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Information on EC 1.5.3.14 - polyamine oxidase (propane-1,3-diamine-forming) and Organism(s) Zea mays and UniProt Accession O64411
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1.5.3.14 polyamine oxidase (propane-1,3-diamine-forming)IUBMB Comments
As the products of the reaction cannot be converted directly to other polyamines, this class of polyamine oxidases is considered to be involved in the terminal catabolism of polyamines . This enzyme less efficiently catalyses the oxidation of N1-acetylspermine and spermine. A flavoprotein (FAD). Differs in specificity from EC 1.5.3.13 (N1-acetylpolyamine oxidase), 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
- 1.5.3.14
- spermine
- oxidases
-
back-conversion
- apoplastic
- thermospermine
- putrescine
- tabacum
-
fad-dependent
-
tunnel
- barley
- mesocotyl
- 1,3-diaminopropane
-
tetraamines
- aminoaldehyde
- 1,8-diaminooctane
-
h2o2-producing
-
u-shaped
- guazatine
The taxonomic range for the selected organisms is: Zea mays
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
zmpao, ospao7, maize polyamine oxidase, maize pao, flavin-containing polyamine oxidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
spermidine:oxygen oxidoreductase (propane-1,3-diamine-forming)
As the products of the reaction cannot be converted directly to other polyamines, this class of polyamine oxidases is considered to be involved in the terminal catabolism of polyamines [1]. This enzyme less efficiently catalyses the oxidation of N1-acetylspermine and spermine. A flavoprotein (FAD). Differs in specificity from EC 1.5.3.13 (N1-acetylpolyamine oxidase), 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)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
spermine + O2 + H2O
1-(3-aminopropyl)-4-aminobutanal + propane-1,3-diamine + H2O2
-
-
-
?
spermine + O2 + H2O
propane-1,3-diamine + N-(3-aminopropyl)-4-aminobutanal + H2O2
-
-
-
-
?
spermidine + O2 + H2O
propane-1,3-diamine + 4-aminobutanal + H2O2
enzyme activity is measured spectrophotometrically by following the formation of a pink adduct resulting from the H2O2-dependent oxidation of 4-aminoantipyrine catalyzed by horseradish peroxidase and the subsequent condensation of oxidized 4-aminoantipyrine with 3,5-dichloro-2-hydroxybenzenesulfonic acid
-
-
?
spermidine + O2 + H2O
1,3-diaminopropane + 4-aminobutanal + H2O2
-
preferred substrate
-
-
?
spermidine + O2 + H2O
propane-1,3-diamine + 4-aminobutanal + H2O2
-
-
-
-
?
spermidine + O2 + H2O
propane-1,3-diamine + 4-aminobutanal + H2O2
-
best substrate
-
-
?
additional information
?
-
no activity with: acetylputrescine, acetylcadaverine
-
-
?
additional information
?
-
-
analysis of polymaine content in leaves under different salt conditions, overview
-
-
?
additional information
?
-
-
effects of increased H2O2 production on the expression of enzymes involved in the antioxidant machinery, overview
-
-
?
additional information
?
-
effects of increased H2O2 production on the expression of enzymes involved in the antioxidant machinery, overview
-
-
?
additional information
?
-
-
involvement of polyamine oxidase in abscisic acid-induced cytosolic antioxidant defense in leaves of maize. MPAO contributes to abscisic acid-induced cytosolic antioxidant defense through H2O2, a spermidine catabolic product, overview
-
-
?
additional information
?
-
-
the enzyme from Zea mays oxidizes the carbon on the endo-side of the N5-nitrogen of spermidine and spermine
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
spermine + O2 + H2O
propane-1,3-diamine + N-(3-aminopropyl)-4-aminobutanal + H2O2
-
-
-
-
?
spermidine + O2 + H2O
propane-1,3-diamine + 4-aminobutanal + H2O2
-
-
-
-
?
additional information
?
-
-
analysis of polymaine content in leaves under different salt conditions, overview
-
-
?
additional information
?
-
-
effects of increased H2O2 production on the expression of enzymes involved in the antioxidant machinery, overview
-
-
?
additional information
?
-
effects of increased H2O2 production on the expression of enzymes involved in the antioxidant machinery, overview
-
-
?
additional information
?
