Pub. Date : 2005 Jun 1
PMID : 15686448
8 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Arabidopsis thaliana beta1,2-xylosyltransferase: an unusual glycosyltransferase with the potential to act at multiple stages of the plant N-glycosylation pathway. | Nitrogen | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 2 | XylT (beta1,2-xylosyltransferase) is a unique Golgi-bound glycosyltransferase that is involved in the biosynthesis of glycoprotein-bound N-glycans in plants. | n-glycans | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 3 | XylT (beta1,2-xylosyltransferase) is a unique Golgi-bound glycosyltransferase that is involved in the biosynthesis of glycoprotein-bound N-glycans in plants. | n-glycans | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 4 | Characterization of the N-glycosylation status of recombinant XylT revealed that all three potential N-glycosylation sites of the protein are occupied by N-linked oligosaccharides. | Nitrogen | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 5 | Characterization of the N-glycosylation status of recombinant XylT revealed that all three potential N-glycosylation sites of the protein are occupied by N-linked oligosaccharides. | Nitrogen | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 6 | Characterization of the N-glycosylation status of recombinant XylT revealed that all three potential N-glycosylation sites of the protein are occupied by N-linked oligosaccharides. | n-linked oligosaccharides | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 7 | In contrast with most other glycosyltransferases, XylT is enzymatically active in the absence of added metal ions. | Metals | beta-1,2-xylosyltransferase | Arabidopsis thaliana |
| 8 | These experiments revealed that the substrate specificity of XylT permits the enzyme to act at multiple stages of the plant N-glycosylation pathway. | Nitrogen | beta-1,2-xylosyltransferase | Arabidopsis thaliana |