the beta1,2-linked N-acetylglucosamine (GlcNAc) residue at the nonreducing terminus of the alpha1,3-branched mannose (Man) residue (GlcNAcbeta1,2-Manalpha1,3-Man; GNM3B) for activity. | 2-manalpha1 | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 13 | Recombinant AtXYLT expressed in insect cells required the beta1,2-linked N-acetylglucosamine (GlcNAc) residue at the nonreducing terminus of the alpha1,3-branched mannose (Man) residue (GlcNAcbeta1,2-Manalpha1,3-Man; GNM3B) for activity. | 3-man | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 14 | Recombinant AtXYLT expressed in insect cells required the beta1,2-linked N-acetylglucosamine (GlcNAc) residue at the nonreducing terminus of the alpha1,3-branched mannose (Man) residue (GlcNAcbeta1,2-Manalpha1,3-Man; GNM3B) for activity. | gnm3b | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 15 | However, AtXYLT showed decreased activity with substrates that contained alpha1,3-fucose at the chitobiose core-GlcNAc or a terminal GlcNAc at the alpha1,6-branched Man residue of GlcNAcbeta1,2-Man (GlcNAcbeta1,2-Manalpha1,6-Man; GNM3A), whose ratios were 10% and 50% of the optimal substrate, GNM3B, respectively. | 2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 16 | However, AtXYLT showed decreased activity with substrates that contained alpha1,3-fucose at the chitobiose core-GlcNAc or a terminal GlcNAc at the alpha1,6-branched Man residue of GlcNAcbeta1,2-Man (GlcNAcbeta1,2-Manalpha1,6-Man; GNM3A), whose ratios were 10% and 50% of the optimal substrate, GNM3B, respectively. | 2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 17 | However, AtXYLT showed decreased activity with substrates that contained alpha1,3-fucose at the chitobiose core-GlcNAc or a terminal GlcNAc at the alpha1,6-branched Man residue of GlcNAcbeta1,2-Man (GlcNAcbeta1,2-Manalpha1,6-Man; GNM3A), whose ratios were 10% and 50% of the optimal substrate, GNM3B, respectively. | glcnacbeta1 | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 18 | However, AtXYLT showed decreased activity with substrates that contained alpha1,3-fucose at the chitobiose core-GlcNAc or a terminal GlcNAc at the alpha1,6-branched Man residue of GlcNAcbeta1,2-Man (GlcNAcbeta1,2-Manalpha1,6-Man; GNM3A), whose ratios were 10% and 50% of the optimal substrate, GNM3B, respectively. | 2-man | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 19 | However, AtXYLT showed decreased activity with substrates that contained alpha1,3-fucose at the chitobiose core-GlcNAc or a terminal GlcNAc at the alpha1,6-branched Man residue of GlcNAcbeta1,2-Man (GlcNAcbeta1,2-Manalpha1,6-Man; GNM3A), whose ratios were 10% and 50% of the optimal substrate, GNM3B, respectively. | glcnacbeta1 | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 20 | However, AtXYLT showed decreased activity with substrates that contained alpha1,3-fucose at the chitobiose core-GlcNAc or a terminal GlcNAc at the alpha1,6-branched Man residue of GlcNAcbeta1,2-Man (GlcNAcbeta1,2-Manalpha1,6-Man; GNM3A), whose ratios were 10% and 50% of the optimal substrate, GNM3B, respectively. | 2-manalpha1,6-man | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 21 | Moreover, AtXYLT did not show any activity in the transfer of the Xyl residue to N-glycans that contained a mammalian-type beta1,4-linked galactose (Gal) residue at the nonreducing terminus of GlcNAcbeta1,2-Man. | glcnacbeta1 | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 22 | These findings suggest that AtXYLT acts on protein-bound N-glycans prior to alpha1,3-fucosyltransferase and mannosidase II in planta. | n-glycans | beta-1,2-xylosyltransferase | Arabidopsis thaliana |