EC Number   |
Protein Variants |
Reference |
|---|
    3.5.3.11 | E274A |
1-2% of wild type activity |
649495 |
| 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 |
| 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 | H65A |
incubation of the mutant with 50 mM EDTA (pH 7.5) and subsequent dialysis to remove the chelating agent results in the loss of agmatinase activity. Even in the presence of Mn2+ only about 20% of the activity of the mutant enzyme is recovered. Km-value for agmatine is 1.44fold higher than the Km-value for the wild-type enzyme. kcat is 1.1fold higher as compared to the wild-type enzyme |
754341 |
| 3.5.3.11 | H435A |
Km-value for agmatine is 1.5fold higher than the Km-value for the wild-type enzyme. kcat ist 70% compared to the wild-type value |
754341 |
| 3.5.3.11 | H206A |
Km-value for agmatine is 2.1fold lower than the Km-value for the wild-type enzyme. kcat is 90% compared to the wild-type value |
754341 |
| 3.5.3.11 | H394A |
Km-value for agmatine is 2.3fold higher than the Km-value for the wild-type enzyme. kcat ist identical to wild-type enzyme |
754341 |
| 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 |
