Information on EC 1.5.3.17 - non-specific polyamine oxidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.5.3.17
-
RECOMMENDED NAME
GeneOntology No.
non-specific polyamine oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N1-acetylspermidine + O2 + H2O = putrescine + 3-acetamidopropanal + H2O2
show the reaction diagram
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-
-
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N1-acetylspermine + O2 + H2O = spermidine + 3-acetamidopropanal + H2O2
show the reaction diagram
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-
-
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spermidine + O2 + H2O = putrescine + 3-aminopropanal + H2O2
show the reaction diagram
-
-
-
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spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2
show the reaction diagram
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
-
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beta-alanine biosynthesis IV
-
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beta-Alanine metabolism
-
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spermine and spermidine degradation I
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spermine and spermidine degradation III
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polyamine pathway
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SYSTEMATIC NAME
IUBMB Comments
polyamine:oxygen oxidoreductase (3-aminopropanal or 3-acetamidopropanal-forming)
A flavoprotein (FAD). The non-specific polyamine oxidases may differ from each other considerably. The enzyme from Saccharomyces cerevisiae shows a rather broad specificity and also oxidizes N8-acetylspermidine [3]. The enzyme from Ascaris suum shows high activity with spermine and spermidine, but also oxidizes norspermine [2]. The enzyme from Arabidopsis thaliana shows high activity with spermidine, but also oxidizes other polyamines [1]. The specific polyamine oxidases are classified as EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.14 (polyamine oxidase (propane-1,3-diamine-forming)), EC 1.5.3.15 (N8-acetylspermidine oxidase (propane-1,3-diamine-forming)) and EC 1.5.3.16 (spermine oxidase).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
-
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Manually annotated by BRENDA team
female Sprague-Dawley rats
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
benzylamidine + O2 + H2O
?
show the reaction diagram
-
-
-
-
?
N,N'-dibenzyl-1,4-diaminobutane + O2 + H2O
? + H2O2
show the reaction diagram
-
slow substrate
-
-
?
N1-acetylspermidine + O2 + H2O
?
show the reaction diagram
weak activity
-
-
?
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetamidopropanal + H2O2
show the reaction diagram
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetaminopropanal + H2O2
show the reaction diagram
-
-
-
?
N1-acetylspermine + O2 + H2O
?
show the reaction diagram
weak activity
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
show the reaction diagram
-
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetaminopropanal + H2O2
show the reaction diagram
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + acetaminopropanal
show the reaction diagram
N1-acetylspermine + O2 + H2O
spermidine + N-acetyl-3-aminopropanal + H2O2
show the reaction diagram
norspermidine + O2 + H2O
?
show the reaction diagram
-
-
-
-
?
norspermine + O2 + H2O
?
show the reaction diagram
norspermine + O2 + H2O
? + H2O2
show the reaction diagram
spermidine + O2 + H2O
putrescine + 3-aminobutanal + H2O2
show the reaction diagram
spermidine + O2 + H2O
putrescine + 3-aminopropanal + H2O2
show the reaction diagram
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
show the reaction diagram
spermine + O2 + H2O
spermidine + aminopropanal + H2O2
show the reaction diagram
thermospermine + O2 + H2O
?
show the reaction diagram
-
-
-
?
thermospermine + O2 + H2O
? + H2O2
show the reaction diagram
tryptamine + O2 + H2O
?
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
N,N'-dibenzyl-1,4-diaminobutane + O2 + H2O
? + H2O2
show the reaction diagram
-
slow substrate
-
-
?
