| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-99 |
Sentence |
denotes |
Inhibition of Escherichia coli glucosamine-6-phosphate synthase by reactive intermediate analogues. |
| T2 |
100-146 |
Sentence |
denotes |
The role of the 2-amino function in catalysis. |
| T3 |
147-308 |
Sentence |
denotes |
Glucosamine-6-phosphate synthase (GlmS) catalyzes the formation of D-glucosamine 6-phosphate from D-fructose 6-phosphate using L-glutamine as the ammonia source. |
| T4 |
309-499 |
Sentence |
denotes |
Because N-acetylglucosamine is an essential building block of both bacterial cell walls and fungal cell wall chitin, the enzyme is a potential target for antibacterial and antifungal agents. |
| T5 |
500-692 |
Sentence |
denotes |
The most potent carbohydrate-based inhibitor of GlmS reported to date is 2-amino-2-deoxy-D-glucitol 6-phosphate, an analogue of the putative cis-enolamine intermediate formed during catalysis. |
| T6 |
693-805 |
Sentence |
denotes |
The interaction of a series of structurally related cis-enolamine intermediate analogues with GlmS is described. |
| T7 |
806-936 |
Sentence |
denotes |
Although arabinose oxime 5-phosphate is identified as a good competitive inhibitor of GlmS with an inhibition constant equal to 1. |
| T8 |
937-1052 |
Sentence |
denotes |
2 (+/-0.3) mM, the presence of the amino function at the 2-position is shown to be important for potent inhibition. |
| T9 |
1053-1276 |
Sentence |
denotes |
Comparison of the binding affinities of 2-deoxy-D-glucitol 6-phosphate and 2-amino-2-deoxy-D-glucitol 6-phosphate indicates that the amino function contributes -4.1 (+/-0.1) kcal/mol to the free energy of inhibitor binding. |
| T10 |
1277-1495 |
Sentence |
denotes |
Similarly, comparison of the binding affinities of 2-deoxy-D-glucose 6-phosphate and D-glucosamine 6-phosphate indicates that the amino function contributes -3.0 (+/-0.1) kcal/mol to the free energy of product binding. |
| T11 |
1496-1822 |
Sentence |
denotes |
Interactions between GlmS and the 2-amino function of its ligands contribute to the uniform binding of the product and the cis-enolamine intermediate as evidenced by the similar contribution of the amino group to the free energy of binding of D-glucosamine 6-phosphate and 2-amino-2-deoxy-D-glucitol 6-phosphate, respectively. |
