EC Number   |
Protein Variants |
Reference |
|---|
    4.1.2.25 | D39E |
FasA domain mutant D39E and FasB domain mutant G175A have no detectable activity of dihydroneopterin aldolase. The FasA domain mutants, G53A and Q63N and the FasB domain mutant Q185N, show approximately 11-fold, 16-fold and 24-fold decrease, respectively, in specific activity compared to wild-type FasAB-Met23. The activity of the FasB domain mutant D161E is similar to that of wild-type enzyme. The two mutant enzymes K96R and K218R have levels of activity comparable to wild-type enzyme |
5106 |
| 4.1.2.25 | E21A |
strongly reduced kcat |
678176 |
| 4.1.2.25 | E22A |
strongly reduced kcat |
678176 |
| 4.1.2.25 | E25Q |
the mutation causes a more than 25fold increase in Km value |
-, 748090 |
| 4.1.2.25 | E29A |
multistage tandem mass spectrometry (MS/MS and MS3) of gas-phase fragmentation reaction of the mutant enzyme yields identical product ion spectrum to the wild-type protein |
663629 |
| 4.1.2.25 | E73A |
strongly reduced kcat |
678176 |
| 4.1.2.25 | E74A |
mutation causes dramatic changes in the affinities of the enzyme for the substrate or product analogues or the rate constants |
678176 |
| 4.1.2.25 | E81A |
multistage tandem mass spectrometry (MS/MS and MS3) of gas-phase fragmentation reaction of the mutant enzyme yields identical product ion spectrum to the wild-type protein |
663629 |
| 4.1.2.25 | G175A |
FasA domain mutant D39E and FasB domain mutant G175A have no detectable activity of dihydroneopterin aldolase. The FasA domain mutants, G53A and Q63N and the FasB domain mutant Q185N, show approximately 11-fold, 16-fold and 24-fold decrease, respectively, in specific activity compared to wild-type FasAB-Met23. The activity of the FasB domain mutant D161E is similar to that of wild-type enzyme. The two mutant enzymes K96R and K218R have levels of activity comparable to wild-type enzyme |
5106 |
| 4.1.2.25 | H35N |
the mutant shows an about 20fold decreases in kcat value |
-, 748090 |
