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Information on EC 1.5.3.13 - N1-acetylpolyamine oxidase and Organism(s) Homo sapiens

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EC Tree
     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.3 With oxygen as acceptor
                1.5.3.13 N1-acetylpolyamine oxidase
IUBMB Comments
The enzyme also catalyses the reaction: N1,N12-diacetylspermine + O2 + H2O = N1-acetylspermidine + 3-acetamamidopropanal + H2O2 . No or very weak activity with spermine, or spermidine in absence of aldehydes. In presence of aldehydes the enzyme catalyses the reactions: 1. spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2, and with weak efficiency 2. spermidine + O2 + H2O = putrescine + 3-aminopropanal + H2O2 . A flavoprotein (FAD). This enzyme, encoded by the PAOX gene, is found in mammalian peroxisomes and oxidizes N1-acetylated polyamines at the exo (three-carbon) side of the secondary amine, forming 3-acetamamidopropanal. Since the products of the reactions are deacetylated polyamines, this process is known as polyamine back-conversion. Differs in specificity from 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)], EC 1.5.3.16 (spermine oxidase) and EC 1.5.3.17 (non-specific polyamine oxidase).
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
polyamine oxidase, paoh1, n1-acetylpolyamine oxidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N1-acetyl polyamine oxidase
-
-
N1-acetylpolyamine oxidase
-
PAOh1
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
N1-acetylpolyamine:oxygen oxidoreductase (3-acetamidopropanal-forming)
The enzyme also catalyses the reaction: N1,N12-diacetylspermine + O2 + H2O = N1-acetylspermidine + 3-acetamamidopropanal + H2O2 [1]. No or very weak activity with spermine, or spermidine in absence of aldehydes. In presence of aldehydes the enzyme catalyses the reactions: 1. spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2, and with weak efficiency 2. spermidine + O2 + H2O = putrescine + 3-aminopropanal + H2O2 [2]. A flavoprotein (FAD). This enzyme, encoded by the PAOX gene, is found in mammalian peroxisomes and oxidizes N1-acetylated polyamines at the exo (three-carbon) side of the secondary amine, forming 3-acetamamidopropanal. Since the products of the reactions are deacetylated polyamines, this process is known as polyamine back-conversion. Differs in specificity from 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)], EC 1.5.3.16 (spermine oxidase) and EC 1.5.3.17 (non-specific polyamine oxidase).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-alpha-methylspermidine + O2 + H2O
?
show the reaction diagram
-
PAO supplemented with benzaldehyde predominantly catalyzes the cleavage of (R)-isomer of alpha-methylspermidine, whereas in the presence of pyridoxal the (S)-alpha-methylspermidine is preferred
-
-
?
(S)-alpha-methylspermidine + O2 + H2O
?
show the reaction diagram
-
PAO supplemented with benzaldehyde predominantly catalyzes the cleavage of (R)-isomer of alpha-methylspermidine, whereas in the presence of pyridoxal the (S)-alpha-methylspermidine is preferred
-
-
?
(S)-N1-(2-methyl-1-butyl)-N11-ethyl-4,8-diazaundecane-1,11-diamine + O2 + H2O
?
show the reaction diagram
-
-
-
?
1-amino-8-acetamido-5-azanonane + O2 + H2O
?
show the reaction diagram
-
less preferred substrate
-
-
?
alpha-methylspermidine + O2 + H2O
?
show the reaction diagram
-
weak oxidation in presence of benzaldehyde, no oxidation without benzaldehyde
-
-
?
alpha-methylspermine + O2 + H2O
?
show the reaction diagram
-
oxidation in presence of benzaldehyde, no oxidation without benzaldehyde
-
-
?
alpha-methylspermine + O2 + H2O
spermidine + alpha-methylspermidine + ?
show the reaction diagram
-
-
-
-
?
bis-alpha,alpha'-methylspermine + O2 + H2O
alpha-methylspermidine + ?
show the reaction diagram
-
-
-
-
?
