EC Number   |
Protein Variants |
Reference |
|---|
   4.1.2.52 | D42A |
inactive, the mutation leads to a concomitant loss of the metal ion |
725493 |
| 4.1.2.52 | H45A |
by site-directed mutagenesis, mutant enzyme has 24fold higher dissociation constant for Co2+ compared to the wild-type enzyme, apparent Km value for Co2+ increases by about 800fold compared to the wild-type enzyme, different kcat and km values |
722258 |
| 4.1.2.52 | H45A |
the mutation leads to a decrease in kcat of the enzyme by 78fold |
725493 |
| 4.1.2.52 | H45Q |
by site-directed mutagenesis, mutant enzyme has 69fold higher dissociation constant for Co2+ compared to the wild-type enzyme, apparent Km value for Co2+ increases by about 800fold compared to the wild-type enzyme, different kcat and km values |
722258 |
| 4.1.2.52 | H45Q |
the mutation leads to a decrease in kcat of the enzyme by 2059fold |
725493 |
| 4.1.2.52 | R70A |
almost inactive |
725493 |
| 4.1.2.52 | R70A |
replacement by site-specific mutagenesis results in an enzyme that lacks both aldolase and decarboxylase activities. The mutant enzyme is also unable to catalyze pyruvate proton exchange |
721601 |
| 4.1.2.52 | R70K |
the mutation reduces catalytic efficiency by 270fold |
725493 |