-
-
involvement of polyamine oxidase in abscisic acid-induced cytosolic antioxidant defense in leaves of maize. MPAO contributes to abscisic acid-induced cytosolic antioxidant defense through H2O2, a spermidine catabolic product, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
oxidized FAD is the prominent form during steady-state turnover, consistent with the reductive half-reaction being rate-limiting
FAD
the FAD prosthetic group is non-covalently bound to the protein and is deeply embedded within the structure. All FAD atoms are solvent-inaccessible, with the exception of the flavin C5a, N5 and C4a atoms that line the active centre
FAD
-
dependent on. Residue K300 is hydrogen-bound to the N5 atom of FAD via a H2O molecule (HOH309), the only solvent molecule present inside the catalytic site in the enzyme inhibitor complexes. In turn, K300 is the only active-site residue whose conformation changes upon FAD reduction, possibly allowing for a reorientation of the HOH309 molecule. The water molecule might thus function as a hydrogen-bond acceptor with the protonated N5 atom of reduced FAD
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(N1-5-aminopentyl)-N3-(cyclohexylethyl)-N1,N2,N3-tris(tert-butoxycarbonyl)guanidine
-
1-(4-aminobutyl)-3-but-3-en-1-ylguanidine
competitive inhibition of spermidine oxidation
1-(4-aminobutyl)-3-but-3-yn-1-ylguanidine
competitive inhibition of spermidine oxidation
1-(5-aminopentyl)-3-(4-methylpent-3-en-1-yl)guanidine
competitive inhibition of spermidine oxidation
1-(6-aminohexyl)-3-(4-methylpent-3-en-1-yl)guanidine
competitive inhibition of spermidine oxidation
1-(guanidino)-17-(N1-(gamma,gamma-dimethylallyl)guanidino)-9-azaheptadecane tris(trifluoroacetate)
-
1-[7-[(9-carbamimidamidononyl)amino]heptyl]-3-(2-cyclopropylethyl)guanidine
-
1-[7-[(9-carbamimidamidononyl)amino]heptyl]-3-(3-methylbut-3-en-1-yl)guanidine
-
3-(4-methylpent-3-en-1-yl)-1-[9-([7-[(4-methylpent-3-en-1-yl)carbamimidamido]heptyl]amino)nonyl]guanidine
-
3-[(2E)-but-2-en-1-yl]-1-[7-[(9-carbamimidamidononyl)amino]heptyl]guanidine
-
N1,N2-bis(tert-butoxycarbonyl)-N1-(gamma,gamma-dimethylallyl)-S-methylisothiourea
-
N1,N2-bis(tert-butoxycarbonyl)-N1-(gamma,gamma-methylallyl)-S-methylisothiourea
-
N1-(3-methoxybenzyl)-N3-(5-aminopentyl)-N2,N3,N4-tris(tertbutoxycarbonyl)guanidine
-
N1-benzylamine-N3-(gamma,gamma-dimethyallyl)-N2,N3,N4-tris(tert-butoxycarbonyl)guanidine
-
N1-benzylamine-N3-(gamma,gamma-dimethylallyl)guanidine bis-(trifluoroacetate)
-
N1-[(30-aminopropyl)-3-aminopropyl]-N3-(gamma,gamma-dimethylallyl)-N2,N3-bis(tert-butoxycarbonyl)guanidine
-
tert-butyl (2E)-but-2-en-1-yl[(E)-[(tert-butoxycarbonyl)imino](methylsulfanyl)methyl]carbamate
-
tert-butyl (4-[(tert-butoxycarbonyl)[(E)-[(tert-butoxycarbonyl)imino](methylsulfanyl)methyl]amino]butyl)methylcarbamate
-
tert-butyl (6-aminohexyl)[(tert-butoxycarbonyl)(cyclopropylmethyl)carbamimidoyl]carbamate
-
tert-butyl (6-aminohexyl)[(tert-butoxycarbonyl)[(3E)-4-phenylbut-3-en-1-yl]carbamimidoyl]carbamate
-
tert-butyl benzyl[(E)-[(tert-butoxycarbonyl)imino](methylsulfanyl)methyl]carbamate
-
tert-butyl [(1E)-[(tert-butoxycarbonyl)(cyclopropylmethyl)amino](methylsulfanyl)methylidene]carbamate
-
tert-butyl [(E)-[(tert-butoxycarbonyl)imino](methylsulfanyl)methyl]prop-2-yn-1-ylcarbamate
-
tert-butyl [(E)-[(tert-butoxycarbonyl)imino](methylsulfanyl)methyl][(2E)-3-phenylprop-2-en-1-yl]carbamate
-
N-prenylagmatine
-
i.e. G3, a specific and selective ZmPAO inhibitor. G3 strongly inhibits lignin and suberin polyphenolic domain deposition along the wound periderm in maize mesocoty
1-(4-aminobutyl)-3-(4-fluorobenzyl)guanidine
competitive inhibition of spermidine oxidation
N,N'''-butane-1,4-diylbis[3-(3-methylbut-2-en-1-yl)guanidine]
competitive inhibition of spermidine oxidation
additional information
docking simulations carried out with the charged and uncharged forms of MPAO inhibitors indicate that the stereoelectronic properties of the MPAO active site are consistent with the binding of inhibitors in the protonated form, a feature which can shed light on the still obscure MPAO catalytic mechanism