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetamidopropanal + H2O2
show the reaction diagram
N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
show the reaction diagram
-
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + N-acetyl-3-aminopropanal + H2O2
show the reaction diagram
spermidine + O2 + H2O
putrescine + 3-aminobutanal + H2O2
show the reaction diagram
spermidine + O2 + H2O
putrescine + 3-aminopropanal + H2O2
show the reaction diagram
Q9LYT1
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithioerythritol
-
up to 0.010 mM increase the enzyme activity, higher concentrations inhibit
dithiothreitol
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up to 0.010 mM increase the enzyme activity, higher concentrations inhibit
Iproniazid
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0.01 mM, 87% inhibition
Isoniazid
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0.01 mM, 81% inhibition
MDL 27391
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-
MDL 27695
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-
MDL 72145
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inhibited in a time-dependent manner. Half-life under saturation conditions is 0.8 min. MDL 72145 might be a chemical lead compound for the design of new chemotherapeutic agents against nematode infections
MDL 72527
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the specific inhibitor of mammalian polyamine oxidase, has no effect on the Ascaris suum enzyme
N8-Acetylspermidine
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NEM
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0.01 mM, 85% inhibition
additional information
-
the polyamine oxidase inhibitor MDL 72527 has no effect on the parasite polyamine oxidase activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.6
benzylamidine
-
pH 8.5, 37C
0.027 - 0.37
N,N'-dibenzyl-1,4-diaminobutane
0.042 - 1
N1-acetylspermidine
0.011 - 2
N1-acetylspermine
5
norspermidine
-
pH 8.5, 37C
0.045 - 2
norspermine
0.015 - 53
O2
0.139 - 0.66
spermidine
0.04 - 0.588
spermine
0.05
thermospermine
2.5
tryptamine
-
pH 8.5, 37C
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.16 - 0.9
N,N'-dibenzyl-1,4-diaminobutane
0.042 - 1
N1-acetylspermidine
0.014 - 49
N1-acetylspermine
0.45 - 2.9
norspermine
0.1 - 4.6
spermidine
0.12 - 39
spermine
0.1 - 0.5
thermospermine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6 - 33
N,N'-dibenzyl-1,4-diaminobutane
8969
0.01 - 1400
N1-acetylspermine
1108
24.4
norspermine
Arabidopsis thaliana
Q9LYT1, Q9SKX5
pH 7.5, temperature not specified in the publication
4120
0.08 - 428
O2
9
11.2 - 12.4
spermidine
148
1.4 - 330
spermine
197
10
thermospermine
Arabidopsis thaliana
Q9LYT1, Q9SKX5
pH 7.5, temperature not specified in the publication
4728
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00108 - 0.0018
aminoguanidine
0.000028
guazatine
37C, pH 7.0; pH 7.5, 37C, recombinant AtPAO3
0.02
MDL 27695
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pH 8.5, 37C
0.0009
MDL 72145
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-
0.0408
N8-Acetylspermidine
37C, pH 7.0; pH 7.5, 37C, recombinant AtPAO3
0.0615
putrescine
37C, pH 7.0; pH 7.5, 37C, recombinant AtPAO3
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
dependent on the substrate
8.6 - 10
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assay at
9
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substrate N1-acetylspermine
9.35
-
substrate spermine
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8.5
pH 7: about 95% of maximal activity, pH 8.5: about 55% of maximal activity
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
37
; at higher temperatures, AtPAO3 is quickly inactivated
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 40
30C: about 85% of maximal activity, 40C: about 60% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.81
AtPAO3, sequence calculation; calculated from sequence
7.8
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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from Pneumocystis carinii infected rats
Manually annotated by BRENDA team
expression at higher extent in the later growth stage within restricted parts of the organs, such as shoot meristem, leaf petiole and also in anther
Manually annotated by BRENDA team
; already in very young, completely closed flower buds
Manually annotated by BRENDA team
expression at higher extent in the later growth stage within restricted parts of the organs, such as shoot meristem, leaf petiole and also in anther
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54100
x * 54100, AtPAO3, sequence calculation; x * 54100, calculated from sequence
66000
-
x * 66000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme mutant H67Q, sitting drop vapor diffusion method, mixing of protein solution, in 25 mM HEPES, pH 7.5, in a 1:1 ratio with buffer containing 20% w/v PEG 3350, 0.2 M sodium acetate, and 0.1 M bis-Tris propane, pH 7.5, X-ray diffraction structure determination and analysis at 2.4 A resolution, molecular replacement
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purified recombinant enzyme mutant N195A, sitting drop vapour diffusion method, mixing of protein solution, containing 25 mM HEPES, 25 mM NaCl, and 2% glycerol, pH 7.5, in a 1:1 ratio with buffer containing 30 mM diethylene glycol, 30 mM triethylene glycol, 30 mM tetraethylene glycol, 30 mM pentaethylene glycol, 10% ethylene glycol, 20% PEG 8000, and 0.1 MES-imidazole, pH 6.5, 1 week, X-ray diffraction structure determination and analysis at 2.0 A resolution
