1.4.3.10: putrescine oxidase
This is an abbreviated version!
For detailed information about putrescine oxidase, go to the full flat file.
Word Map on EC 1.4.3.10
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1.4.3.10
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diamine
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polyamines
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spermidine
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cadaverine
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micrococcus
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rubens
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erythropolis
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1.4.3.4
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analysis
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precisions
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electroactive
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diagnostics
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food industry
- 1.4.3.10
- diamine
- polyamines
- spermidine
- cadaverine
- micrococcus
- rubens
- erythropolis
-
1.4.3.4
- analysis
-
precisions
-
electroactive
- diagnostics
- food industry
Reaction
Synonyms
adenine dinucleotide-containing putrescine oxidase, APUO, oxidase, putrescine, PO, PuO, PUOX, PUT oxidase, PutOx, putrescine oxidase, Re-PuO
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Inhibitors
Inhibitors on EC 1.4.3.10 - putrescine oxidase
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1-ethyl-3-(3-dimethylaminopropyl)carbodiimide
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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
Cd2+
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inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
Co2+
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inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
Cu2+
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inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
Hg2+
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inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
Ni2+
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inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
Zn2+
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inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
putrescine
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inhibition potency of the enzyme in the combined cross-linked enzyme aggregate of monoamine oxidase and putrescine oxidase by the substrate is reduced by two-fold in comparison of the mixed free enzymes
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not inhibited by spermidine and cadevarine
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additional information
short diamines and monoamines strongly inhibit activity
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additional information
no substrate inhibition at concentrations as high as 100 mM/l cadaverine
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