Literature summary extracted from

Salas, M.; Lopez, V.; Uribe, E.; Carvajal, N.
Studies on the interaction of Escherichia coli agmatinase with manganese ions: structural and kinetic studies of the H126N and H151N variants (2004), J. Inorg. Biochem., 98, 1032-1036.

Protein Variants

EC Number	Protein Variants	Comment	Organism
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	Escherichia coli
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	Escherichia coli

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
3.5.3.11	putrescine	-	Escherichia coli

Metals/Ions

EC Number	Metals/Ions	Comment	Organism	Structure
3.5.3.11	Mn2+	activates	Escherichia coli

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.5.3.11	Escherichia coli	-	-	-

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Release 2023.1 (January 2023)