-
additional information
-
docking simulations carried out with the charged and uncharged forms of MPAO inhibitors indicate that the stereoelectronic properties of the MPAO active site are consistent with the binding of inhibitors in the protonated form, a feature which can shed light on the still obscure MPAO catalytic mechanism
-
additional information
-
no inhibition by 1,3-diaminopropane (1 mM) and H2O2 (1 mM)
-
additional information
no inhibition by 1,3-diaminopropane (1 mM) and H2O2 (1 mM)
-
additional information
computational structure-function analysis of inhibitors, overview
-
additional information
-
computational structure-function analysis of inhibitors, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0007
1-(4-carbamimidamidobutyl)-3-(3-methylbut-2-en-1-yl)guanidine
pH 6.5, 25°C
0.00153
1-(5-aminopentyl)-3-[(2E)-3-phenylprop-2-en-1-yl]guanidine
pH 6.5, 25°C
0.000003
1-(guanidino)-17-(N1-(gamma,gamma-dimethylallyl)guanidino)-9-azaheptadecane tris(trifluoroacetate)
pH 6.5, 25°C
0.00121
1-[3-[(3-aminopropyl)amino]propyl]-3-(3-methylbut-2-en-1-yl)guanidine
pH 6.5, 25°C
0.00000008
1-[7-[(9-carbamimidamidononyl)amino]heptyl]-3-(2-cyclopropylethyl)guanidine
pH 6.5, 25°C
0.000001
1-[7-[(9-carbamimidamidononyl)amino]heptyl]-3-(2-phenylethyl)guanidine
pH 6.5, 25°C
0.0000005
1-[7-[(9-carbamimidamidononyl)amino]heptyl]-3-(3-methylbut-3-en-1-yl)guanidine
pH 6.5, 25°C
0.0000017
3-(4-methylpent-3-en-1-yl)-1-[9-([7-[(4-methylpent-3-en-1-yl)carbamimidamido]heptyl]amino)nonyl]guanidine
pH 6.5, 25°C
0.0000007
3-but-3-yn-1-yl-1-[7-[(9-carbamimidamidononyl)amino]heptyl]guanidine
pH 6.5, 25°C
0.0000011
3-[(2E)-but-2-en-1-yl]-1-[7-[(9-carbamimidamidononyl)amino]heptyl]guanidine
pH 6.5, 25°C
0.02
N-[[2-carboxy-5-(4-methoxyphenyl)thiophen-3-yl]carbamoyl]-L-tyrosine
N1-acetyl-3-aminopropyl-4-aminobutanal
0.018
N1-benzylamine-N3-(gamma,gamma-dimethylallyl)guanidine bis-(trifluoroacetate)
pH 6.5, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
the ZmPAO-K300M mutant is catalytically impaired with a 1400fold decrease in the rate of flavin reduction. Substrates are bound in an out-of-register mode and the HOH309 water molecule is absent in the enzyme-substrate complexes. K300 mutation brings about a 60 mV decrease in the FAD redox potential and a 30fold decrease in the FAD reoxidation rate, within a virtually unaltered geometry of the catalytic pocket
physiological function
additional information
-
active site structure of wild-type and mutant K300M enzymes, overview. The active site is formed by a catalytic tunnel in which the N5 atom of FAD lies in close proximity to the K300 side chain, the only active-site residue conserved in all PAOs. A water molecule, HOH309, is hydrogen-bound to the amino group of K300. The HOH309-K300 couple plays a major role in multiple steps of ZmPAO catalytic mechanism, such as correct substrate binding geometry as well as FAD reduction and reoxidation kinetics. Substrate binding mechanism and structure, and comparison to Saccharomyces cerevisiae Fms1, EC 1.5.3.17, overview. The differences include a planar conformation of the isoalloxazine ring in Fms1 versus a highly bent conformation in ZmPAO and important substitutions in the relevant topological positions of the active site, i.e. E170W, F171H, E62H, V196N, S87D, F318K, F403Y, V331F, T348L, Y169L and Y298L, numbering referring to ZmPAO. The substrate-binding site of Fms1 is more hydrophobic than that of ZmPAO
physiological function
-
involvement of ZmPA-mediated H2O2 production in wound-healing events
physiological function
-
polyamine oxidase activity contributes to sustain maize leaf elongation under saline stress providing a significant production of reactive oxygen species in the apoplast
physiological function
-
role of MPAO in abscisic acid-induced antioxidant defense in leaves of maize plants
