| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-118 |
Sentence |
denotes |
Screening a limited structure-based library identifies UDP-GalNAc-specific mutants of alpha-1,3-galactosyltransferase. |
| T1 |
0-118 |
Sentence |
denotes |
Screening a limited structure-based library identifies UDP-GalNAc-specific mutants of alpha-1,3-galactosyltransferase. |
| T1 |
0-118 |
Sentence |
denotes |
Screening a limited structure-based library identifies UDP-GalNAc-specific mutants of alpha-1,3-galactosyltransferase. |
| TextSentencer_T2 |
119-234 |
Sentence |
denotes |
Complex glycans have important roles in biological recognition processes and considerable pharmaceutical potential. |
| T2 |
119-234 |
Sentence |
denotes |
Complex glycans have important roles in biological recognition processes and considerable pharmaceutical potential. |
| T2 |
119-234 |
Sentence |
denotes |
Complex glycans have important roles in biological recognition processes and considerable pharmaceutical potential. |
| TextSentencer_T3 |
235-361 |
Sentence |
denotes |
The synthesis of novel glycans can be facilitated by engineering glycosyltransferases to modify their substrate specificities. |
| T3 |
235-361 |
Sentence |
denotes |
The synthesis of novel glycans can be facilitated by engineering glycosyltransferases to modify their substrate specificities. |
| T3 |
235-361 |
Sentence |
denotes |
The synthesis of novel glycans can be facilitated by engineering glycosyltransferases to modify their substrate specificities. |
| TextSentencer_T4 |
362-575 |
Sentence |
denotes |
The choice of sites to modify requires the knowledge of the structures of enzyme-substrate complexes while the complexity of protein structures necessitates the exploration of a large array of multisite mutations. |
| T4 |
362-575 |
Sentence |
denotes |
The choice of sites to modify requires the knowledge of the structures of enzyme-substrate complexes while the complexity of protein structures necessitates the exploration of a large array of multisite mutations. |
| T4 |
362-575 |
Sentence |
denotes |
The choice of sites to modify requires the knowledge of the structures of enzyme-substrate complexes while the complexity of protein structures necessitates the exploration of a large array of multisite mutations. |
| TextSentencer_T5 |
576-773 |
Sentence |
denotes |
The retaining glycosyltransferase, alpha-1,3-galactosyltransferase (alpha3GT), which catalyzes the synthesis of the alpha-Gal epitope, has strict specificity for UDP-galactose as a donor substrate. |
| T5 |
576-773 |
Sentence |
denotes |
The retaining glycosyltransferase, alpha-1,3-galactosyltransferase (alpha3GT), which catalyzes the synthesis of the alpha-Gal epitope, has strict specificity for UDP-galactose as a donor substrate. |
| T5 |
576-773 |
Sentence |
denotes |
The retaining glycosyltransferase, alpha-1,3-galactosyltransferase (alpha3GT), which catalyzes the synthesis of the alpha-Gal epitope, has strict specificity for UDP-galactose as a donor substrate. |
| TextSentencer_T6 |
774-996 |
Sentence |
denotes |
Based on the structure of a complex of UDP-galactose with alpha3GT, the specificity for the galactose moiety can be partly attributed to residues that interact with the galactose 2-OH group, particularly His280 and Ala282. |
| T6 |
774-996 |
Sentence |
denotes |
Based on the structure of a complex of UDP-galactose with alpha3GT, the specificity for the galactose moiety can be partly attributed to residues that interact with the galactose 2-OH group, particularly His280 and Ala282. |
| T6 |
774-996 |
Sentence |
denotes |
Based on the structure of a complex of UDP-galactose with alpha3GT, the specificity for the galactose moiety can be partly attributed to residues that interact with the galactose 2-OH group, particularly His280 and Ala282. |
| TextSentencer_T7 |
997-1249 |
Sentence |
denotes |
With the goal of engineering a variant of bovine alpha3GT with GalNAc transferase activity, we constructed a limited library of 456 alpha3GT mutants containing 19 alternative amino acids at position 280, two each at 281 and 282 and six at position 283. |
| T7 |
997-1249 |
Sentence |
denotes |
With the goal of engineering a variant of bovine alpha3GT with GalNAc transferase activity, we constructed a limited library of 456 alpha3GT mutants containing 19 alternative amino acids at position 280, two each at 281 and 282 and six at position 283. |
| T7 |
997-1249 |
Sentence |
denotes |
With the goal of engineering a variant of bovine alpha3GT with GalNAc transferase activity, we constructed a limited library of 456 alpha3GT mutants containing 19 alternative amino acids at position 280, two each at 281 and 282 and six at position 283. |
| TextSentencer_T8 |
1250-1372 |
Sentence |
denotes |
Clones (1500) were screened by assaying partially purified bacterially expressed variants for GalNAc transferase activity. |
| T8 |
1250-1372 |
Sentence |
denotes |
Clones (1500) were screened by assaying partially purified bacterially expressed variants for GalNAc transferase activity. |
| T8 |
1250-1372 |
Sentence |
denotes |
Clones (1500) were screened by assaying partially purified bacterially expressed variants for GalNAc transferase activity. |
| TextSentencer_T9 |
1373-1487 |
Sentence |
denotes |
Mutants with the highest levels of GalNAc transferase activity, AGGL or GGGL, had substitutions at all four sites. |
| T9 |
1373-1487 |
Sentence |
denotes |
Mutants with the highest levels of GalNAc transferase activity, AGGL or GGGL, had substitutions at all four sites. |
| T9 |
1373-1487 |
Sentence |
denotes |
Mutants with the highest levels of GalNAc transferase activity, AGGL or GGGL, had substitutions at all four sites. |
| TextSentencer_T10 |
1488-1629 |
Sentence |
denotes |
The AGGL mutant had slightly superior GalNAc transferase activity amounting to about 3% of the activity of the wild-type enzyme with UDP-Gal. |
| T10 |
1488-1629 |
Sentence |
denotes |
The AGGL mutant had slightly superior GalNAc transferase activity amounting to about 3% of the activity of the wild-type enzyme with UDP-Gal. |
| T10 |
1488-1830 |
Sentence |
denotes |
The AGGL mutant had slightly superior GalNAc transferase activity amounting to about 3% of the activity of the wild-type enzyme with UDP-Gal. This mutant had a low activity with UDP-Gal; its crystallographic structure suggests that the smaller side chains at residues 280-282 form a pocket to accommodate the larger acetamido group of GalNAc. |
| TextSentencer_T11 |
1630-1830 |
Sentence |
denotes |
This mutant had a low activity with UDP-Gal; its crystallographic structure suggests that the smaller side chains at residues 280-282 form a pocket to accommodate the larger acetamido group of GalNAc. |
| T11 |
1630-1830 |
Sentence |
denotes |
This mutant had a low activity with UDP-Gal; its crystallographic structure suggests that the smaller side chains at residues 280-282 form a pocket to accommodate the larger acetamido group of GalNAc. |
| TextSentencer_T12 |
1831-1913 |
Sentence |
denotes |
Mutational studies indicate that Leu283 is important for stability in this mutant. |
| T11 |
1831-1913 |
Sentence |
denotes |
Mutational studies indicate that Leu283 is important for stability in this mutant. |
| T12 |
1831-1913 |
Sentence |
denotes |
Mutational studies indicate that Leu283 is important for stability in this mutant. |