N,N'-bis-(3-benzylaminopropyl)butane-1,4-diamine + O2 + H2O
N1-(3-benzylaminopropyl)butane-1,4-diamine + H2O2 + ?
show the reaction diagram
-
-
main product
-
?
N,N'-bis-(3-benzylaminopropyl)butane-1,4-diamine + O2 + H2O
N1-(3-benzylaminopropyl)butane-1,4-diamine + N-(3-aminopropyl)-N'-(3-Benzylaminopropyl)butane-1,4-diamine + H2O2
show the reaction diagram
-
-
-
-
?
N,N'-bis-(3-ethylaminopropyl)butane-1,4-diamine + O2 + H2O
N1-(3-ethylaminopropyl)butane-1,4-diamine + H2O2 + ?
show the reaction diagram
-
minor N4-endo cleavage pathways resulting in formation of N1-ethylpropane-1,3-diamine
-
-
?
N-(3-benzylaminopropyl)-N'-(3-ethylaminopropyl)butane-1,4-diamine + O2 + H2O
N1-(3-ethylaminopropyl)butane-1,4-diamine + H2O2 + ?
show the reaction diagram
-
-
-
-
?
N-[(2R)-4-[(4-aminobutyl)amino]butan-2-yl]pyridine-4-carboxamide + O2 + H2O
putrescine + (3R)-3-[(pyridin-4-yl)amino]butanal + H2O2
show the reaction diagram
-
-
-
?
N-[(2S)-4-[(4-aminobutyl)amino]butan-2-yl]pyridine-4-carboxamide + O2 + H2O
putrescine + (3S)-3-[(pyridin-4-yl)amino]butanal + H2O2
show the reaction diagram
-
-
-
?
N1,N11-diacetylnorspermine + O2 + H2O
?
show the reaction diagram
-
-
-
-
?
N1,N11-didansylnorspermine + O2 + H2O
? + H2O2
show the reaction diagram
-
-
-
-
?
N1,N11-diethylnorspermine + O2 + H2O
?
show the reaction diagram
-
-
-
?
N1,N12-diacetylspermine + O2 + H2O
?
show the reaction diagram
N1,N12-diacetylspermine + O2 + H2O
N1-acetylspermidine + 3-acetamidopropanal + H2O2
show the reaction diagram
N1,N12-diethylspermine + O2 + H2O
?
show the reaction diagram
-
-
-
?
N1,N14-diethylhomospermine + O2 + H2O
?
show the reaction diagram
-
-
-
?
N1-(3-benzylaminopropyl)butane-1,4-diamine + O2 + H2O
spermidine + H2O2 + benzylalcohol
show the reaction diagram
-
-
-
-
?
N1-acetyl-2-methylspermidine + O2 + H2O
putrescine + N-(2-methyl-3-oxopropyl)acetamide + H2O2
show the reaction diagram
-
-
-
?
N1-acetyl-8-methylspermidine + O2 + H2O
pentane-1,4-diamine + 3-acetamidopropanal + H2O2
show the reaction diagram
-
-
-
?
N1-acetylspermidine + O2 + H2O
?
show the reaction diagram
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetamidopropanal
show the reaction diagram
-
-
-
?
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetamidopropanal + 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-benzoyl-(R)-alpha-methylspermidine + O2 + H2O
putrescine + N-[(2R)-4-oxobutan-2-yl]benzamide + H2O2
show the reaction diagram
-
-
-
?
N1-benzoyl-(S)-alpha-methylspermidine + O2 + H2O
putrescine + N-[(2S)-4-oxobutan-2-yl]benzamide + H2O2
show the reaction diagram
-
-
-
?
N1-benzyl-propane-1,3-diamine + O2 + H2O
propane-1,3-diamine + H2O2 + benzylalcohol
show the reaction diagram
-
-
-
-
?
N1-cyclopropylmethyl-N11-ethylnorspermine + O2 + H2O
?
show the reaction diagram
-
-
-
-
?
N1-ethyl-N11-(cycloheptyl)methyl-4,8-diazaundecane-1,11-diamine + O2 + H2O
?
show the reaction diagram
-
-
-
?
