Table 1.
Calculated pKa values of the TIM catalytic Glu residue
| Structure | Organism | pKa (apo)a | pKa (w/substrate)b |
| Subfamily #1 | |||
| 1hg3 | P. woesei | 2.37 | 9.07 |
| Subfamily #2 | |||
| 1b9b | T. maritima | −0.32 | n/a |
| 1btm | B. stearothermophilus | 0.51 | 7.12 |
| Subfamily #3 | |||
| 1lyx | P. falciparum | −0.94 | 7.23 |
| 1mo0 | C. elegans | −0.04 | n/a |
| 2ypi | S. cerevisiae | 0.77 | 8.00 |
| 1m6j | E. histolytica | 0.47 | n/a |
| 1n55 | L. mexicana | 0.09 | 8.05 |
| 1tcd | T. cruzi | 0.55 | n/a |
| 1kv5 | T. brucei | 0.38 | 7.45 |
| 1tre | E. coli | 0.72 | n/a |
| 1aw1 | V. marinus | 0.97 | 7.75 |
The model (aqueous) pKa value of Glu is 4.40.
a The homogeneity of pKa values from the true and computationally plucked apostructures leads us to conclude that significant induced fit conformational changes do not occur.
b All substrates are 2-phosphoacetic acid.