EC Number   |
Protein Variants |
Reference |
|---|
    2.4.2.19 | D235A |
does not affect ligand binding or catalysis, KD value for quinolinic acid is similar to wild-type, increases KD value for 5-phospho-alpha-D-ribose 1-diphosphate by 2fold |
702358 |
| 2.4.2.19 | E214A |
increases KD value for quinolinic acid by 2fold and for 5-phospho-alpha-D-ribose 1-diphosphate by 15fold, causes at least a 4000fold reduction in kcat. Presence of benzene-1,2-dicarboxylic acid results in 3.4fold tightening of 5-phospho-alpha-D-ribose 1-diphosphate binding |
702358 |
| 2.4.2.19 | E214D |
KD value for quinolinic acid is similar to wild-type, increases KD value for 5-phospho-alpha-D-ribose 1-diphosphate by 10fold. Presence of benzene-1,2-dicarboxylic acid results in 6fold tightening of 5-phospho-alpha-D-ribose 1-diphosphate binding |
702358 |
| 2.4.2.19 | E214Q |
increases KD value for quinolinic acid by 2fold and for 5-phospho-alpha-D-ribose 1-diphosphate by 2fold, has only modest effects on ligand binding and catalysis, wild-type-like pH profile. Presence of benzene-1,2-dicarboxylic acid results in 2fold tightening of 5-phospho-alpha-D-ribose 1-diphosphate binding |
702358 |
| 2.4.2.19 | H175A |
inactive |
-, 737126 |
| 2.4.2.19 | K139A |
inactive, K139 is part of quinolinic acid binding site |
693620 |
| 2.4.2.19 | K139S |
inactive, K139 is part of quinolinic acid binding site |
693620 |
| 2.4.2.19 | K153A |
inactive enzyme, kcat value decreases by more than 4000fold, is able to bind quinolinic acid with a KD value 2fold higher than that of wild-type |
702358 |
| 2.4.2.19 | K171A |
inactive, K171 is part of quinolinic acid binding site |
693620 |
| 2.4.2.19 | K171S |
inactive, K171 is part of quinolinic acid binding site |
693620 |