N1-ethyl-N11-(cyclopropyl)methyl-4,8-diazaundecane + O2 + H2O
?
show the reaction diagram
-
-
-
?
N1-phenyl-(R)-alpha-methylspermidine + O2 + H2O
putrescine + (3R)-3-anilinobutanal + H2O2
show the reaction diagram
-
-
-
?
N1-phenyl-(S)-alpha-methylspermidine + O2 + H2O
putrescine + (3S)-3-anilinobutanal + H2O2
show the reaction diagram
-
-
-
?
spermidine + O2 + H2O
?
show the reaction diagram
spermine + O2 + H2O
?
show the reaction diagram
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
show the reaction diagram
least favoured substrate
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N,N'-bis-(3-benzylaminopropyl)butane-1,4-diamine + O2 + H2O
N1-(3-benzylaminopropyl)butane-1,4-diamine + N-(3-aminopropyl)-N'-(3-Benzylaminopropyl)butane-1,4-diamine + H2O2
show the reaction diagram
-
-
-
-
?
N1,N12-diacetylspermine + O2 + H2O
?
show the reaction diagram
-
-
-
-
?
N1,N12-diacetylspermine + O2 + H2O
N1-acetylspermidine + 3-acetamidopropanal + H2O2
show the reaction diagram
-
-
-
-
?
N1-acetylspermidine + O2 + H2O
?
show the reaction diagram
-
-
-
-
?
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetamidopropanal + 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
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
MDL72527
-
-
N,N-di-2,3-butadienyl-1,4-butanediamine
-
i.e. MDL 72527, strong inhibition
N,N'-butanedienyl butanediamine
-
i.e. MDL 72527 or CPC-200, a small molecule specific inhibitor of polyamine oxidase, effectively blocks androgen-induced reactive oxygen species production in human prostate cancer cells, as well as significantly delays prostate cancer progression and death in animals developing spontaneous prostate cancer
N-(3-aminopropyl)-N-2-propenyl-1,4-butanediamine
-
moderate inhibition
N-(3-aminopropyl)-N-2,3-butadienyl-1,4-butanediamine
-
strong inhibition
N-[3-(2,3-butadienylamino)propyl]-1,4-butanediamine
-
strong inhibition
N-[3-(2-propenylamino) propyl]-1,4-butanediamine
-
moderate inhibition
N1,N4-bis(2,3-butadienyl)-1,4-butanediamine
i.e. MDL 72,527
SL-11144
0.01 mM, 80% inhibition
SL-11150
0.01 mM, complete inhibition
SL-11158
0.01 mM, complete inhibition
additional information
-
no inhibitory activity: N-(3-aminopropyl)-N-2-propynyl-1,4-butanediamine and N-[3-(2-propynylamino)propyl]-1,4-butanediamine
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.016
alpha-methylspermidine
-
addition of 5 mM benzyldehyde, hPAO
0.011 - 0.019
alpha-methylspermine
0.0036
N-[(2R)-4-[(4-aminobutyl)amino]butan-2-yl]pyridine-4-carboxamide
pH 9, 25Ā°C
-
0.0008
N-[(2S)-4-[(4-aminobutyl)amino]butan-2-yl]pyridine-4-carboxamide
pH 9, 25Ā°C
-
0.0027
N1,N11-diacetylnorspermine
-
-
0.0021 - 0.028
N1-acetylspermidine
0.00085 - 0.0011
N1-acetylspermine
0.0012
N1-benzoyl-(R)-alpha-methylspermidine
pH 9, 25Ā°C
-
0.0002
N1-benzoyl-(S)-alpha-methylspermidine
pH 9, 25Ā°C
-
0.0016 - 0.002
N1-phenyl-(R)-alpha-methylspermidine
-
0.015
spermidine
-
addition of 5 mM benzyldehyde, hPAO
0.0093 - 0.047
spermine
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0052
N-[(2R)-4-[(4-aminobutyl)amino]butan-2-yl]pyridine-4-carboxamide
pH 9, 25Ā°C
-
0.00001
N-[(2S)-4-[(4-aminobutyl)amino]butan-2-yl]pyridine-4-carboxamide
pH 9, 25Ā°C
-
19
N1,N11-diacetylnorspermine
-
-
2.7 - 15
N1-acetylspermidine
17 - 31.7
N1-acetylspermine
4.6
N1-benzoyl-(R)-alpha-methylspermidine
pH 9, 25Ā°C
-
0.03
N1-benzoyl-(S)-alpha-methylspermidine
pH 9, 25Ā°C
-
0.00003 - 0.00014
N1-phenyl-(R)-alpha-methylspermidine
-
0.0004
spermine
-
-
additional information
additional information
