Information on EC 1.5.3.17 - non-specific polyamine oxidase

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-

?

(3S,3'S)-dimethylspermine + 2 O2 + 2 H2O

putrescine + 2 3-aminobutanal + 2 H2O2

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-

?

benzylamidine + O2 + H2O

?

-

-

?

N,N'-bis(3-aminopropyl)ethylenediamine + O2 + H2O

?

-

-

?

N,N'-dibenzyl-1,4-diaminobutane + O2 + H2O

? + H2O2

-

slow substrate

-

?

N1-acetylspermidine + O2 + H2O

?

weak activity

-

?

N1-acetylspermidine + O2 + H2O

putrescine + 3-acetamidopropanal + H2O2

N1-acetylspermidine + O2 + H2O

putrescine + 3-acetaminopropanal + H2O2

-

-

?

N1-acetylspermine + O2 + H2O

?

N1-acetylspermine + O2 + H2O

spermidine + 3-acetamidopropanal + H2O2

7 entries

N1-acetylspermine + O2 + H2O

spermidine + 3-acetaminopropanal + H2O2

N1-acetylspermine + O2 + H2O

spermidine + N-acetyl-3-aminopropanal + H2O2

norspermidine + O2 + H2O

?

-

-

?

norspermine + O2 + H2O

?

9 entries

norspermine + O2 + H2O

? + H2O2

spermidine + O2 + H2O

?

-

-

?

spermidine + O2 + H2O

putrescine + 3-aminobutanal + H2O2

5 entries

spermidine + O2 + H2O

putrescine + 3-aminopropanal + H2O2

8 entries

spermine + O2 + H2O

spermidine + 3-aminopropanal + H2O2

19 entries

spermine + O2 + H2O

spermidine + aminopropanal + H2O2

thermospermine + O2 + H2O

?

6 entries

thermospermine + O2 + H2O

? + H2O2

thermospermine + O2 + H2O

norspermidine + 3-acetamidopropanal + H2O2

thermospermine + O2 + H2O

norspermidine + ?

thermospermine + O2 + H2O

spermidine + ?

tryptamine + O2 + H2O

?

-

-

?

additional information

?

-

29 entries

N,N'-dibenzyl-1,4-diaminobutane + O2 + H2O

? + H2O2

-

slow substrate

-

?

N1-acetylspermidine + O2 + H2O

putrescine + 3-acetamidopropanal + H2O2

N1-acetylspermine + O2 + H2O

spermidine + 3-acetamidopropanal + H2O2

-

-

?

N1-acetylspermine + O2 + H2O

spermidine + N-acetyl-3-aminopropanal + H2O2

spermidine + O2 + H2O

putrescine + 3-aminobutanal + H2O2

spermidine + O2 + H2O

putrescine + 3-aminopropanal + H2O2

-

-

?

spermine + O2 + H2O

spermidine + 3-aminopropanal + H2O2

7 entries

thermospermine + O2 + H2O

?

thermospermine + O2 + H2O

norspermidine + 3-acetamidopropanal + H2O2

norspermidine is generated via thermospermine catabolism in Selaginella lepidophylla

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?

additional information

?

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FAD

10 entries

additional information

aminoguanidine

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dithioerythritol

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up to 0.010 mM increase the enzyme activity, higher concentrations inhibit

dithiothreitol

-

up to 0.010 mM increase the enzyme activity, higher concentrations inhibit

guazatine

Iproniazid

-

0.01 mM, 87% inhibition

isoniazid

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0.01 mM, 81% inhibition

MDL 27391

-

MDL 27695

-

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

-

the specific inhibitor of mammalian polyamine oxidase, has no effect on the Ascaris suum enzyme

N,N'-bis(2,3-butadienyl)-1,4-butanediamine

-

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

putrescine

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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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0.098

