Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-90 |
Sentence |
denotes |
Biochemical characterization of an α1,2-colitosyltransferase from Escherichia coli O55:H7. |
T1 |
0-90 |
Sentence |
denotes |
Biochemical characterization of an α1,2-colitosyltransferase from Escherichia coli O55:H7. |
T1 |
0-90 |
Sentence |
denotes |
Biochemical characterization of an α1,2-colitosyltransferase from Escherichia coli O55:H7. |
TextSentencer_T2 |
91-222 |
Sentence |
denotes |
Colitose, also known as 3,6-dideoxy-l-galactose or 3-deoxy-l-fucose, is one of the only five naturally occurred 3,6-dideoxyhexoses. |
T2 |
91-222 |
Sentence |
denotes |
Colitose, also known as 3,6-dideoxy-l-galactose or 3-deoxy-l-fucose, is one of the only five naturally occurred 3,6-dideoxyhexoses. |
T2 |
91-222 |
Sentence |
denotes |
Colitose, also known as 3,6-dideoxy-l-galactose or 3-deoxy-l-fucose, is one of the only five naturally occurred 3,6-dideoxyhexoses. |
TextSentencer_T3 |
223-368 |
Sentence |
denotes |
Colitose was found in lipopolysaccharide of a number of infectious bacteria, including Escherichia coli O55 & O111 and Vibrio cholera O22 & O139. |
T3 |
223-368 |
Sentence |
denotes |
Colitose was found in lipopolysaccharide of a number of infectious bacteria, including Escherichia coli O55 & O111 and Vibrio cholera O22 & O139. |
T3 |
223-368 |
Sentence |
denotes |
Colitose was found in lipopolysaccharide of a number of infectious bacteria, including Escherichia coli O55 & O111 and Vibrio cholera O22 & O139. |
TextSentencer_T4 |
369-502 |
Sentence |
denotes |
To date, no colitosyltransferase (ColT) has been characterized, probably due to the inaccessibility of the sugar donor, GDP-colitose. |
T4 |
369-502 |
Sentence |
denotes |
To date, no colitosyltransferase (ColT) has been characterized, probably due to the inaccessibility of the sugar donor, GDP-colitose. |
T4 |
369-502 |
Sentence |
denotes |
To date, no colitosyltransferase (ColT) has been characterized, probably due to the inaccessibility of the sugar donor, GDP-colitose. |
TextSentencer_T5 |
503-747 |
Sentence |
denotes |
In this study, starting with chemically prepared colitose, 94.6 mg of GDP-colitose was prepared via a facile and efficient one-pot two-enzyme system involving an l-fucokinase/GDP-l-Fuc pyrophosphorylase and an inorganic pyrophosphatase (EcPpA). |
T5 |
503-747 |
Sentence |
denotes |
In this study, starting with chemically prepared colitose, 94.6 mg of GDP-colitose was prepared via a facile and efficient one-pot two-enzyme system involving an l-fucokinase/GDP-l-Fuc pyrophosphorylase and an inorganic pyrophosphatase (EcPpA). |
T5 |
503-747 |
Sentence |
denotes |
In this study, starting with chemically prepared colitose, 94.6 mg of GDP-colitose was prepared via a facile and efficient one-pot two-enzyme system involving an l-fucokinase/GDP-l-Fuc pyrophosphorylase and an inorganic pyrophosphatase (EcPpA). |
TextSentencer_T6 |
748-902 |
Sentence |
denotes |
WbgN, a putative ColT from E. coli O55:H5 was then cloned, overexpressed, purified and biochemically characterized by using GDP-colitose as a sugar donor. |
T6 |
748-902 |
Sentence |
denotes |
WbgN, a putative ColT from E. coli O55:H5 was then cloned, overexpressed, purified and biochemically characterized by using GDP-colitose as a sugar donor. |
T6 |
748-902 |
Sentence |
denotes |
WbgN, a putative ColT from E. coli O55:H5 was then cloned, overexpressed, purified and biochemically characterized by using GDP-colitose as a sugar donor. |
TextSentencer_T7 |
903-1025 |
Sentence |
denotes |
Activity assay and structural identification of the synthetic product clearly demonstrated that wbgN encodes an α1,2-ColT. |
T7 |
903-1025 |
Sentence |
denotes |
Activity assay and structural identification of the synthetic product clearly demonstrated that wbgN encodes an α1,2-ColT. |
T7 |
903-1025 |
Sentence |
denotes |
Activity assay and structural identification of the synthetic product clearly demonstrated that wbgN encodes an α1,2-ColT. |
TextSentencer_T8 |
1026-1124 |
Sentence |
denotes |
Biophysical study showed that WbgN does not require metal ion, and is highly active at pH 7.5-9.0. |
T8 |
1026-1124 |
Sentence |
denotes |
Biophysical study showed that WbgN does not require metal ion, and is highly active at pH 7.5-9.0. |
T8 |
1026-1124 |
Sentence |
denotes |
Biophysical study showed that WbgN does not require metal ion, and is highly active at pH 7.5-9.0. |
TextSentencer_T9 |
1125-1238 |
Sentence |
denotes |
In addition, acceptor specificity study indicated that WbgN exclusively recognize lacto-N-biose (Galβ1,3-GlcNAc). |
T9 |
1125-1238 |
Sentence |
denotes |
In addition, acceptor specificity study indicated that WbgN exclusively recognize lacto-N-biose (Galβ1,3-GlcNAc). |
T9 |
1125-1238 |
Sentence |
denotes |
In addition, acceptor specificity study indicated that WbgN exclusively recognize lacto-N-biose (Galβ1,3-GlcNAc). |
TextSentencer_T10 |
1239-1414 |
Sentence |
denotes |
Most interestingly, it was found that WbgN exhibits similar activity toward GDP-l-Fuc (kcat/Km = 9.2 min(-1) mM(-1)) as that toward GDP-colitose (kcat/Km = 12 min(-1) mM(-1)). |
T10 |
1239-1414 |
Sentence |
denotes |
Most interestingly, it was found that WbgN exhibits similar activity toward GDP-l-Fuc (kcat/Km = 9.2 min(-1) mM(-1)) as that toward GDP-colitose (kcat/Km = 12 min(-1) mM(-1)). |
T10 |
1239-1414 |
Sentence |
denotes |
Most interestingly, it was found that WbgN exhibits similar activity toward GDP-l-Fuc (kcat/Km = 9.2 min(-1) mM(-1)) as that toward GDP-colitose (kcat/Km = 12 min(-1) mM(-1)). |
TextSentencer_T11 |
1415-1517 |
Sentence |
denotes |
Finally, taking advantage of this, type 1 H-antigen was successfully synthesized in preparative scale. |
T11 |
1415-1517 |
Sentence |
denotes |
Finally, taking advantage of this, type 1 H-antigen was successfully synthesized in preparative scale. |
T11 |
1415-1517 |
Sentence |
denotes |
Finally, taking advantage of this, type 1 H-antigen was successfully synthesized in preparative scale. |