| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-126 |
Sentence |
denotes |
Distantly related plant and nematode core α1,3-fucosyltransferases display similar trends in structure-function relationships. |
| TextSentencer_T2 |
127-369 |
Sentence |
denotes |
Here, we present a comparative structure-function study of a nematode and a plant core α1,3-fucosyltransferase based on deletion and point mutations of the coding regions of Caenorhabditis elegans FUT-1 and Arabidopsis thaliana FucTA (FUT11). |
| TextSentencer_T3 |
370-513 |
Sentence |
denotes |
In particular, our results reveal a novel "first cluster motif" shared by both core and Lewis-type α1,3-fucosyltransferases of the GT10 family. |
| TextSentencer_T4 |
514-650 |
Sentence |
denotes |
To evaluate the role of the conserved serine within this motif, this residue was replaced with alanine in FucTA (S218) and FUT-1 (S243). |
| TextSentencer_T5 |
651-797 |
Sentence |
denotes |
The S218A replacement completely abolished the enzyme activity of FucTA, while the S243A mutant of FUT-1 retained 20% of the "wild-type" activity. |
| TextSentencer_T6 |
798-1004 |
Sentence |
denotes |
Based on the results of homology modeling of FucTA, other residues potentially involved in the donor substrate binding were examined, and mutations of N219 and R226 dramatically affected enzymatic activity. |
| TextSentencer_T7 |
1005-1118 |
Sentence |
denotes |
Finally, as both FucTA and FUT-1 were shown to be N-glycosylated, we examined the putative N-glycosylation sites. |
| TextSentencer_T8 |
1119-1327 |
Sentence |
denotes |
While alanine replacements at single potential N-glycosylation sites of FucTA resulted in a loss of up to 80% of the activity, a triple glycosylation site mutant still retained 5%, as compared to the control. |
| TextSentencer_T9 |
1328-1593 |
Sentence |
denotes |
In summary, our data indicate similar trends in structure-function relationships of distantly related enzymes which perform similar biochemical reactions and form the basis for future work aimed at understanding the structure of α1,3-fucosyltransferases in general. |
| T1 |
0-126 |
Sentence |
denotes |
Distantly related plant and nematode core α1,3-fucosyltransferases display similar trends in structure-function relationships. |
| T2 |
127-369 |
Sentence |
denotes |
Here, we present a comparative structure-function study of a nematode and a plant core α1,3-fucosyltransferase based on deletion and point mutations of the coding regions of Caenorhabditis elegans FUT-1 and Arabidopsis thaliana FucTA (FUT11). |
| T3 |
370-513 |
Sentence |
denotes |
In particular, our results reveal a novel "first cluster motif" shared by both core and Lewis-type α1,3-fucosyltransferases of the GT10 family. |
| T4 |
514-650 |
Sentence |
denotes |
To evaluate the role of the conserved serine within this motif, this residue was replaced with alanine in FucTA (S218) and FUT-1 (S243). |
| T5 |
651-797 |
Sentence |
denotes |
The S218A replacement completely abolished the enzyme activity of FucTA, while the S243A mutant of FUT-1 retained 20% of the "wild-type" activity. |
| T6 |
798-1004 |
Sentence |
denotes |
Based on the results of homology modeling of FucTA, other residues potentially involved in the donor substrate binding were examined, and mutations of N219 and R226 dramatically affected enzymatic activity. |
| T7 |
1005-1118 |
Sentence |
denotes |
Finally, as both FucTA and FUT-1 were shown to be N-glycosylated, we examined the putative N-glycosylation sites. |
| T8 |
1119-1327 |
Sentence |
denotes |
While alanine replacements at single potential N-glycosylation sites of FucTA resulted in a loss of up to 80% of the activity, a triple glycosylation site mutant still retained 5%, as compared to the control. |
| T9 |
1328-1593 |
Sentence |
denotes |
In summary, our data indicate similar trends in structure-function relationships of distantly related enzymes which perform similar biochemical reactions and form the basis for future work aimed at understanding the structure of α1,3-fucosyltransferases in general. |
| T1 |
0-126 |
Sentence |
denotes |
Distantly related plant and nematode core α1,3-fucosyltransferases display similar trends in structure-function relationships. |
| T2 |
127-369 |
Sentence |
denotes |
Here, we present a comparative structure-function study of a nematode and a plant core α1,3-fucosyltransferase based on deletion and point mutations of the coding regions of Caenorhabditis elegans FUT-1 and Arabidopsis thaliana FucTA (FUT11). |
| T3 |
370-513 |
Sentence |
denotes |
In particular, our results reveal a novel "first cluster motif" shared by both core and Lewis-type α1,3-fucosyltransferases of the GT10 family. |
| T4 |
514-650 |
Sentence |
denotes |
To evaluate the role of the conserved serine within this motif, this residue was replaced with alanine in FucTA (S218) and FUT-1 (S243). |
| T5 |
651-797 |
Sentence |
denotes |
The S218A replacement completely abolished the enzyme activity of FucTA, while the S243A mutant of FUT-1 retained 20% of the "wild-type" activity. |
| T6 |
798-1004 |
Sentence |
denotes |
Based on the results of homology modeling of FucTA, other residues potentially involved in the donor substrate binding were examined, and mutations of N219 and R226 dramatically affected enzymatic activity. |
| T7 |
1005-1118 |
Sentence |
denotes |
Finally, as both FucTA and FUT-1 were shown to be N-glycosylated, we examined the putative N-glycosylation sites. |
| T8 |
1119-1327 |
Sentence |
denotes |
While alanine replacements at single potential N-glycosylation sites of FucTA resulted in a loss of up to 80% of the activity, a triple glycosylation site mutant still retained 5%, as compared to the control. |
| T9 |
1328-1593 |
Sentence |
denotes |
In summary, our data indicate similar trends in structure-function relationships of distantly related enzymes which perform similar biochemical reactions and form the basis for future work aimed at understanding the structure of α1,3-fucosyltransferases in general. |
