| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-167 |
Sentence |
denotes |
Rice Endosperm Starch Phosphorylase (Pho1) Assembles with Disproportionating Enzyme (Dpe1) to Form a Protein Complex That Enhances Synthesis of Malto-oligosaccharides. |
| T2 |
168-265 |
Sentence |
denotes |
Starch synthesis in cereal grain endosperm is dependent on the concerted actions of many enzymes. |
| T3 |
266-436 |
Sentence |
denotes |
The starch plastidial phosphorylase (Pho1) plays an important role in the initiation of starch synthesis and in the maturation of starch granule in developing rice seeds. |
| T4 |
437-578 |
Sentence |
denotes |
Prior evidence has suggested that the rice enzyme, OsPho1, may have a physical/functional interaction with other starch biosynthetic enzymes. |
| T5 |
579-756 |
Sentence |
denotes |
Pulldown experiments showed that OsPho1 as well as OsPho1 devoid of its L80 region, a peptide unique to higher plant phosphorylases, captures disproportionating enzyme (OsDpe1). |
| T6 |
757-894 |
Sentence |
denotes |
Interaction of the latter enzyme form with OsDpe1 indicates that the putative regulatory L80 is not responsible for multienzyme assembly. |
| T7 |
895-1162 |
Sentence |
denotes |
This heterotypic enzyme complex, determined at a molar ratio of 1:1, was validated by reciprocal co-immunoprecipitation studies of native seed proteins and by co-elution chromatographic and co-migration electrophoretic patterns of these enzymes in rice seed extracts. |
| T8 |
1163-1382 |
Sentence |
denotes |
The OsPho1-OsDpe1 complex utilized a broader range of substrates for enhanced synthesis of larger maltooligosaccharides than each individual enzyme and significantly elevated the substrate affinities of OsPho1 at 30 °C. |
| T9 |
1383-1546 |
Sentence |
denotes |
Moreover, the assembly with OsDpe1 enables OsPho1 to utilize products of transglycosylation reactions involving G1 and G3, sugars that it cannot catalyze directly. |
