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Literature summary for 3.5.3.11 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.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
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
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

Inhibitors Comment Organism Structure
putrescine
-
Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ activates Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-