Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-102 |
Sentence |
denotes |
Studies on the glycosylation of wild-type and mutant forms of Aspergillus niger pectin methylesterase. |
TextSentencer_T2 |
103-278 |
Sentence |
denotes |
Pectin methylesterase (PME) is one of a number of enzymes released by the fungus Aspergillus niger that are involved in the degradation of specific plant cell-wall structures. |
TextSentencer_T3 |
279-355 |
Sentence |
denotes |
PME is a glycoprotein with three potential sites for N-linked glycosylation. |
TextSentencer_T4 |
356-445 |
Sentence |
denotes |
The glycosylation may affect the hydrolytic activity or the substrate specificity of PME. |
TextSentencer_T5 |
446-573 |
Sentence |
denotes |
In this work, we investigate first the structures and the attachment sites of the glycans present on recombinant wild-type PME. |
TextSentencer_T6 |
574-722 |
Sentence |
denotes |
Further, a series of PME mutants was created in which the three potential N-linked glycosylation sites were eliminated in all possible combinations. |
TextSentencer_T7 |
723-795 |
Sentence |
denotes |
The glycosylation of the mutants and their activities were then studied. |
TextSentencer_T8 |
796-967 |
Sentence |
denotes |
Mass spectrometric techniques tailored for carbohydrate analysis were applied to both characterize the glycan structures and to determine the specific sites of attachment. |
TextSentencer_T9 |
968-1082 |
Sentence |
denotes |
High mannose structures with variable numbers of mannose were found on the wild-type, as well as the mutant forms. |
TextSentencer_T10 |
1083-1177 |
Sentence |
denotes |
Studies using the mutants suggest that glycosylation does not strongly influence the activity. |
TextSentencer_T11 |
1178-1296 |
Sentence |
denotes |
Whether it may affect the substrate specify of the enzyme is unknown, and that aspect will be explored in future work. |
T1 |
0-102 |
Sentence |
denotes |
Studies on the glycosylation of wild-type and mutant forms of Aspergillus niger pectin methylesterase. |
T2 |
103-278 |
Sentence |
denotes |
Pectin methylesterase (PME) is one of a number of enzymes released by the fungus Aspergillus niger that are involved in the degradation of specific plant cell-wall structures. |
T3 |
279-355 |
Sentence |
denotes |
PME is a glycoprotein with three potential sites for N-linked glycosylation. |
T4 |
356-445 |
Sentence |
denotes |
The glycosylation may affect the hydrolytic activity or the substrate specificity of PME. |
T5 |
446-573 |
Sentence |
denotes |
In this work, we investigate first the structures and the attachment sites of the glycans present on recombinant wild-type PME. |
T6 |
574-722 |
Sentence |
denotes |
Further, a series of PME mutants was created in which the three potential N-linked glycosylation sites were eliminated in all possible combinations. |
T7 |
723-795 |
Sentence |
denotes |
The glycosylation of the mutants and their activities were then studied. |
T8 |
796-967 |
Sentence |
denotes |
Mass spectrometric techniques tailored for carbohydrate analysis were applied to both characterize the glycan structures and to determine the specific sites of attachment. |
T9 |
968-1082 |
Sentence |
denotes |
High mannose structures with variable numbers of mannose were found on the wild-type, as well as the mutant forms. |
T10 |
1083-1177 |
Sentence |
denotes |
Studies using the mutants suggest that glycosylation does not strongly influence the activity. |
T11 |
1178-1296 |
Sentence |
denotes |
Whether it may affect the substrate specify of the enzyme is unknown, and that aspect will be explored in future work. |