| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-140 |
Sentence |
denotes |
Biochemical characterization of WbdN, a β1,3-glucosyltransferase involved in O-antigen synthesis in enterohemorrhagic Escherichia coli O157. |
| T1 |
0-140 |
Sentence |
denotes |
Biochemical characterization of WbdN, a β1,3-glucosyltransferase involved in O-antigen synthesis in enterohemorrhagic Escherichia coli O157. |
| T1 |
0-140 |
Sentence |
denotes |
Biochemical characterization of WbdN, a β1,3-glucosyltransferase involved in O-antigen synthesis in enterohemorrhagic Escherichia coli O157. |
| TextSentencer_T2 |
141-364 |
Sentence |
denotes |
The enterohemorrhagic O157 strain of Escherichia coli, which is one of the most well-known bacterial pathogens, has an O-antigen repeating unit structure with the sequence [-2-d-Rha4NAcα1-3-l-Fucα1-4-d-Glcβ1-3-d-GalNAcα1-]. |
| T2 |
141-364 |
Sentence |
denotes |
The enterohemorrhagic O157 strain of Escherichia coli, which is one of the most well-known bacterial pathogens, has an O-antigen repeating unit structure with the sequence [-2-d-Rha4NAcα1-3-l-Fucα1-4-d-Glcβ1-3-d-GalNAcα1-]. |
| T2 |
141-364 |
Sentence |
denotes |
The enterohemorrhagic O157 strain of Escherichia coli, which is one of the most well-known bacterial pathogens, has an O-antigen repeating unit structure with the sequence [-2-d-Rha4NAcα1-3-l-Fucα1-4-d-Glcβ1-3-d-GalNAcα1-]. |
| TextSentencer_T3 |
365-497 |
Sentence |
denotes |
The O-antigen gene cluster of E. coli O157 contains the genes responsible for the assembly of this repeating unit and includes wbdN. |
| T3 |
365-497 |
Sentence |
denotes |
The O-antigen gene cluster of E. coli O157 contains the genes responsible for the assembly of this repeating unit and includes wbdN. |
| T3 |
365-497 |
Sentence |
denotes |
The O-antigen gene cluster of E. coli O157 contains the genes responsible for the assembly of this repeating unit and includes wbdN. |
| TextSentencer_T4 |
498-635 |
Sentence |
denotes |
In spite of cloning many O-antigen genes, biochemical characterization has been done on very few enzymes involved in O-antigen synthesis. |
| T4 |
498-635 |
Sentence |
denotes |
In spite of cloning many O-antigen genes, biochemical characterization has been done on very few enzymes involved in O-antigen synthesis. |
| T4 |
498-635 |
Sentence |
denotes |
In spite of cloning many O-antigen genes, biochemical characterization has been done on very few enzymes involved in O-antigen synthesis. |
| TextSentencer_T5 |
636-734 |
Sentence |
denotes |
In this work, we expressed the wbdN gene in E. coli BL21, and the His-tagged protein was purified. |
| T5 |
636-734 |
Sentence |
denotes |
In this work, we expressed the wbdN gene in E. coli BL21, and the His-tagged protein was purified. |
| T5 |
636-734 |
Sentence |
denotes |
In this work, we expressed the wbdN gene in E. coli BL21, and the His-tagged protein was purified. |
| TextSentencer_T6 |
735-884 |
Sentence |
denotes |
WbdN activity was characterized using the donor substrate UDP-[(14)C]Glc and the synthetic acceptor substrate GalNAcα-O-PO(3)-PO(3)-(CH(2))(11)-O-Ph. |
| T6 |
735-884 |
Sentence |
denotes |
WbdN activity was characterized using the donor substrate UDP-[(14)C]Glc and the synthetic acceptor substrate GalNAcα-O-PO(3)-PO(3)-(CH(2))(11)-O-Ph. |
| T6 |
735-1047 |
Sentence |
denotes |
