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Information on EC 1.4.3.10 - putrescine oxidase
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1.4.3.10 putrescine oxidaseIUBMB Comments
A flavoprotein (FAD). 4-Aminobutanal condenses non-enzymically to 1-pyrroline.
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Word Map
- 1.4.3.10
- diamine
- polyamines
- spermidine
- cadaverine
- micrococcus
- rubens
- erythropolis
-
1.4.3.4
- analysis
-
precisions
-
electroactive
- diagnostics
- food industry
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
putrescine oxidase, adenine dinucleotide-containing putrescine oxidase, putox, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenine dinucleotide-containing putrescine oxidase
APUO
oxidase, putrescine
-
-
-
-
PO
-
-
-
-
PuO
PUOX
PUT oxidase
PutOx
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
putrescine + O2 + H2O = 4-aminobutanal + NH3 + H2O2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidative deamination
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-
-
-
redox reaction
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-
-
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reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
putrescine:oxygen oxidoreductase (deaminating)
A flavoprotein (FAD). 4-Aminobutanal condenses non-enzymically to 1-pyrroline.
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CAS REGISTRY NUMBER
COMMENTARY
9076-87-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,6-diaminohexane + O2 + H2O
6-aminohexanal + NH3 + H2O2
1.4% activity compared to putrescine
-
-
?
2-hydroxyputrescine + O2 + H2O
?
28% activity compared to putrescine
-
-
?
4-amino-1-butanol + O2 + H2O
4-hydroxybutanal + NH3 + H2O2
0.6% activity compared to putrescine
-
-
?
L-ornithine + O2 + H2O
?
0.08% activity compared to putrescine
-
-
?
tryptamine + O2 + H2O
1H-indol-3-yl-acetaldehyde + NH3 + H2O2
-
5.2% activity compared to putrescine
-
-
?
cadaverine + O2 + H2O
5-aminopentanal + NH3 + H2O2
-
7% of the activity with putrescine
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-
?
cadaverine + O2 + H2O
5-aminopentanal + NH3 + H2O2
-
10.7% activity compared to putrescine
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-
?
cadaverine + O2 + H2O
5-aminopentanal + NH3 + H2O2
-
10.7% activity compared to putrescine
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-
?
cadaverine + O2 + H2O
5-aminopentanal + NH3 + H2O2
-
47% of the activity with putrescine
-
-
?
cadaverine + O2 + H2O
5-aminopentanal + NH3 + H2O2
-
8.8% activity compared to putrescine
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-
?
cadaverine + O2 + H2O
5-aminopentanal + NH3 + H2O2
-
8.8% activity compared to putrescine
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-
?
cadaverine + O2 + H2O
5-aminopentanal + NH3 + H2O2
-
at 11% of the activity with putrescine
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-
?
cadaverine + O2 + H2O
5-aminopentanal + NH3 + H2O2
14% activity compared to putrescine
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-
?
cadaverine + O2 + H2O
5-aminopentanal + NH3 + H2O2
14% activity compared to putrescine
-
-
?
histamine + O2 + H2O
1H-imidazol-4-ylacetaldehyde + NH3 + H2O2
-
1.7% activity compared to putrescine
-
-
?
histamine + O2 + H2O
1H-imidazol-4-ylacetaldehyde + NH3 + H2O2
-
1.7% activity compared to putrescine
-
-
?
putrescine + O2 + H2O
4-aminobutanal + NH3 + H2O2
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-
-
-
?
putrescine + O2 + H2O
4-aminobutanal + NH3 + H2O2
-
primary electron acceptor is FAD, reversible reaction is FADH2 + O2 = FAD + H2O2
-
-
?
putrescine + O2 + H2O
4-aminobutanal + NH3 + H2O2
-
best substrate
-
-
?
putrescine + O2 + H2O
4-aminobutanal + NH3 + H2O2
-
the catalytic effciency of the combined cross-linked enzyme aggregates of monoamine oxidase and putrescine oxidase for putrescine is reduced by 41%
-
-
?
putrescine + O2 + H2O
4-aminobutanal + NH3 + H2O2
-
best substrate
-
-
?
putrescine + O2 + H2O
4-aminobutanal + NH3 + H2O2
-
-
-
?
putrescine + O2 + H2O
4-aminobutanal + NH3 + H2O2
100% activity
-
-
?
putrescine + O2 + H2O
4-aminobutanal + NH3 + H2O2
-
-
-
-
?
putrescine + O2 + H2O
4-aminobutanal + NH3 + H2O2
-
-
-
?
putrescine + O2 + H2O
4-aminobutanal + NH3 + H2O2
100% activity
-
-
?
spermidine + O2 + H2O
4-aminobutyraldehyde + 1,3-diaminopropane + H2O2
-
no activity
-
-
?
spermidine + O2 + H2O
4-aminobutyraldehyde + 1,3-diaminopropane + H2O2
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no activity at spermidine concentrations of 0.0175 mM, activity at 1 mM
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-
?
spermidine + O2 + H2O
4-aminobutyraldehyde + 1,3-diaminopropane + H2O2
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-
-
-
?
spermidine + O2 + H2O
4-aminobutyraldehyde + 1,3-diaminopropane + H2O2
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-
no liberation of ammonia
?
spermidine + O2 + H2O
4-aminobutyraldehyde + 1,3-diaminopropane + H2O2
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-
no liberation of ammonia
?
spermidine + O2 + H2O
4-aminobutyraldehyde + 1,3-diaminopropane + H2O2
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10% of the activity with putrescine
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-
?
spermidine + O2 + H2O
4-aminobutyraldehyde + 1,3-diaminopropane + H2O2
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5.0% activity compared to putrescine
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-
?
