Information on EC 1.4.3.10 - putrescine oxidase

Word Map on EC 1.4.3.10
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.4.3.10
-
RECOMMENDED NAME
GeneOntology No.
putrescine oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
putrescine + O2 + H2O = 4-aminobutanal + NH3 + H2O2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
oxidative deamination
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
-
-
Metabolic pathways
-
-
putrescine degradation IV
-
-
SYSTEMATIC NAME
IUBMB Comments
putrescine:oxygen oxidoreductase (deaminating)
A flavoprotein (FAD). 4-Aminobutanal condenses non-enzymically to 1-pyrroline.
CAS REGISTRY NUMBER
COMMENTARY hide
9076-87-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
formerly Micrococcus rubens
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,3-diaminopropane + O2 + H2O
3-aminopropanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
1,6-diaminohexane + O2 + H2O
6-aminohexanal + NH3 + H2O2
show the reaction diagram
1.4% activity compared to putrescine
-
-
?
1,6-diaminohexane + O2 + H2O
?
show the reaction diagram
1,7-diaminoheptane + O2 + H2O
?
show the reaction diagram
-
-
-
-
?
2-hydroxyputrescine + O2 + H2O
?
show the reaction diagram
28% activity compared to putrescine
-
-
?
4-amino-1-butanol + O2 + H2O
4-hydroxybutanal + NH3 + H2O2
show the reaction diagram
0.6% activity compared to putrescine
-
-
?
benzylamine + O2 + H2O
benzaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
cadaverine + O2 + H2O
5-aminopentanal + NH3 + H2O2
show the reaction diagram
ethylamine + O2 + H2O
?
show the reaction diagram
-
-
-
-
?
histamine + O2 + H2O
1H-imidazol-4-ylacetaldehyde + NH3 + H2O2
show the reaction diagram
histamine + O2 + H2O
?
show the reaction diagram
L-ornithine + O2 + H2O
?
show the reaction diagram
0.08% activity compared to putrescine
-
-
?
N-acetylputrescine + O2 + H2O
N4-acetylaminobutanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
N1-acetylspermidine + O2 + H2O
?
show the reaction diagram
-
-
-
-
?
N8-acetylspermidine + O2 + H2O
?
show the reaction diagram
-
-
-
-
?
putrescine + O2 + H2O
4-aminobutanal + NH3 + H2O2
show the reaction diagram
spermidine + O2 + H2O
4-aminobutyraldehyde + 1,3-diaminopropane + H2O2
show the reaction diagram
spermidine + O2 + H2O
N,N'-bis(3-aminopropyl)-4-aminobutanal + NH3 + H2O2
show the reaction diagram
spermine + O2 + H2O
N,N'-bis(3-aminopropyl)-4-aminobutanal + NH3 + H2O2
show the reaction diagram
tryptamine + O2 + H2O
1H-indol-3-yl-acetaldehyde + NH3 + H2O2
show the reaction diagram
-
5.2% activity compared to putrescine
-
-
?
tyramine + O2 + H2O
(4-hydroxyphenyl)acetaldehyde + NH3 + H2O2
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
putrescine + O2 + H2O
4-aminobutanal + NH3 + H2O2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
ADP competes with FAD, about 50% of wild type monomers isolated are occupied by ADP instead of FAD
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no activation by divalent cations
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2-aminoethyl)-trimethylammonium
competitive inhibitor
1,1,4,4-tetramethyl-1,4-diaminobutane
-
-
1,10-Diaminodecane
-
-
1,12-diaminododecane
-
-
1,3-Diaminopropane
1,6-diaminohexane
-
-
1,7-Diaminoheptane
-
-
1,8-diaminooctane
-
-
1-aminoethanol
-
-
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
2-Aminoethanol
-
-
3-Amino-1-propanol
-
-
4-amino-1-butanoic acid
-
-
5-amino-1-pentanoic acid
-
-
5-amino-1-pentanol
-
-
6-amino-1-hexanoic acid
-
-
6-amino-1-hexanol
-
-
8-amino-1-octanoic acid
-
-
agmatine
-
-
allylamine
-
-
Aminoethanol
competitive inhibitor
aminoguanidine
-
-
Aminoguanidine hydrogen carbonate
-
-
ammonium
-
-
benzylamine
-
-
Butylamine
-
-
cadaverine
-
noncompetitive against putrescine
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
cyanide
-
-
dodecylamine
-
-
ethylamine
-
-
ethylenediamine
heptylamine
-
-
Hexylamine
-
-
Hg2+
-
inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
hydroxylamine
-
-
Iproniazid
-
-
methylamine
-
-
methylglyoxal bis(guanylhydrazine)dihydrochloride monohydrate
-
-
N,N,N',N'-tetramethyl-1,4-diaminobutane
-
-
n-butylamine
competitive inhibitor
Ni2+
-
inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
Pentylamine
-
-
Phenylethylamine
-
-
Propylamine
-
-
putrescine
spermidine
-
competitive inhibition of putrescine oxidation
spermine
-
competitive inhibition of putrescine oxidation
tyramine
-
-
Zn2+
-
inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.17
1,6-diaminohexane
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25C
0.065
2-hydroxyputrescine
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25C
0.018 - 1.1
cadaverine
0.33
L-ornithine
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25C
0.124
O2
-
-
0.0026 - 110
putrescine
0.025 - 0.35
spermidine
0.47
spermine
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.37
1,6-diaminohexane
Rhodococcus erythropolis
B0F9F6
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25C
7.5
2-hydroxyputrescine
Rhodococcus erythropolis
B0F9F6
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25C
1.72 - 3.9
cadaverine
0.0198
L-ornithine
Rhodococcus erythropolis
B0F9F6
