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Literature summary for 3.5.3.11 extracted from

  • Carvajal, N.; Orellana, M.S.; Salas, M.; Enriquez, P.; Alarcon, R.; Uribe, E.; Lopez, V.
    Kinetic studies and site-directed mutagenesis of Escherichia coli agmatinase. A role for Glu274 in binding and correct positioning of the substrate guanidinium group (2004), Arch. Biochem. Biophys., 430, 185-190.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
E274A 1-2% of wild type activity Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
guanidinium ion competitive Escherichia coli
putrescine competitive Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1
-
agmatine wild type Escherichia coli
6.3
-
agmatine mutant E274A Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
agmatine + H2O
-
Escherichia coli putrescine + urea
-
?

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
15
-
guanidinium ion wild type Escherichia coli
44.2
-
guanidinium ion mutant E274A Escherichia coli