(3R,3'R)-dimethylspermine

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pH 7.4, 25°C

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0.061

(3S,3'S)-dimethylspermine

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pH 7.4, 25°C

-

1.6

benzylamidine

-

pH 8.5, 37°C

1.898

N,N'-bis(3-aminopropyl)ethylenediamine

-

pH 7.2, 37°C

0.027 - 0.37

N,N'-dibenzyl-1,4-diaminobutane

0.042 - 1

N1-acetylspermidine

0.0019 - 2.125

N1-acetylspermine

23 entries

5

norspermidine

-

pH 8.5, 37°C

0.011 - 2

norspermine

7 entries

0.0046 - 53

O2

17 entries

0.007 - 2.34

spermidine

23 entries

0.0049 - 0.588

spermine

27 entries

0.0037 - 0.05

thermospermine

5 entries

2.5

tryptamine

-

pH 8.5, 37°C

additional information

6 entries

-

0.77

(3R,3'R)-dimethylspermine

-

pH 7.4, 25°C

-

1.85

(3S,3'S)-dimethylspermine

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pH 7.4, 25°C

-

0.16 - 0.9

N,N'-dibenzyl-1,4-diaminobutane

0.042 - 1

N1-acetylspermidine

0.014 - 49

N1-acetylspermine

17 entries

0.012 - 2.9

norspermine

9 entries

0.009 - 4.6

spermidine

9 entries

0.009 - 39

spermine

20 entries

0.035 - 0.5

thermospermine

8 entries

7.9

(3R,3'R)-dimethylspermine

-

pH 7.4, 25°C

-

30

(3S,3'S)-dimethylspermine

-

pH 7.4, 25°C

-

0.6 - 33

N,N'-dibenzyl-1,4-diaminobutane

0.01 - 1400

N1-acetylspermine

12 entries

0.747 - 24.4

norspermine

5 entries

0.08 - 428

O2

18 entries

0.185 - 12.4

spermidine

0.115 - 400

spermine

15 entries

2.6 - 23.3

thermospermine

0.00108 - 0.0018

aminoguanidine

0.000028

guazatine

0.02

MDL 27695

-

pH 8.5, 37°C

0.0009

MDL 72145

-

0.0408

N8-Acetylspermidine

0.0615

putrescine

0.172

triethylenetetramine

-

pH 7.2, 37°C, with spermine as substrate

2.3

-

6

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substrate: thermospermine

743460

6.5

Q9SU79

substrate: thermospermine

743491

7

substrate: thermospermine

7 - 8

dependent on the substrate

7.2

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assay at

7.5

7.5 - 8

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8

8.5

8.6 - 10

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assay at

9

9.35

substrate spermine

6 - 10

pH 6.0: about 65% of maximal activity, pH 10.0: about 35% of maximal activity, substrate: thermospermine

743491

7 - 8.5

pH 7: about 95% of maximal activity, pH 8.5: about 55% of maximal activity

7 - 9

Q9SU79

pH 7.0: about 60% of maximal activity, pH 9.0: about 45% of maximal activity, substrate: spermine

743491

additional information

25

30

30 - 37

-

35

37

37 - 42

substrate: spermine

45

substrate: thermospermine

25 - 50

30 - 40

30°C: about 85% of maximal activity, 40°C: about 60% of maximal activity

4.9

calculated from sequence

5.13

calculated from sequence

5.81

7.8

-

isoelectric focusing

Arabidopsis thaliana Col-0

19 entries

Arabidopsis thaliana Columbia-0

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Oryza sativa cv. Nipponbare

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-

-

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-

-

743460

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Plantae

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764377

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Rattus norvegicus

female Sprague-Dawley rats

704633

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-

742522, 765637

Synechocystis sp. PCC 6803

UniProt

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UniProt

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from Pneumocystis carinii infected rats

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

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hindgut

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of seedling

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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

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-

additional information

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evolution

malfunction

metabolism

physiological function

15 entries

additional information

Saccharomyces cerevisiae S288C

54100

66000

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x * 66000, SDS-PAGE

?

flavoprotein

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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

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

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

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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme

H64N

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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme

H64Q

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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

30

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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

-20°C, stable for 2 days (minimal loss of activity), complete loss of enzyme activity after 14 days

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native enzyme partially from leaves by ammonium sulfate fractionation

Hordeum vulgare

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703471

recombinant AtPAO3 fused to the maltose-binding protein from Escherichia coli

recombinant His-tagged wild-type and mutant enzymes by nickel affinity chhromatography

recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography

recombinant maltose-binding protein fusion enzyme from Escherichia coli by amylose affinity chromatography

Synechocystis sp. PCC 6803

recombinant protein

Q6ZEN7

765603

recombinant wild-type and mutant enzymes

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

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

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

DNA and amino acid sequence determination and analysis, recombinant expression of wild-type and mutant enzymes

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expression in Escherichia coli

gene AtPAO2, construction of AtPAO::GUS transgenic Arabidopsis thaliana plants

723919

gene AtPAO3, construction of AtPAO::GUS transgenic Arabidopsis thaliana plants

723919

gene AtPAO5, construction of AtPAO::GUS transgenic Arabidopsis thaliana plants

723919

production of recombinant SelPAO5 protein in Escherichia coli

recombinant expression of His-tagged wild-type and mutant enzymes

recombinant expression of wild-type and mutant enzymes

transient expression of isozyme AtPAO3 in Arabidopsis thaliana root cell peroxisomes as monomeric red fluorescent protein fusion protein

694651

wild-type and mutant enzymes expressed in Escherichia coli

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

Q9SKX5

743272

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

cellular iron levels robustly regulate 13 polyamine pathway proteins. Four proteins are down-regulated (i.e., acireductone dioxygenase 1, methionine adenosyltransferase 2alpha, antizyme and polyamine oxidase) and three proteins are up-regulated (i.e., S-adenosyl methionine decarboxylase, antizyme inhibitor 1 and spermidine/spermine-N1-acetyltransferase 1). Depletion of iron also markedly decreases polyamine pools, (i.e., spermidine and/or spermine, but not putrescine)

Homo sapiens

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764224

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

isoforms PAO1 and PAO2 genes are transcriptionally up-regulated in plants infected by Pseudomonas syringae

Q9FNA2, Q9SKX5

765617

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

Q9SKX5

743529

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

Q9SKX5

743529

positive regulation of AtPAO5 expression by polyamines at the transcriptional and post-transcriptional level

Q9SU79

742993

the peptide derived from the AtPAO2 uORF is necessary for translational regulation of the AtPAO2 mORF

analysis

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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

703471

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

synthesis

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application of simple guide molecules, being either covalently attached to polyamines or used as a supplement to the substrate mixtures, for controlling the enzyme's regioselectivity and stereospecificity