| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-140 |
Sentence |
denotes |
Biochemical and Structural Characterization of a Five-domain GH115 α-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T. |
| T1 |
0-140 |
Sentence |
denotes |
Biochemical and Structural Characterization of a Five-domain GH115 α-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T. |
| TextSentencer_T2 |
141-305 |
Sentence |
denotes |
Glucuronic acid (GlcAp) and/or methylglucuronic acid (MeGlcAp) decorate the major forms of xylan in hardwood and coniferous softwoods as well as many cereal grains. |
| T2 |
141-305 |
Sentence |
denotes |
Glucuronic acid (GlcAp) and/or methylglucuronic acid (MeGlcAp) decorate the major forms of xylan in hardwood and coniferous softwoods as well as many cereal grains. |
| TextSentencer_T3 |
306-524 |
Sentence |
denotes |
Accordingly, the complete utilization of glucuronoxylans or conversion to sugar precursors requires the action of main chain xylanases as well as α-glucuronidases that release the α- (1→2)-linked (Me)GlcAp side groups. |
| T3 |
306-524 |
Sentence |
denotes |
Accordingly, the complete utilization of glucuronoxylans or conversion to sugar precursors requires the action of main chain xylanases as well as α-glucuronidases that release the α- (1→2)-linked (Me)GlcAp side groups. |
| TextSentencer_T4 |
525-765 |
Sentence |
denotes |
Herein, a family GH115 enzymefrom the marine bacterium Saccharophagus degradans 2-40(T), SdeAgu115A, demonstrated activity toward glucuronoxylan and oligomers thereof with preference toward MeGlcAp linked to internal xylopyranosyl residues. |
| T4 |
525-765 |
Sentence |
denotes |
Herein, a family GH115 enzymefrom the marine bacterium Saccharophagus degradans 2-40(T), SdeAgu115A, demonstrated activity toward glucuronoxylan and oligomers thereof with preference toward MeGlcAp linked to internal xylopyranosyl residues. |
| TextSentencer_T5 |
766-839 |
Sentence |
denotes |
Unique biochemical characteristics of NaCl activation were also observed. |
| T5 |
766-839 |
Sentence |
denotes |
Unique biochemical characteristics of NaCl activation were also observed. |
| TextSentencer_T6 |
840-1051 |
Sentence |
denotes |
The crystal structure of SdeAgu115A revealed a five-domain architecture, with an additional insertion C(+) domain that had significant impact on the domain arrangement of SdeAgu115A monomer and its dimerization. |
| T6 |
840-1051 |
Sentence |
denotes |
The crystal structure of SdeAgu115A revealed a five-domain architecture, with an additional insertion C(+) domain that had significant impact on the domain arrangement of SdeAgu115A monomer and its dimerization. |
| TextSentencer_T7 |
1052-1226 |
Sentence |
denotes |
The participation of domain C(+) in substrate binding was supported by reduced substrate inhibition upon introducing W773A, W689A, and F696A substitutions within this domain. |
| T7 |
1052-1226 |
Sentence |
denotes |
The participation of domain C(+) in substrate binding was supported by reduced substrate inhibition upon introducing W773A, W689A, and F696A substitutions within this domain. |
| TextSentencer_T8 |
1227-1331 |
Sentence |
denotes |
In addition to Asp-335, the catalytic essentiality of Glu-216 was revealed by site-specific mutagenesis. |
| T8 |
1227-1331 |
Sentence |
denotes |
In addition to Asp-335, the catalytic essentiality of Glu-216 was revealed by site-specific mutagenesis. |
| TextSentencer_T9 |
1332-1502 |
Sentence |
denotes |
A primary sequence analysis suggested that the SdeAgu115A architecture is shared by more than half of GH115 members, thus defining a distinct archetype for GH115 enzymes. |
| T9 |
1332-1502 |
Sentence |
denotes |
A primary sequence analysis suggested that the SdeAgu115A architecture is shared by more than half of GH115 members, thus defining a distinct archetype for GH115 enzymes. |