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Literature summary for 1.4.3.10 extracted from

  • Desa, R.J.
    Putrescine oxidase from Micrococcus rubens. Purification and properties of the enzyme (1972), J. Biol. Chem., 247, 5527-5534.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
cadaverine noncompetitive against putrescine Kocuria rosea

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.038
-
putrescine
-
Kocuria rosea
0.124
-
O2
-
Kocuria rosea

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
46000
-
2 * 46000, SDS-PAGE Kocuria rosea
83400 87000 calculation from sedimentation data Kocuria rosea
90000
-
gel filtration Kocuria rosea

Organism

Organism UniProt Comment Textmining
Kocuria rosea
-
-
-

Oxidation Stability

Oxidation Stability Organism
photoreduction of the enzyme in presence of EDTA Kocuria rosea

Purification (Commentary)

Purification (Comment) Organism
-
Kocuria rosea

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
59.16
-
-
Kocuria rosea

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme is a weak 2-mercaptoethanol oxidase Kocuria rosea ?
-
?
putrescine + O2 + H2O
-
Kocuria rosea 4-aminobutanal + NH3 + H2O2
-
?

Subunits

Subunits Comment Organism
dimer 2 * 46000, SDS-PAGE Kocuria rosea

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
the enzyme is resistant to heat denaturation as long as it is maintained in a fully reduced state Kocuria rosea

Cofactor

Cofactor Comment Organism Structure
FAD contains 1 FAD per 82000 Da Kocuria rosea

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.28
-
cadaverine
-
Kocuria rosea