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 | UniProt | Comment | Textmining |
---|---|---|---|
Kocuria rosea | - |
- |
- |
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 | Comment | Organism | Structure |
---|---|---|---|
FAD | contains FAD | Kocuria rosea |