| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-137 |
Sentence |
denotes |
Dissection of the two transferase activities of the Pasteurella multocida hyaluronan synthase: two active sites exist in one polypeptide. |
| T1 |
0-137 |
Sentence |
denotes |
Dissection of the two transferase activities of the Pasteurella multocida hyaluronan synthase: two active sites exist in one polypeptide. |
| T1 |
0-137 |
Sentence |
denotes |
Dissection of the two transferase activities of the Pasteurella multocida hyaluronan synthase: two active sites exist in one polypeptide. |
| TextSentencer_T2 |
138-245 |
Sentence |
denotes |
Type A Pasteurella multocida, an animal pathogen, employs a hyaluronan [HA] capsule to avoid host defenses. |
| T2 |
138-245 |
Sentence |
denotes |
Type A Pasteurella multocida, an animal pathogen, employs a hyaluronan [HA] capsule to avoid host defenses. |
| T2 |
138-245 |
Sentence |
denotes |
Type A Pasteurella multocida, an animal pathogen, employs a hyaluronan [HA] capsule to avoid host defenses. |
| TextSentencer_T3 |
246-381 |
Sentence |
denotes |
PmHAS, the 972-residue membrane-associated hyaluronan synthase, catalyzes the transfer of both GlcNAc and GlcUA to form the HA polymer. |
| T3 |
246-381 |
Sentence |
denotes |
PmHAS, the 972-residue membrane-associated hyaluronan synthase, catalyzes the transfer of both GlcNAc and GlcUA to form the HA polymer. |
| T3 |
246-381 |
Sentence |
denotes |
PmHAS, the 972-residue membrane-associated hyaluronan synthase, catalyzes the transfer of both GlcNAc and GlcUA to form the HA polymer. |
| TextSentencer_T4 |
382-467 |
Sentence |
denotes |
To define the catalytic and membrane-associated domains, pmHAS mutants were analyzed. |
| T4 |
382-467 |
Sentence |
denotes |
To define the catalytic and membrane-associated domains, pmHAS mutants were analyzed. |
| T4 |
382-467 |
Sentence |
denotes |
To define the catalytic and membrane-associated domains, pmHAS mutants were analyzed. |
| TextSentencer_T5 |
468-607 |
Sentence |
denotes |
PmHAS1-703 is a soluble, active HA synthase suggesting that the carboxyl-terminus is involved in membrane association of the native enzyme. |
| T5 |
468-607 |
Sentence |
denotes |
PmHAS1-703 is a soluble, active HA synthase suggesting that the carboxyl-terminus is involved in membrane association of the native enzyme. |
| T5 |
468-607 |
Sentence |
denotes |
PmHAS1-703 is a soluble, active HA synthase suggesting that the carboxyl-terminus is involved in membrane association of the native enzyme. |
| TextSentencer_T6 |
608-689 |
Sentence |
denotes |
PmHAS1-650 is inactive as a HA synthase, but retains GlcNAc-transferase activity. |
| T6 |
608-689 |
Sentence |
denotes |
PmHAS1-650 is inactive as a HA synthase, but retains GlcNAc-transferase activity. |
| T6 |
608-689 |
Sentence |
denotes |
PmHAS1-650 is inactive as a HA synthase, but retains GlcNAc-transferase activity. |
| TextSentencer_T7 |
690-840 |
Sentence |
denotes |
Within the pmHAS sequence, there is a duplicated domain containing a short motif, Asp-Gly-Ser, that is conserved among many beta-glycosyltransferases. |
| T7 |
690-840 |
Sentence |
denotes |
Within the pmHAS sequence, there is a duplicated domain containing a short motif, Asp-Gly-Ser, that is conserved among many beta-glycosyltransferases. |
| T7 |
690-840 |
Sentence |
denotes |
Within the pmHAS sequence, there is a duplicated domain containing a short motif, Asp-Gly-Ser, that is conserved among many beta-glycosyltransferases. |
| TextSentencer_T8 |
841-965 |
Sentence |
denotes |
Changing this aspartate in either domain to asparagine, glutamate, or lysine reduced the HA synthase activity to low levels. |
| T8 |
841-965 |
Sentence |
denotes |
Changing this aspartate in either domain to asparagine, glutamate, or lysine reduced the HA synthase activity to low levels. |
| T8 |
841-965 |
Sentence |
denotes |
Changing this aspartate in either domain to asparagine, glutamate, or lysine reduced the HA synthase activity to low levels. |
| TextSentencer_T9 |
966-1119 |
Sentence |
denotes |
The mutants substituted at residue 196 possessed GlcUA-transferase activity while those substituted at residue 477 possessed GlcNAc-transferase activity. |
| T9 |
966-1119 |
Sentence |
denotes |
The mutants substituted at residue 196 possessed GlcUA-transferase activity while those substituted at residue 477 possessed GlcNAc-transferase activity. |
| T9 |
966-1119 |
Sentence |
denotes |
The mutants substituted at residue 196 possessed GlcUA-transferase activity while those substituted at residue 477 possessed GlcNAc-transferase activity. |
| TextSentencer_T10 |
1120-1310 |
Sentence |
denotes |
The Michaelis constants of the functional transferase activity of the various mutants, a measure of the apparent affinity of the enzymes for the precursors, were similar to wild-type values. |
| T10 |
1120-1310 |
Sentence |
denotes |
The Michaelis constants of the functional transferase activity of the various mutants, a measure of the apparent affinity of the enzymes for the precursors, were similar to wild-type values. |
| T10 |
1120-1310 |
Sentence |
denotes |
The Michaelis constants of the functional transferase activity of the various mutants, a measure of the apparent affinity of the enzymes for the precursors, were similar to wild-type values. |
| TextSentencer_T11 |
1311-1452 |
Sentence |
denotes |
Furthermore, mixing D196N and D477K mutant proteins in the same reaction allowed HA polymerization at levels similar to the wild-type enzyme. |
| T11 |
1311-1452 |
Sentence |
denotes |
Furthermore, mixing D196N and D477K mutant proteins in the same reaction allowed HA polymerization at levels similar to the wild-type enzyme. |
| T11 |
1311-1452 |
Sentence |
denotes |
Furthermore, mixing D196N and D477K mutant proteins in the same reaction allowed HA polymerization at levels similar to the wild-type enzyme. |
| TextSentencer_T12 |
1453-1579 |
Sentence |
denotes |
These results provide the first direct evidence that the synthase polypeptide utilizes two separate glycosyltransferase sites. |
| T12 |
1453-1579 |
Sentence |
denotes |
These results provide the first direct evidence that the synthase polypeptide utilizes two separate glycosyltransferase sites. |
| T12 |
1453-1579 |
Sentence |
denotes |
These results provide the first direct evidence that the synthase polypeptide utilizes two separate glycosyltransferase sites. |