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Literature summary for 3.5.3.11 extracted from

  • Satishchandran, C.; Boyle S.M.
    Purification and properties of agmatine ureohydrolase, a putrescine biosynthetic enzyme in Escherichia coli (1986), J. Bacteriol., 165, 843-848.
    View publication on PubMedView publication on EuropePMC
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Inhibitors

Inhibitors Comment Organism Structure
arginine competitive inhibitor Escherichia coli
EDTA 1 mM causes 53% inhibition Escherichia coli
EGTA 1 mM causes 74% inhibition Escherichia coli
ornithine noncompetitive inhibitor Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2
-
 agmatine
-
 Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
33409
-
 2 * 38000, SDS-PAGE, 2 * 33409, deduced from sequence Escherichia coli
38000
-
 2 * 38000, SDS-PAGE, 2 * 33409, deduced from sequence Escherichia coli
80000
-
 gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Storage Stability

Storage Stability Organism
-80°C, at least three months Escherichia coli

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
dimer 2 * 38000, SDS-PAGE, 2 * 33409, deduced from sequence Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
42
-
-
 Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
-
 Escherichia coli