Id |
Subject |
Object |
Predicate |
Lexical cue |
T1 |
0-101 |
Sentence |
denotes |
Enhanced CO2/O2 specificity of a site-directed mutant of ribulose-bisphosphate carboxylase/oxygenase. |
T2 |
102-253 |
Sentence |
denotes |
The CO2/O2 specificity factor of ribulose-bisphosphate carboxylase/oxygenase partially determines the efficiency of photosynthetic carbon assimilation. |
T3 |
254-359 |
Sentence |
denotes |
Heretofore, engineered alterations of the enzyme have only decreased the selectivity for CO2 utilization. |
T4 |
360-543 |
Sentence |
denotes |
We show that alanyl replacement of active-site Ser-368 of the Rhodospirillum rubrum carboxylase enhances the carboxylation selectivity approximately 1.6-fold over the wild-type level. |
T5 |
544-652 |
Sentence |
denotes |
This enhancement reflects a greater relative decline in oxygenase efficiency than in carboxylase efficiency. |
T6 |
653-863 |
Sentence |
denotes |
In contrast to wild-type enzyme, the carboxylase activity of the Ser-368 mutant protein is not perceptibly inhibited by O2, perhaps indicative of a change in rate-limiting steps in the overall reaction pathway. |
T1 |
0-101 |
Sentence |
denotes |
Enhanced CO2/O2 specificity of a site-directed mutant of ribulose-bisphosphate carboxylase/oxygenase. |
T2 |
102-253 |
Sentence |
denotes |
The CO2/O2 specificity factor of ribulose-bisphosphate carboxylase/oxygenase partially determines the efficiency of photosynthetic carbon assimilation. |
T3 |
254-359 |
Sentence |
denotes |
Heretofore, engineered alterations of the enzyme have only decreased the selectivity for CO2 utilization. |
T4 |
360-543 |
Sentence |
denotes |
We show that alanyl replacement of active-site Ser-368 of the Rhodospirillum rubrum carboxylase enhances the carboxylation selectivity approximately 1.6-fold over the wild-type level. |
T5 |
544-652 |
Sentence |
denotes |
This enhancement reflects a greater relative decline in oxygenase efficiency than in carboxylase efficiency. |
T6 |
653-863 |
Sentence |
denotes |
In contrast to wild-type enzyme, the carboxylase activity of the Ser-368 mutant protein is not perceptibly inhibited by O2, perhaps indicative of a change in rate-limiting steps in the overall reaction pathway. |