EC Number   |
Protein Variants |
Reference |
|---|
    2.5.1.6 | A55D |
the mutation reduces the enzyme activity by more than 50% |
737636 |
| 2.5.1.6 | C113S |
compared with the wild type enzyme the mutant enzyme is only weakly activated by PfTrx1. The mutation significantly decreases the affinity to the substrate L-methionine. The mutant enzyme shows higher affinity towards ATP when compared with the wild type |
759436 |
| 2.5.1.6 | C187S |
with regard to specific activity the mutant enzyme does not show major differences compared with the wild type enzyme. The mutant enzyme shows higher affinity towards ATP when compared with the wild type |
759436 |
| 2.5.1.6 | C35S |
reduction in Vmax value |
659298 |
| 2.5.1.6 | C52S |
compared with the wild type enzyme the mutant enzyme is only weakly activated by PfTrx1. With regard to specific activity the mutant enzyme does not show major differences compared with the wild type enzyme. The mutation significantly decreases the affinity to the substrate L-methionine and ATP |
759436 |
| 2.5.1.6 | C61S |
reduction in Vmax value |
659298 |
| 2.5.1.6 | D107C |
enzyme activity similar to wild-type, attachment of methanethiosulfonate spin label to form D107R1, increase in Km-value, decrease in kcat value |
657653 |
| 2.5.1.6 | D121N |
no basal enzymic activity, little activity in presence of S-adenosyl methionine |
658640 |
| 2.5.1.6 | D166N |
reduced enzymic activity, little activation by S-adenosyl methionine |
658640 |
| 2.5.1.6 | D19N |
no basal enzymic activity, little activity in presence of S-adenosyl methionine |
658640 |
