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