| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-133 |
Sentence |
denotes |
A sequence motif involved in the donor substrate binding by alpha1,6-fucosyltransferase: the role of the conserved arginine residues. |
| T1 |
0-133 |
Sentence |
denotes |
A sequence motif involved in the donor substrate binding by alpha1,6-fucosyltransferase: the role of the conserved arginine residues. |
| TextSentencer_T2 |
134-258 |
Sentence |
denotes |
Alpha1,6-fucosyltransferase catalyzes the transfer of fucose to the innermost GlcNAc residue of an N-linked oligosaccharide. |
| T2 |
134-258 |
Sentence |
denotes |
Alpha1,6-fucosyltransferase catalyzes the transfer of fucose to the innermost GlcNAc residue of an N-linked oligosaccharide. |
| TextSentencer_T3 |
259-559 |
Sentence |
denotes |
In order to identify the amino acid residue(s) which are associated with the enzyme activity and to investigate their function, we prepared a series of mutant human alpha1,6-fucosyltransferases in which the conserved residues in the region homologous to alpha1,2-fucosyltransferase had been replaced. |
| T3 |
259-559 |
Sentence |
denotes |
In order to identify the amino acid residue(s) which are associated with the enzyme activity and to investigate their function, we prepared a series of mutant human alpha1,6-fucosyltransferases in which the conserved residues in the region homologous to alpha1,2-fucosyltransferase had been replaced. |
| TextSentencer_T4 |
560-619 |
Sentence |
denotes |
These proteins were then characterized by kinetic analyses. |
| T4 |
560-619 |
Sentence |
denotes |
These proteins were then characterized by kinetic analyses. |
| TextSentencer_T5 |
620-728 |
Sentence |
denotes |
The wild-type and mutant alpha1,6-fucosyltransferases were expressed using a baculovirus-insect cell system. |
| T5 |
620-728 |
Sentence |
denotes |
The wild-type and mutant alpha1,6-fucosyltransferases were expressed using a baculovirus-insect cell system. |
| TextSentencer_T6 |
729-950 |
Sentence |
denotes |
The activity assay showed that replacement of Arg-365 by Ala or Lys led to a complete loss of activity while substitution of Ala or Lys for the neighboring Arg-366 decreased the activity to about 3% that of the wild type. |
| T6 |
729-950 |
Sentence |
denotes |
The activity assay showed that replacement of Arg-365 by Ala or Lys led to a complete loss of activity while substitution of Ala or Lys for the neighboring Arg-366 decreased the activity to about 3% that of the wild type. |
| TextSentencer_T7 |
951-1160 |
Sentence |
denotes |
Kinetic analyses revealed that the replacements of Arg-366 lead to an increase in the apparent K (m) value for both GDP-fucose and the acceptor oligosaccharide but did not markedly affect the apparent V (max). |
| T7 |
951-1160 |
Sentence |
denotes |
Kinetic analyses revealed that the replacements of Arg-366 lead to an increase in the apparent K (m) value for both GDP-fucose and the acceptor oligosaccharide but did not markedly affect the apparent V (max). |
| TextSentencer_T8 |
1161-1349 |
Sentence |
denotes |
When these mutants were inhibited by GDP in a competitive manner with respect to the donor substrate, the K (i) values were found to be 50-100 times higher than the value in the wild type. |
| T8 |
1161-1349 |
Sentence |
denotes |
When these mutants were inhibited by GDP in a competitive manner with respect to the donor substrate, the K (i) values were found to be 50-100 times higher than the value in the wild type. |
| TextSentencer_T9 |
1350-1471 |
Sentence |
denotes |
On the other hand, in the inhibition by GMP, the K (i) values for the mutants were very similar to that of the wild type. |
| T9 |
1350-1471 |
Sentence |
denotes |
On the other hand, in the inhibition by GMP, the K (i) values for the mutants were very similar to that of the wild type. |
| TextSentencer_T10 |
1472-1701 |
Sentence |
denotes |
These findings suggest that Arg-366 contributes to the binding of GDP-fucose via an interaction with the beta-phosphoryl group of the GDP moiety of the donor, and that Arg-365 may also play an essential role in substrate binding. |
| T10 |
1472-1701 |
Sentence |
denotes |
These findings suggest that Arg-366 contributes to the binding of GDP-fucose via an interaction with the beta-phosphoryl group of the GDP moiety of the donor, and that Arg-365 may also play an essential role in substrate binding. |
| TextSentencer_T11 |
1702-1849 |
Sentence |
denotes |
The results suggest that the motif common to alpha1,2- and alpha1,6-fucosyltransferases is critical for binding of the donor substrate, GDP-fucose. |
| T11 |
1702-1849 |
Sentence |
denotes |
The results suggest that the motif common to alpha1,2- and alpha1,6-fucosyltransferases is critical for binding of the donor substrate, GDP-fucose. |