| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-80 |
Sentence |
denotes |
Investigation of the substrate specificity of K5 lyase A from K5A bacteriophage. |
| T1 |
0-80 |
Sentence |
denotes |
Investigation of the substrate specificity of K5 lyase A from K5A bacteriophage. |
| T1 |
0-80 |
Sentence |
denotes |
Investigation of the substrate specificity of K5 lyase A from K5A bacteriophage. |
| TextSentencer_T2 |
81-236 |
Sentence |
denotes |
K5 lyase A (KflA) is a tailspike protein from the K5A phage that catalyzes the degradation of the capsule polysaccharide of K5 strains of Escherichia coli. |
| T2 |
81-236 |
Sentence |
denotes |
K5 lyase A (KflA) is a tailspike protein from the K5A phage that catalyzes the degradation of the capsule polysaccharide of K5 strains of Escherichia coli. |
| T2 |
81-236 |
Sentence |
denotes |
K5 lyase A (KflA) is a tailspike protein from the K5A phage that catalyzes the degradation of the capsule polysaccharide of K5 strains of Escherichia coli. |
| TextSentencer_T3 |
237-469 |
Sentence |
denotes |
The K5 E. coli capsule polysaccharide, also known as heparosan, is composed of the disaccharide repeating unit of [-4)-GlcA-β(1,4)-GlcNAc-α(1-] and therefore identical to the biological precursor of heparin and heparan sulfate (HS). |
| T3 |
237-469 |
Sentence |
denotes |
The K5 E. coli capsule polysaccharide, also known as heparosan, is composed of the disaccharide repeating unit of [-4)-GlcA-β(1,4)-GlcNAc-α(1-] and therefore identical to the biological precursor of heparin and heparan sulfate (HS). |
| T3 |
237-469 |
Sentence |
denotes |
The K5 E. coli capsule polysaccharide, also known as heparosan, is composed of the disaccharide repeating unit of [-4)-GlcA-β(1,4)-GlcNAc-α(1-] and therefore identical to the biological precursor of heparin and heparan sulfate (HS). |
| TextSentencer_T4 |
470-539 |
Sentence |
denotes |
KflA could supplement the heparin lyases for heparin and HS analysis. |
| T4 |
470-539 |
Sentence |
denotes |
KflA could supplement the heparin lyases for heparin and HS analysis. |
| T4 |
470-539 |
Sentence |
denotes |
KflA could supplement the heparin lyases for heparin and HS analysis. |
| TextSentencer_T5 |
540-692 |
Sentence |
denotes |
The first part of this study aimed to clarify ambiguity resulting from the revision of the KflA amino acid sequence in 2010 from that published in 2000. |
| T5 |
540-692 |
Sentence |
denotes |
The first part of this study aimed to clarify ambiguity resulting from the revision of the KflA amino acid sequence in 2010 from that published in 2000. |
| T5 |
540-692 |
Sentence |
denotes |
The first part of this study aimed to clarify ambiguity resulting from the revision of the KflA amino acid sequence in 2010 from that published in 2000. |
| TextSentencer_T6 |
693-864 |
Sentence |
denotes |
We found that only the expression of the updated sequence gave a soluble active enzyme, which produced heparosan degradation products similar to those of previous studies. |
| T6 |
693-864 |
Sentence |
denotes |
We found that only the expression of the updated sequence gave a soluble active enzyme, which produced heparosan degradation products similar to those of previous studies. |
| T6 |
693-864 |
Sentence |
denotes |
We found that only the expression of the updated sequence gave a soluble active enzyme, which produced heparosan degradation products similar to those of previous studies. |
| TextSentencer_T7 |
865-1022 |
Sentence |
denotes |
Next, we examined the specificity of KflA toward heparosan oligosaccharides of varying sizes, all containing a single N-sulfated glucosamine (GlcNS) residue. |
| T7 |
865-1022 |
Sentence |
denotes |
Next, we examined the specificity of KflA toward heparosan oligosaccharides of varying sizes, all containing a single N-sulfated glucosamine (GlcNS) residue. |
| T7 |
865-1022 |
Sentence |
denotes |
Next, we examined the specificity of KflA toward heparosan oligosaccharides of varying sizes, all containing a single N-sulfated glucosamine (GlcNS) residue. |
| TextSentencer_T8 |
1023-1177 |
Sentence |
denotes |
The presence of GlcNS in an octasaccharide and a nonasaccharide chain directed cleavage by KflA to a single position at the reducing end of the substrate. |
| T8 |
1023-1177 |
Sentence |
denotes |
The presence of GlcNS in an octasaccharide and a nonasaccharide chain directed cleavage by KflA to a single position at the reducing end of the substrate. |
| T8 |
1023-1177 |
Sentence |
denotes |
The presence of GlcNS in an octasaccharide and a nonasaccharide chain directed cleavage by KflA to a single position at the reducing end of the substrate. |
| TextSentencer_T9 |
1178-1382 |
Sentence |
denotes |
However, an N-sulfated decasaccharide exhibited extensive cleavage at the nonreducing end of the chain, illustrating a distinct change in the cleavage pattern of KflA toward substrates of differing sizes. |
| T9 |
1178-1382 |
Sentence |
denotes |
However, an N-sulfated decasaccharide exhibited extensive cleavage at the nonreducing end of the chain, illustrating a distinct change in the cleavage pattern of KflA toward substrates of differing sizes. |
| T9 |
1178-1382 |
Sentence |
denotes |
However, an N-sulfated decasaccharide exhibited extensive cleavage at the nonreducing end of the chain, illustrating a distinct change in the cleavage pattern of KflA toward substrates of differing sizes. |
| TextSentencer_T10 |
1383-1539 |
Sentence |
denotes |
Because KflA is able to cleave a substrate containing isolated GlcNS residues, this enzyme could be used for the analysis of low-sulfate content HS domains. |
| T10 |
1383-1539 |
Sentence |
denotes |
Because KflA is able to cleave a substrate containing isolated GlcNS residues, this enzyme could be used for the analysis of low-sulfate content HS domains. |
| T10 |
1383-1539 |
Sentence |
denotes |
Because KflA is able to cleave a substrate containing isolated GlcNS residues, this enzyme could be used for the analysis of low-sulfate content HS domains. |