-
kinetic characteristics of the degradation of spermidine, racemic, and different isomers of alpha-methylspermidine by human polyamine oxidase in the presence of different aldehydes. Kinetic values of spermine and different diastereomers of bis-alpha,alpha'-methylspermine for human polyamine oxidase in the presence of different aldehydes
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1400
N-[(2R)-4-[(4-aminobutyl)amino]butan-2-yl]pyridine-4-carboxamide
pH 9, 25Ā°C
-
18
N-[(2S)-4-[(4-aminobutyl)amino]butan-2-yl]pyridine-4-carboxamide
pH 9, 25Ā°C
-
330
N1-acetylspermidine
pH 9, 25Ā°C
3800
N1-benzoyl-(R)-alpha-methylspermidine
pH 9, 25Ā°C
-
150
N1-benzoyl-(S)-alpha-methylspermidine
pH 9, 25Ā°C
-
18 - 71
N1-phenyl-(R)-alpha-methylspermidine
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
assay at
9
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
reduced level of PAO in neoplastic tissue
Manually annotated by BRENDA team
-
androgen-treated and untreated prostate adenocarcinoma cells
Manually annotated by BRENDA team
reduced level of PAO in neoplastic tissue
Manually annotated by BRENDA team
reduced level of PAO in neoplastic tissue
Manually annotated by BRENDA team
additional information
-
APAO is constitutively expressed in various tissues
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
-
polyamine oxidation is a major pathway for reactive oxygen species production in prostate, inhibiting this pathway successfully delays prostate cancer progression
additional information
-
method development for determination of polyamines and acetylpolyamines in the polyamine catabolic pathway creating heptafluorobutyryl derivatives of the compounds for TOF and hybrid tandem mass spectrometry, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PAOX_HUMAN
511
0
55513
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
x * 55000, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 55000, calculated from sequence
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA is transiently transfected into HEK-293 cells
expressed in HEK 293 cells
-
expression in HEK-293 cells
-
stable expression of hPAO-1 in A549 cell line
transfection of A-549 cell
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
high expression of APAO in A549 cells inhibits accumulation of antitumor polyamine analogue, N1-cyclopropylmethyl-N11-ethylnorspermine, decreases their sensitivity to the toxicity of N1-cyclopropylmethyl-N11-ethylnorspermine and prevents N1-cyclopropylmethyl-N11-ethylnorspermine-induced apoptosis
pharmacology
-
N,N'-butanedienyl butanediamine, i.e. MDL 72527 or CPC-200, a small molecule specific inhibitor of polyamine oxidase, effectively blocks androgen-induced reactive oxygen species production in human prostate cancer cells, as well as significantly delays prostate cancer progression and death in animals developing spontaneous prostate cancer
synthesis
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vujcic, S.; Liang, P.; Diegelman, P.; Kramer, D.L.; Porter, C.W.
Genomic identification and biochemical characterization of the mammalian polyamine oxidase involved in polyamine back-conversion
Biochem. J.
370
19-28
2003
Homo sapiens (Q6QHF9), Homo sapiens
Manually annotated by BRENDA team
Wang, Y.; Hacker, A.; Murray-Stewart, T.; Frydman, B.; Valasinas, A.; Fraser, A.V.; Woster, P.M.; Casero Jr, R.A.
Properties of recombinant human N1-acetylpolyamine oxidase (hPAO): potential role in determining drug sensitivity
Cancer Chemother. Pharmacol.
