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	
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	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	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