EC Number   |
Protein Variants |
Reference |
|---|
   4.3.2.10 | C9A |
mutant of subunit HisF. The catalytic efficiencies kcat/Km of both isolated and complexed tHisF_C9A are not significantly different from wild-type tHisF, ruling out any central catalytic role for the replaced residue |
748148 |
| 4.3.2.10 | D130N |
mutant of subunit HisF. The catalytic efficiency kcat/Km for 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide is decreased by approximately 5 orders of magnitude |
-, 748148 |
| 4.3.2.10 | D176N |
mutant of subunit HisF. Variant tHisF_D176N shows a 40-50 fold decrease in kcat, both in isolated form and in complex with tHisH |
-, 748148 |
| 4.3.2.10 | D183N |
mutant of subunit HisF. The catalytic efficiencies kcat/Km of both isolated and complexed tHisF_D183N are not significantly different from wild-type tHisF, ruling out any central catalytic role for the replaced residue. Both kcat and Km are drastically impaired in the mutant enzyme |
-, 748148 |
| 4.3.2.10 | D51N |
mutant of subunit HisF. The catalytic efficiencies kcat/Km of both isolated and complexed tHisF_D51N are not significantly different from wild-type tHisF, ruling out any central catalytic role for the replaced residue |
-, 748148 |
| 4.3.2.10 | D98A |
HisF subunit mutant, mutation reduces glutaminase activity to 3% compared to activity of wild-type enzyme |
749186 |
| 4.3.2.10 | K19A |
HisF subunit mutant, mutation reduces glutaminase activity to 3% compared to activity of wild-type enzyme |
749186 |
| 4.3.2.10 | K19S |
mutant of subunit HisF. The ammonia-dependent reactions of isolated tHisF_K19S are similarly efficient as those of wild-type tHisF. In contrast, the efficiencies of the glutamine-dependent reactions of the tHisHtHisF_K19S complex are significantly impaired |
748148 |
| 4.3.2.10 | K258A |
about 2600fold decrease in kcat/Km for glutamine dependent cyclase reaction, basal and stimulated glutaminase functions are not altered. The stoichiometry of reaction glutamine: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide turnover is 43:1 compared to wild-type value 1:1 |
-, 747058 |
| 4.3.2.10 | K258R |
about 20fold decrease in kcat/Km for glutamine dependent cyclase reaction,basal and stimulated glutaminase functions are not altered. The stoichiometry of reaction glutamine: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide turnover is 43:1 compared to wild-type value 3:1 |
-, 747058 |
