EC Number   |
Protein Variants |
Reference |
|---|
   2.7.1.105 | A44G |
the Km values for ATP and fructose-6-phosphate of the mutant enzyme are decreased by approximately 20fold compared to wilde-type values |
674911 |
| 2.7.1.105 | A44V |
the Km values for ATP and fructose-6-phosphate of the mutant enzyme are decreased by 8fold and 20fold compared to wilde-type values |
674911 |
| 2.7.1.105 | C238A |
site-directed mutagenesis, the mutation does not affect the kinetic parameters, allosteric inhibition, dimer stability, nor oligomeric structure of the enzyme |
661754 |
| 2.7.1.105 | C238F |
site-directed mutagenesis, the mutation does not affect the kinetic parameters, allosteric inhibition, dimer stability, nor oligomeric structure of the enzyme |
661754 |
| 2.7.1.105 | C295A |
site-directed mutagenesis, decreased kcat and increased Km for ATP and beta-D-fructose 6-phosphate compared to the wild-type enzyme |
661754 |
| 2.7.1.105 | C295F |
site-directed mutagenesis, decreased kcat and increased Km for ATP and beta-D-fructose 6-phosphate compared to the wild-type enzyme |
661754 |
| 2.7.1.105 | E190Q |
mutant presents a 50fold decrease in the kcat value and a 15fold increment in the apparent Km for MgATP2+. E190Q mutant presents alterations in the inhibition by MgATP2- and phosphate |
672208 |
| 2.7.1.105 | H253A |
site-directed mutagenesis, altered kinetics compared to wild-type enzyme, overview |
660814 |
| 2.7.1.105 | H253A/S460D |
site-directed mutagenesis, altered kinetics compared to wild-type enzyme, overview |
660814 |
| 2.7.1.105 | H256A |
crystal structure |
640331 |
