Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.3.11 guanidinium ion competitive Escherichia coli
3.5.3.11 putrescine competitive Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.3.11 1.1
-
agmatine wild type Escherichia coli
3.5.3.11 6.3
-
agmatine mutant E274A Escherichia coli

Organism

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

Substrates and Products (Substrate)

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

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.5.3.11 15
-
guanidinium ion wild type Escherichia coli
3.5.3.11 44.2
-
guanidinium ion mutant E274A Escherichia coli