WbdN activity was characterized using the donor substrate UDP-[(14)C]Glc and the synthetic acceptor substrate GalNAcα-O-PO(3)-PO(3)-(CH(2))(11)-O-Ph. The enzyme product was isolated by high pressure liquid chromatography, and mass spectrometry showed that one Glc residue was transferred to the acceptor by WbdN. |
| TextSentencer_T7 |
885-1047 |
Sentence |
denotes |
The enzyme product was isolated by high pressure liquid chromatography, and mass spectrometry showed that one Glc residue was transferred to the acceptor by WbdN. |
| T7 |
885-1047 |
Sentence |
denotes |
The enzyme product was isolated by high pressure liquid chromatography, and mass spectrometry showed that one Glc residue was transferred to the acceptor by WbdN. |
| TextSentencer_T8 |
1048-1154 |
Sentence |
denotes |
Nuclear magnetic resonance analysis of the product structure indicated that Glc was β1-3 linked to GalNAc. |
| T7 |
1048-1154 |
Sentence |
denotes |
Nuclear magnetic resonance analysis of the product structure indicated that Glc was β1-3 linked to GalNAc. |
| T8 |
1048-1154 |
Sentence |
denotes |
Nuclear magnetic resonance analysis of the product structure indicated that Glc was β1-3 linked to GalNAc. |
| TextSentencer_T9 |
1155-1242 |
Sentence |
denotes |
WbdN contains a conserved DxD motif and requires divalent metal ions for full activity. |
| T8 |
1155-1242 |
Sentence |
denotes |
WbdN contains a conserved DxD motif and requires divalent metal ions for full activity. |
| T9 |
1155-1242 |
Sentence |
denotes |
WbdN contains a conserved DxD motif and requires divalent metal ions for full activity. |
| TextSentencer_T10 |
1243-1349 |
Sentence |
denotes |
WbdN activity has an optimal pH between 7 and 8 and is highly specific for UDP-Glc as the donor substrate. |
| T9 |
1243-1349 |
Sentence |
denotes |
WbdN activity has an optimal pH between 7 and 8 and is highly specific for UDP-Glc as the donor substrate. |
| T10 |
1243-1349 |
Sentence |
denotes |
WbdN activity has an optimal pH between 7 and 8 and is highly specific for UDP-Glc as the donor substrate. |
| TextSentencer_T11 |
1350-1507 |
Sentence |
denotes |
GalNAcα derivatives lacking the diphosphate group were inactive as substrates, and the enzyme did not transfer Glc to GlcNAcα-O-PO(3)-PO(3)-(CH(2))(11)-O-Ph. |
| T11 |
1350-1507 |
Sentence |
denotes |
GalNAcα derivatives lacking the diphosphate group were inactive as substrates, and the enzyme did not transfer Glc to GlcNAcα-O-PO(3)-PO(3)-(CH(2))(11)-O-Ph. |
| T10 |
1350-1610 |
Sentence |
denotes |
GalNAcα derivatives lacking the diphosphate group were inactive as substrates, and the enzyme did not transfer Glc to GlcNAcα-O-PO(3)-PO(3)-(CH(2))(11)-O-Ph. Our results illustrate that WbdN is a specific UDP-Glc:GalNAcα-diphosphate-lipid β1,3-Glc-transferase. |
| TextSentencer_T12 |
1508-1610 |
Sentence |
denotes |
Our results illustrate that WbdN is a specific UDP-Glc:GalNAcα-diphosphate-lipid β1,3-Glc-transferase. |
| T12 |
1508-1610 |
Sentence |
denotes |
Our results illustrate that WbdN is a specific UDP-Glc:GalNAcα-diphosphate-lipid β1,3-Glc-transferase. |
| TextSentencer_T13 |
1611-1700 |
Sentence |
denotes |
The enzyme is a target for the development of inhibitors to block O157-antigen synthesis. |
| T11 |
1611-1700 |
Sentence |
denotes |
The enzyme is a target for the development of inhibitors to block O157-antigen synthesis. |
| T13 |
1611-1700 |
Sentence |
denotes |
The enzyme is a target for the development of inhibitors to block O157-antigen synthesis. |