EC Number   |
Protein Variants |
Reference |
|---|
   4.2.1.28 | D335A |
computational mutation study. The OH group migration is accelerated in the Asp335Ala mutant, due to the absence of the electric repulsion between Asp335 and the migrating OH group |
747443 |
| 4.2.1.28 | D335A |
does not form (alpha-beta-gamma)complex |
675716 |
| 4.2.1.28 | D335A |
inactive mutant |
675716 |
| 4.2.1.28 | D335N |
inactive mutant |
675716 |
| 4.2.1.28 | E170A |
inactive mutant |
675716 |
| 4.2.1.28 | E170A E170Q |
computational mutation study. The spectator OH group is not fully activated in the Glu170Gln and Glu170Ala mutants during the OH group migration, and thus the activation energies in the Glu170Gln and Glu170Ala mutants are higher than that in the wild-type enzyme |
747443 |
| 4.2.1.28 | E170H |
does not form (alpha-beta-gamma)complex |
675716 |
| 4.2.1.28 | E170Q |
computational mutation study. The spectator OH group is not fully activated in the Glu170Gln and Glu170Ala mutants during the OH group migration, and thus the activation energies in the Glu170Gln and Glu170Ala mutants are higher than that in the wild-type enzyme |
747443 |
| 4.2.1.28 | E221A |
does not form (alpha-beta-gamma)complex |
675716 |
| 4.2.1.28 | H143A |
computational mutation study. The resonance stabilization of the transition state in the OH group migration is observed in the wild-type enzyme while not in the His143Ala mutant. Since the cleavage of the C2-oxygen bond of 1,2-diol radical proceeds in a more homolytic manner in the His143Ala mutant, Glu170 cannot effectively deprotonate the spectator OH group in the transition state, leading to increased activation energy of the OH group migration in the His143Ala mutant |
747443 |
