| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-102 |
Sentence |
denotes |
A single amino acid toggles Escherichia coli polysialyltransferases between mono- and bifunctionality. |
| T1 |
0-102 |
Sentence |
denotes |
A single amino acid toggles Escherichia coli polysialyltransferases between mono- and bifunctionality. |
| T1 |
0-102 |
Sentence |
denotes |
A single amino acid toggles Escherichia coli polysialyltransferases between mono- and bifunctionality. |
| TextSentencer_T2 |
103-255 |
Sentence |
denotes |
The enteropathogenic Escherichia coli K92 synthesizes a unique capsule consisting of polysialic acid (polySia) with alternating α2,8- and α2,9-linkages. |
| T2 |
103-255 |
Sentence |
denotes |
The enteropathogenic Escherichia coli K92 synthesizes a unique capsule consisting of polysialic acid (polySia) with alternating α2,8- and α2,9-linkages. |
| T2 |
103-255 |
Sentence |
denotes |
The enteropathogenic Escherichia coli K92 synthesizes a unique capsule consisting of polysialic acid (polySia) with alternating α2,8- and α2,9-linkages. |
| TextSentencer_T3 |
256-450 |
Sentence |
denotes |
The fact that a single enzyme is responsible for the synthesis of these alternating regioisomeric linkages raises questions as to how this controlled bifunctionality is achieved mechanistically. |
| T3 |
256-450 |
Sentence |
denotes |
The fact that a single enzyme is responsible for the synthesis of these alternating regioisomeric linkages raises questions as to how this controlled bifunctionality is achieved mechanistically. |
| T3 |
256-450 |
Sentence |
denotes |
The fact that a single enzyme is responsible for the synthesis of these alternating regioisomeric linkages raises questions as to how this controlled bifunctionality is achieved mechanistically. |
| TextSentencer_T4 |
451-725 |
Sentence |
denotes |
Aiming to identify the sequence elements responsible for dual regiospecificity, we have utilized a high-throughput polysialyltransferase (polyST) activity screen to explore the relevant sequence space between this enzyme and its close monofunctional homolog from E. coli K1. |
| T4 |
451-725 |
Sentence |
denotes |
Aiming to identify the sequence elements responsible for dual regiospecificity, we have utilized a high-throughput polysialyltransferase (polyST) activity screen to explore the relevant sequence space between this enzyme and its close monofunctional homolog from E. coli K1. |
| T4 |
451-725 |
Sentence |
denotes |
Aiming to identify the sequence elements responsible for dual regiospecificity, we have utilized a high-throughput polysialyltransferase (polyST) activity screen to explore the relevant sequence space between this enzyme and its close monofunctional homolog from E. coli K1. |
| TextSentencer_T5 |
726-855 |
Sentence |
denotes |
The linkage specificity of selected mutants was subsequently confirmed using a polySia permethylation linkage analysis technique. |
| T5 |
726-855 |
Sentence |
denotes |
The linkage specificity of selected mutants was subsequently confirmed using a polySia permethylation linkage analysis technique. |
| T5 |
726-855 |
Sentence |
denotes |
The linkage specificity of selected mutants was subsequently confirmed using a polySia permethylation linkage analysis technique. |
| TextSentencer_T6 |
856-984 |
Sentence |
denotes |
We have identified a single amino acid exchange at residue 52 that toggles these enzymes between mono and dual regiospecificity. |
| T6 |
856-984 |
Sentence |
denotes |
We have identified a single amino acid exchange at residue 52 that toggles these enzymes between mono and dual regiospecificity. |
| T6 |
856-984 |
Sentence |
denotes |
We have identified a single amino acid exchange at residue 52 that toggles these enzymes between mono and dual regiospecificity. |
| TextSentencer_T7 |
985-1098 |
Sentence |
denotes |
The results have implications for the mechanism by which the E. coli K92 polyST achieves bifunctional elongation. |
| T7 |
985-1098 |
Sentence |
denotes |
The results have implications for the mechanism by which the E. coli K92 polyST achieves bifunctional elongation. |
| T7 |
985-1098 |
Sentence |
denotes |
The results have implications for the mechanism by which the E. coli K92 polyST achieves bifunctional elongation. |