56
83-90
2005
Homo sapiens (Q6QHF9), Homo sapiens
Manually annotated by BRENDA team
Jaervinen, A.; Keinaenen, T.A.; Grigorenko, N.A.; Khomutov, A.R.; Uimari, A.; Vepsaelaeinen, J.; Naervaenen, A.; Alhonen, L.; Jaenne, J.
Guide molecule-driven stereospecific degradation of alpha-methylpolyamines by polyamine oxidase
J. Biol. Chem.
281
4589-4595
2006
Homo sapiens
Manually annotated by BRENDA team
Järvinen, A.; Grigorenko, N.; Khomutov, A.R.; Hyvönen, M.T.; Uimari, A.; Vepsäläinen, J.; Sinervirta, R.; Keinänen, T.A.; Vujcic, S.; Alhonen, L.; Porter, C.W.; Jänne, J.
Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural polyamines.
J. Biol. Chem.
280
6595-6601
2005
Homo sapiens
Manually annotated by BRENDA team
Basu, H.S.; Thompson, T.A.; Church, D.R.; Clower, C.C.; Mehraein-Ghomi, F.; Amlong, C.A.; Martin, C.T.; Woster, P.M.; Lindstrom, M.J.; Wilding, G.
A small molecule polyamine oxidase inhibitor blocks androgen-induced oxidative stress and delays prostate cancer progression in the transgenic adenocarcinoma of the mouse prostate model
Cancer Res.
69
7689-7695
2009
Homo sapiens
Manually annotated by BRENDA team
Han, Y.; Ren, Y.S.; Cao, C.Y.; Ren, D.M.; Zhou, Y.Q.; Wang, Y.L.
Highly expressed N1-acetylpolyamine oxidase detoxifies polyamine analogue N1-cyclopropylmethyl-N11-ethylnorspermine in human lung cancer cell line A549
Chin. Med. Sci.
122
1394-1399
2009
Homo sapiens
Manually annotated by BRENDA team
Häkkinen, M.; Hyönen, M.; Auriola, S.; Casero Jr., R.; Vepsäläinen, J.; Khomutov, A.; Alhonen, L.; Keinänen, T.
Metabolism of N-alkylated spermine analogues by polyamine and spermine oxidases
Amino Acids
38
369-381
2010
Homo sapiens
Manually annotated by BRENDA team
Moriya, S.; Iwasaki, K.; Samejima, K.; Takao, K.; Kohda, K.; Hiramatsu, K.; Kawakita, M.
A mass spectrometric method to determine activities of enzymes involved in polyamine catabolism
Anal. Chim. Acta
748
45-52
2012
Homo sapiens
Manually annotated by BRENDA team
Moriya, S.S.; Miura, T.; Takao, K.; Sugita, Y.; Samejima, K.; Hiramatsu, K.; Kawakita, M.
Development of irreversible inactivators of spermine oxidase and N1-acetylpolyamine oxidase
Biol. Pharm. Bull.
37
475-480
2014
Homo sapiens
Manually annotated by BRENDA team
Keinaenen, T.A.; Grigorenko, N.; Khomutov, A.R.; Huang, Q.; Uimari, A.; Alhonen, L.; Hyvoenen, M.T.; Vepsaelaeinen, J.
Controlling the regioselectivity and stereospecificity of FAD-dependent polyamine oxidases with the use of amine-attached guide molecules as conformational modulators
Biosci. Rep.
38
BSR20180527
2018
Homo sapiens (Q6QHF9), Homo sapiens
Manually annotated by BRENDA team
Khomutov, M.; Hyvonen, M.; Simonian, A.; Weisell, J.; Vepsalainen, J.; Alhonen, L.; Kochetkov, S.; Keinanen, T.; Khomutov, A.
Acetylated derivatives of C-methylated analogues of spermidine synthesis and interaction with N1-acetylpolyamine oxidase
Mendeleev Commun.
28
479-481
2018
Homo sapiens (Q6QHF9)
-
Manually annotated by BRENDA team