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
60 min, complete loss of activity
37
-
60 min, complete loss of activity
42
-
60 min, complete loss of activity
56
-
60 min, complete loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for 2 days (minimal loss of activity), complete loss of enzyme activity after 14 days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; recombinant AtPAO3 fused to the maltose-binding protein from Escherichia coli
native enzyme partially from leaves by ammonium sulfate fractionation
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recombinant His-tagged wild-type and mutant enzymes by nickel affinity chhromatography
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recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography; recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography; recombinant maltose-binding protein fusion enzyme from Escherichia coli by amylose affinity chromatography
recombinant wild-type and mutant enzymes
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AtPAO2, DNA and amino acid sequence determination and analysis, intron/exon organization, sequence comparisons, expression of His6-tagged enzyme in Escherichia coli, expression of GFP-tagged AtPAO3 in Arabidopsis thaliana plants using the Agrobacterium tumefaciens (strain C58C1)-mediated floral dip transformation method; AtPAO3, DNA and amino acid sequence determination and analysis, intron/exon organization, sequence comparisons, recombinant expression as maltose-binding protein fusion protein in Escherichia coli, and expression of GFP-tagged AtPAO3 in transgenic Arabidopsis thaliana plants using the Agrobacterium tumefaciens (strain C58C1)-mediated floral dip transformation method resulting in increased putrescine levels after feeding of exogenous spermidine; AtPAO4, DNA and amino acid sequence determination and analysis, intron/exon organization, sequence comparisons, expression of His6-tagged enzyme in Escherichia coli, expression of GFP-tagged AtPAO3 in Arabidopsis thaliana plants using the Agrobacterium tumefaciens (strain C58C1)-mediated floral dip transformation method
AtPAO3, expression as GFP-tagged enzyme in plant cells, expression of AtPAO3 fused to the maltose-binding protein in Escherichia coli strain BL21 in a temperature-dependent manner, overview; expression in Escherichia coli
DNA and amino acid sequence determination and analysis, recombinant expression of wild-type and mutant enzymes
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gene AtPAO2, construction of AtPAO::GUS transgenic Arabidopsis thaliana plants; gene AtPAO3, construction of AtPAO::GUS transgenic Arabidopsis thaliana plants; gene AtPAO5, construction of AtPAO::GUS transgenic Arabidopsis thaliana plants
recombinant expression of His-tagged wild-type and mutant enzymes
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recombinant expression of wild-type and mutant enzymes
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transient expression of isozyme AtPAO3 in Arabidopsis thaliana root cell peroxisomes as monomeric red fluorescent protein fusion protein
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
AtPAO3 mRNA rapidly accumulats in wounded plants 1 h after wounding and returns to almost basal levels 6 h thereafter. Seedlings treated with flagellin 22, a pathogen elicitor that activates the plant basal defense, exhibits AtPAO3 induction after the 6-h time point, with constant increase up to 24 h
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H64A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H64N
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H64Q
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D94N
-
site-directed mutagenesis, the mutation primarily affects the reductive half-reaction. The mutant shows 20-40fold reduced rate constant for flavin reduction with spermine and 450fold with N1-acetylspermine compared to the wild-type enzyme
H67A
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site-directed mutagenesis, the mutant shows a 2-3fold reduced first-order rate constant for flavin reduction and slightly altered kinetics compared to the wild-type enzyme
H67N
-
site-directed mutagenesis, the mutant shows a 2-3fold reduced first-order rate constant for flavin reduction and slightly altered kinetics compared to the wild-type enzyme
H67Q
-
site-directed mutagenesis, the mutant shows a 2-3fold reduced first-order rate constant for flavin reduction and slightly altered kinetics compared to the wild-type enzyme
N195A
-
site-directed mutagenesis, the mutation primarily affects the reductive half-reaction. The mutant shows 20-40fold reduced rate constant for flavin reduction with spermine and 450fold with N1-acetylspermine compared to the wild-type enzyme. Mutant N195A enzyme shows structure with a molecule of tetraethylene glycol in the active site, the mutation has no effect on the protein structure
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
the seedling polyamine oxidase is used for development of colorimetric assay methods to determine total polyamine, i.e. spermidine and spermine, and spermine concentrations in whole blood of humans, respectively, mechanism, overview
medicine
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the inhibitor MDL 72145 might be a chemical lead compound for the design of new chemotherapeutic agents against nematode infections