spermidine + O2 + H2O
4-aminobutyraldehyde + 1,3-diaminopropane + H2O2
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5.0% activity compared to putrescine
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-
?
spermidine + O2 + H2O
4-aminobutyraldehyde + 1,3-diaminopropane + H2O2
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51% of the activity with putrescine
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-
?
spermidine + O2 + H2O
4-aminobutyraldehyde + 1,3-diaminopropane + H2O2
-
2.5% activity compared to putrescine
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-
?
spermidine + O2 + H2O
4-aminobutyraldehyde + 1,3-diaminopropane + H2O2
-
2.5% activity compared to putrescine
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-
?
spermidine + O2 + H2O
4-aminobutyraldehyde + 1,3-diaminopropane + H2O2
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at 9% of the activity with putrescine
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-
?
spermidine + O2 + H2O
4-aminobutyraldehyde + 1,3-diaminopropane + H2O2
5.3% activity compared to putrescine
-
-
?
spermidine + O2 + H2O
4-aminobutyraldehyde + 1,3-diaminopropane + H2O2
5.3% activity compared to putrescine
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-
?
spermine + O2 + H2O
N,N'-bis(3-aminopropyl)-4-aminobutanal + NH3 + H2O2
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1.7% of the activity with putrescine
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-
?
spermine + O2 + H2O
N,N'-bis(3-aminopropyl)-4-aminobutanal + NH3 + H2O2
0.7% activity compared to putrescine
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-
?
spermine + O2 + H2O
N,N'-bis(3-aminopropyl)-4-aminobutanal + NH3 + H2O2
0.7% activity compared to putrescine
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-
?
tyramine + O2 + H2O
(4-hydroxyphenyl)acetaldehyde + NH3 + H2O2
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2.0% activity compared to putrescine
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-
?
tyramine + O2 + H2O
(4-hydroxyphenyl)acetaldehyde + NH3 + H2O2
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2.0% activity compared to putrescine
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?
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
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-
?
additional information
?
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the enzyme is a weak 2-mercaptoethanol oxidase
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?
additional information
?
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no activity with histamine, tyramine, and 2-phenylethylamine
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?
additional information
?
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no activity with histamine, tyramine, and 2-phenylethylamine
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?
additional information
?
-
no activity with aromatic amines and amino alcohols
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-
?
additional information
?
-
no activity with aromatic amines and amino alcohols
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
putrescine + O2 + H2O
4-aminobutanal + NH3 + H2O2
-
best substrate
-
-
?
putrescine + O2 + H2O
4-aminobutanal + NH3 + H2O2
-
best substrate
-
-
?
putrescine + O2 + H2O
4-aminobutanal + NH3 + H2O2
-
-
-
?
putrescine + O2 + H2O
4-aminobutanal + NH3 + H2O2
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
ADP competes with FAD, about 50% of wild type monomers isolated are occupied by ADP instead of FAD
FAD
-
the enzyme is isolated as a mixture of dimers containing two molecules of FAD, two molecules ADP, or one FAD and one ADP molecule, the low FAD:protein ratio is the result of tight binding of ADP thereby competing with FAD binding
FAD
the isolated enzyme appears to include only one noncovalently bound FAD per dimeric protein
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
Cd2+
-
inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
Co2+
-
inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
Cu2+
-
inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
Hg2+
-
inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
Ni2+
-
inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
Zn2+
-
inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
putrescine
-
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
additional information
-
not inhibited by spermidine and cadevarine
-
additional information
short diamines and monoamines strongly inhibit activity
-
additional information
no substrate inhibition at concentrations as high as 100 mM/l cadaverine
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.17
1,6-diaminohexane
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25°C
0.065
2-hydroxyputrescine
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25°C
0.33
L-ornithine
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25°C
0.47
spermine
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25°C
0.018
cadaverine
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25°C
0.0035
putrescine
wild type enzyme, in 50 mM Tris-HCl buffer, pH 9.0, at 25°C
0.0082
putrescine
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25°C
0.0086
putrescine
pH 8.0, 25°C, self-assembled enzyme PutOx-AuBP bound to gold nanoparticles
0.0134
putrescine
mutant enzyme P15I/A394C, at pH 8.3 and 25°C
0.02
putrescine
enzyme immobilized by cross-linking on screen-printed carbon electrodes containing tetrathiafulvalene as mediator, pH not specified in the publication, at 20°C
0.021
putrescine
mutant enzyme A394C/A396T/Q431G, at pH 8.3 and 25°C
0.038
putrescine
free enzyme, pH not specified in the publication, at 20°C
110
putrescine
mutant enzyme E324A, in 50 mM Tris-HCl buffer, pH 9.0, at 25°C
110
putrescine
mutant enzyme E324L, in 50 mM Tris-HCl buffer, pH 9.0, at 25°C
0.1
spermidine
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.37
1,6-diaminohexane
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25°C
7.5
2-hydroxyputrescine
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25°C
0.0198
L-ornithine
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25°C
0.18
spermine
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25°C
3.9
cadaverine
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25°C
0.95
putrescine
mutant enzyme A394C/A396T/Q431G, at pH 8.3 and 25°C
3.2
putrescine
mutant enzyme E324L, in 50 mM Tris-HCl buffer, pH 9.0, at 25°C
6.1
putrescine
mutant enzyme E324A, in 50 mM Tris-HCl buffer, pH 9.0, at 25°C
20.7
putrescine
wild type enzyme, in 50 mM Tris-HCl buffer, pH 9.0, at 25°C
25.5
putrescine
pH 8.0, 25°C, self-assembled enzyme PutOx-AuBP bound to gold nanoparticles
26.4