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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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
beta-alanine biosynthesis IV
-
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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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Arginine and proline metabolism
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beta-Alanine metabolism
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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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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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-
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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
malfunction
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'-bis(3-aminopropyl)ethylenediamine + 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
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
?
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
thermospermine + O2 + H2O
norspermidine + 3-acetamidopropanal + H2O2
show the reaction diagram
norspermidine is generated via thermospermine catabolism in Selaginella lepidophylla
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-
?
thermospermine + O2 + H2O
norspermidine + ?
show the reaction diagram
thermospermine + O2 + H2O
spermidine + ?
show the reaction diagram
tryptamine + O2 + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
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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
thermospermine + O2 + H2O
?
show the reaction diagram
thermospermine + O2 + H2O
norspermidine + 3-acetamidopropanal + H2O2
show the reaction diagram
A0A0M3VGH5
norspermidine is generated via thermospermine catabolism in Selaginella lepidophylla
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-
?
additional information
?
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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
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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
N,N'-bis(2,3-butadienyl)-1,4-butanediamine
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i.e. MDL72527
N1,N4-bis(2,3-butadienyl)-1,4-butanediamine
2.5 mM, 50% inhibition of spermidine oxidation, 70% inhibition of N1-acetylspermine oxidation; 2.5 mM, 50% inhibition of spermidine oxidation, 70% inhibition of spermine oxidation
N8-Acetylspermidine
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NEM
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0.01 mM, 85% inhibition
triethylenetetramine
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competitive inhibitor with spermine as substrate
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
1.898
N,N'-bis(3-aminopropyl)ethylenediamine
-
pH 7.2, 37C
-
0.027 - 0.37
N,N'-dibenzyl-1,4-diaminobutane
0.042 - 1
N1-acetylspermidine
0.0019 - 2.125
N1-acetylspermine
5
norspermidine
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pH 8.5, 37C
0.011 - 2
norspermine
0.0046 - 53
O2
0.007 - 2.34
spermidine
0.0049 - 0.588
spermine
0.0037 - 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
0.012 - 2.9
norspermine
0.009 - 4.6
spermidine
0.009 - 39
spermine
0.035 - 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
0.01 - 1400
N1-acetylspermine
0.747 - 24.4
norspermine
0.08 - 428
O2
0.185 - 12.4
spermidine
0.115 - 330
spermine
2.6 - 23.3
thermospermine
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
0.172
triethylenetetramine
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pH 7.2, 37C, with spermine as substrate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
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substrate: thermospermine
6.5
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substrate: thermospermine
7 - 8
dependent on the substrate
7
substrate: thermospermine
7.2
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assay at
8.6 - 10
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assay at
9.35
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substrate spermine
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
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pH 6.0: about 65% of maximal activity, pH 10.0: about 35% of maximal activity, substrate: thermospermine
7 - 8.5
pH 7: about 95% of maximal activity, pH 8.5: about 55% of maximal activity
7 - 9
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pH 7.0: about 60% of maximal activity, pH 9.0: about 45% of maximal activity, substrate: spermine
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 42
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substrate: spermine
45
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substrate: thermospermine
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 50
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25C: about 45% of maximal activity, 50C: about 90% of maximal activity, substrate: thermospermine; 25C: about 55% of maximal activity, 50C: about 45% of maximal activity, substrate: spermine
30 - 40
30C: about 85% of maximal activity, 40C: about 60% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
calculated from sequence
5.13
calculated from sequence
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
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-
Manually annotated by BRENDA team
; Bjpao1 is predominantly expressed in the notochord, testis and ovary
Manually annotated by BRENDA team
; Bjpao1 is predominantly expressed in the notochord, testis and ovary
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
; Bjpao1 is predominantly expressed in the notochord, testis and ovary
Manually annotated by BRENDA team
additional information
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
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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
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60 min, complete loss of activity
42
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60 min, complete loss of activity
56
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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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expression in Escherichia coli
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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
production of recombinant SelPAO5 protein in Escherichia coli
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
wild-type and mutant enzymes expressed in Escherichia coli; wild-type and mutant enzymes expressed in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
AtPAO2 uORF has a regulatory role in regulating AtPAO2 expression. The fact that uORFs are commonly found in plant polyamine oxidase genes is relevant, implying that regulatory elements in the 5'-UTR of polyamine biosynthetic and catabolic genes might finely control the intracellular concentration of polyamines in plant development and stress responses
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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
expression is down-regulated by dehydration stress
expression is up-regulated by thermospermine treatment
expression of the enzyme OsPAO1 appears to be quite low under physiological conditions, but is markedly induced in rice roots by spermine or thermospermine treatment
NO3- induced AtPAO2::GUS expression is quenched by the presence of NH4+ in the growth medium and abscisic acid-induced AtPAO2::GUS expression is more prominent when the plants are grown on NO3- as the only N source. PAO2OX (an AtPAO2 over-expressing transgenic line) is partially unresponsive to abscisic acid in some growth conditions depending on N-source, pao2 mutants being often more sensitive to abscisic acid than the similarly grown WT; NO3- induced AtPAO2::GUS expression is quenched by the presence of NH4+ in the growth medium and abscisic acid-induced AtPAO2::GUS expression was more prominent when the plants are grown on NO3- as the only N source
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positive regulation of AtPAO5 expression by polyamines at the transcriptional and post-transcriptional level
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the peptide derived from the AtPAO2 uORF is necessary for translational regulation of the AtPAO2 mORF
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H64E
Vmax values for mutant enzyme with substrate spermine or spermidine are lower than Vmax values for wild-type enzym. Km values for mutant enzyme with substrate spermine or spermidine are higher than Km values for wild-type enzym
H64Q
Vmax values for mutant enzyme with substrate spermine or spermidine are lower than Vmax values for wild-type enzym. Km values for mutant enzyme with substrate spermine or spermidine are higher than Km values for wild-type enzym
H69E
compared with the wild-type enzyme the mutant enzyme shows lower Vmax values and higher Km-values for the substrates spermidine and N1-acetylspermine
H69Q
compared with the wild-type enzyme the mutant enzyme shows lower Vmax values and higher Km-values for the substrates spermidine and N1-acetylspermine
K301M
Vmax values for mutant enzyme with substrate spermine or spermidine are lower than Vmax values for wild-type enzym. Km values for mutant enzyme with substrate spermine or spermidine are higher than Km values for wild-type enzym
K315M
compared with the wild-type enzyme the mutant enzyme shows lower Vmax values and higher Km-values for the substrates spermidine and N1-acetylspermine
T460S
Vmax values for mutant enzyme with substrate spermine or spermidine are lower than Vmax values for wild-type enzym. Km values for mutant enzyme with substrate spermine or spermidine are higher than Km values for wild-type enzym
T460Y
Vmax values for mutant enzyme with substrate spermine or spermidine are lower than Vmax values for wild-type enzym. Km values for mutant enzyme with substrate spermine or spermidine are higher than Km values for wild-type enzym
T467S
compared with the wild-type enzyme the mutant enzyme shows lower Vmax values and higher Km-values for the substrates spermidine and N1-acetylspermine
T467Y
compared with the wild-type enzyme the mutant enzyme shows lower Vmax values and higher Km-values for the substrates spermidine and N1-acetylspermine
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
-
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
-
the inhibitor MDL 72145 might be a chemical lead compound for the design of new chemotherapeutic agents against nematode infections