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25C
0.79 - 31.8
putrescine
0.29 - 1.4
spermidine
0.18
spermine
Rhodococcus erythropolis
B0F9F6
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.78
cadaverine
Paenarthrobacter aurescens
-
at pH 8.0 and 55C
533
45 - 419
putrescine
155
0.83
spermidine
Paenarthrobacter aurescens
-
at pH 8.0 and 55C
148
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.8
(2-aminoethyl)-trimethylammonium
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25C
0.19
1,1,4,4-tetramethyl-1,4-diaminobutane
-
-
0.003
1,10-Diaminodecane
-
-
0.002
1,12-diaminododecane
-
-
0.064 - 0.12
1,3-Diaminopropane
0.023
1,6-diaminohexane
-
-
0.0082
1,7-Diaminoheptane
-
-
0.0032
1,8-diaminooctane
-
-
3
2-Aminoethanol
-
-
0.5 - 0.67
3-Amino-1-propanol
440
4-amino-1-butanoic acid
-
-
59
5-amino-1-pentanoic acid
-
-
0.088
5-amino-1-pentanol
-
-
300
6-amino-1-hexanoic acid
-
-
0.31
6-amino-1-hexanol
-
-
160
8-amino-1-octanoic acid
-
-
0.036
agmatine
-
-
0.013
allylamine
-
-
0.0018
Aminoethanol
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25C
0.000022
aminoguanidine
-
with putrescine as substrate
20
ammonium
-
-
0.047
benzylamine
-
-
0.46
Butylamine
-
-
0.28
cadaverine
-
-
0.0082
dodecylamine
-
-
2.3
ethylamine
-
-
0.66 - 0.95
ethylenediamine
0.014
heptylamine
-
-
0.039
Hexylamine
-
-
3.4
methylamine
-
-
0.000024
methylglyoxal bis(guanylhydrazine)dihydrochloride monohydrate
-
-
0.14
N,N,N',N'-tetramethyl-1,4-diaminobutane
-
-
0.12
n-butylamine
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25C
0.24
Pentylamine
-
-
0.087
Phenylethylamine
-
-
0.62
Propylamine
-
-
19.1
putrescine
-
at pH 8.0 and 55C
0.181
spermidine
-
-
0.0581
spermine
-
-
0.039
tyramine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
59.16
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.6
-
-
8 - 11.7
-
-
8.5
-
spermidine
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 9
-
pH 6.8: about 50% of maximal activity, pH 9.0: about 60% of maximal activity
7 - 10
-
the enzyme exhibits more than 90% of the maximum activity at pH 7.0 to 10.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 50
-
20C: about 45% of maximal activity, 50C: about 50% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
ovary senescence is characterized by increased level of putrescine oxidase, constant level of putrescine oxidase during fruit development
Manually annotated by BRENDA team
additional information
-
high level of enzyme is produced in cells from the late exponential growth phase
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46000
-
2 * 46000, SDS-PAGE
54000
2 * 54000, SDS-PAGE
83400 - 87000
-
calculation from sedimentation data
90000
-
gel filtration
98750
theoretical molecular mass
100100
-
mass spectrometry
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 50000, SDS-PAGE
dimer
-
2 * 46000, SDS-PAGE
homodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 2.0-2.4 M ammonium sulfate, 0.1 M sodium citrate, and 0.1 M MES-HCl pH 6.4
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10.5
-
stable
288077
6.4
below pH 6.4, no significant activity can be detected
684634
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 50
at 50C, half of the activity is lost after 2 h, while at 37C, such a degree of inactivation is reached after 1 day
60
-
pH 7.5, 20 min, 93% loss of activity
additional information
-
the enzyme is resistant to heat denaturation as long as it is maintained in a fully reduced state
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
photoreduction of the enzyme in presence of EDTA
-
395438
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, in presence of 25% glycerol, 1 year, stable
-
-22C, stable for months
-
5C, 0.01 M phosphate buffer, pH 6.0-8.0, little loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, HiTrap DEAE column chromatography, EAH Superose column chromatography, and Superose 12 gel filtration
-
His-Trap column chromatography
-
Q-Sepharose column chromatography
three-phase partitioning and DEAE Sephadex gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli Top10 cells
-
expression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A394C/A396T/Q431G
mutant with strongly reduced catalytic efficiency
A394C/V433M
the mutations improve the affinity toward FAD
E324A
the mutant enzyme shows activity with monoamines, which are not accepted by the wild type enzyme
E324L
the mutant enzyme shows activity with monoamines, which are not accepted by the wild type enzyme
P15I/A394C
the mutations improve the affinity toward FAD
A394C
-
active mutant with covalently bound FAD
-
E324A
-
the mutant enzyme shows activity with monoamines, which are not accepted by the wild type enzyme
-
E324L
-
the mutant enzyme shows activity with monoamines, which are not accepted by the wild type enzyme
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
diagnostics
-
enzyme can be used as biosensor for putrescine using dispersed multiwalled carbon nanotubes as ultra-microelectrodes ensuring a good electron transfer from the enzyme, method optimization, overview
food industry
Show AA Sequence (255 entries)
Please use the Sequence Search for a specific query.