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Literature summary for 1.4.3.10 extracted from

  • Okada, M.; Kawashima, S.; Imahori, K.
    Mode of inactivation of putrescine oxidase by 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide or metal ions (1980), J. Biochem., 88, 481-488.
    View publication on PubMed
Search for more literature for 1.4.3.10

Inhibitors

Inhibitors Comment Organism Structure
1-ethyl-3-(3-dimethylaminopropyl)carbodiimide the activity of the modified enzyme towards putrescine is 5.6% of that of the native enzyme. The modified enzyme shows activity towards monoamines such as n-butylamine, n-hexylamine and n-octylamine, which are not substrates of the native enzyme Kocuria rosea
Cd2+ inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme Kocuria rosea
Co2+ inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme Kocuria rosea
Cu2+ inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme Kocuria rosea
Hg2+ inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme Kocuria rosea
Ni2+ inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme Kocuria rosea
Zn2+ inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme Kocuria rosea

Organism

Organism UniProt Comment Textmining
Kocuria rosea
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme modified with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide shows activity towards monoamines such as n-butylamine, n-hexylamine and n-octylamine, which are not substrates of the native enzyme Kocuria rosea ?
-
 ?
putrescine + O2 + H2O
-
 Kocuria rosea 4-aminobutanal + NH3 + H2O2
-
 ?
spermidine + O2 + H2O
-
 Kocuria rosea 4-aminobutyraldehyde + 1,3-diaminopropane + H2O2
-
 ?

Cofactor

Cofactor Comment Organism Structure
FAD contains FAD Kocuria rosea