EC Number   |
Protein Variants  |
Reference |
|---|
    3.5.3.11 | C136A |
mutant has 90% of the activity compared to wild type in the presence of Fe(II). As the wild-type enzyme the mutant enzyme requires dithiothreitol for activity |
-, 726980 |
| 3.5.3.11 | C151S |
mutant has 6% of the activity compared to wild type in the presence of Fe(II). When dithiothreitol is present in the reaction the mutant shows 24% of the wild type activity |
-, 726980 |
| 3.5.3.11 | C229A |
mutant has 92% of the activity compared to wild type in the presence of Fe(II) |
-, 726980 |
| 3.5.3.11 | C71S |
mutant has 4% of the activity compared to wild type in the presence of Fe(II). When dithiothreitol is present in the reaction the mutant shows 24% of the wild type activity |
-, 726980 |
| 3.5.3.11 | E274A |
1-2% of wild type activity |
649495 |
| 3.5.3.11 | H126N |
51% of wild type activity, significant alteration in Mn2+ binding |
651139 |
| 3.5.3.11 | H126N |
51% of wild-type activity with Mn2+-activated mutant enzyme. Interaction with the required Mn2+ is significantly altered. Mutation is not accompanied by change in Km-value, Ki-value for putrescine inhibition, molecular weight, tryptophan fluorescence properties or CD spectra of the enzyme |
665940 |
| 3.5.3.11 | H127A |
Km-value for agmatine is 2.3fold lower than the Km-value for the wild-type enzyme. kcat is 1.7fold higher as compared to the wild-type enzyme |
754341 |
| 3.5.3.11 | H151N |
30% of wild type activity, significant alteration in Mn2+ binding |
651139 |
| 3.5.3.11 | H151N |
30% of wild-type activity with Mn2+-activated mutant enzyme. Interaction with the required Mn2+ is significantly altered. Mutation is not accompanied by change in Km-value, Ki-value for putrescine inhibition, molecular weight, tryptophan fluorescence properties or CD spectra of the enzyme |
665940 |