physiological function
-
plant PAOs oxidize the carbon at the endo-side of the N4-nitrogen of Spd and Spm, producing 4-aminobutanal and N-(3-aminopropyl)-4-aminobutanal, respectively, in addition to 1,3-diaminopropane and H2O2, and are considered to be involved in terminal catabolism of polyamines, physiological role(s) of the polyamine catabolic pathways in plants, overview
physiological function
-
Nicotiana tabacum expressing PAO with reduced activity contained higher Ca2+ levels during salt stress, and show also reduced chlorophyll content index, leaf area and biomass, but taller phenotype compared to the wildtype plants during salt stress. Plants overexpressing PAO have more leaves with slightly greater size compared to the plants with reduced expression and higher antioxidant genes/enzyme activities. Accumulation of proline in the roots is evident at prolonged stress and correlates negatively with PAO deregulation as does the transcripts of genes mediating ethylene biosynthesis
physiological function
-
under drought stress, expression of polyamine oxidase genes PAO1, PAO2, PAO3, PAO4,PAO5, PAO6 and activity of enzymatic polyamine oxidation is increased in both relatively tolerant (Karoon) and sensitive (260) maize cultivars. The enhancement in PAO gene expression and enzyme activity is more prominent in Karoon cultivar compared to 260
physiological function
-
underexpression of PAO in Nicotiana tabacum correlates with increased thermotolerance of the photosynthetic machinery and improved biomass accumulation, accompanied by enhanced levels of the enzymatic and non-enzymatic antioxidants, whereas PAO overexpressors exhibit significant impairment of thermotolerance
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PAO1_MAIZE
500
0
56344
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
flavoprotein
glycoprotein
-
the wild-type enzyme's glycosylation site is at residue N77. Modelling of wild-type subunit C with a branched chain of five ordered sugars (two N-acetyl-D-glucosamine residues as well as a fucose and two mannose residues). The ZmPAO-K300M mutant appears to be less glycosylated than the wild-type enzyme
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallised by the hanging drop vapour-diffusion method, with the protein solution consisting of 5 mg enzyme/ml in 300 mM NaCl and 50 mM sodium phosphate buffer, pH 6.0. Crystal structure of polyamine oxidase is determined to a resolution of 1.9 A. The enzyme contains two domains, which define a remarkable 30 A long U-shaped catalytic tunnel at their interface. The structure of PAO in complex with the inhibitor MDL72527 reveals the residues forming the catalytic machinery and unusual enzyme-inhibitor CH...OH bonds. A ring of glutamate and aspartate residues surrounding one of the two tunnel openings contributes to the steering of the substrate towards the inside of the tunnel
purified recombinant mutant ZmPAO-K300M, hanging drop vapor diffusion method, mixing of 9.0 mg/ml protein in 50 mM sodium acetate, pH 5.5, with an equal volume of reservoir solution containing ammonium sulfate in a concentration range 2.22.8 m and 100 mm sodium acetate, pH 4.6, 20°C, two weeks, X-ray diffraction structure determination and analysis at 2.9 A resolution,mlecular displacement, modelling
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E170Q
mutation results in moderate change of enzyme activity and apparent Km-values
E62Q
mutation results in moderate change of enzyme activity and apparent Km-values
K300M
mutation results in a 1400fold decrease in the rate of flavin reduction and a 160fold decrease in the equilibrium dissociation constant for the K300M-spermidine complex, consistent with a major role for this residue in the mechanism of substrate oxidation
K300M
-
site-directed mutagenesis, catalyitically impaired active site mutant, that is less glycosylated than the wild-type enzyme. The mutant shows a 1400fold decrease in the rate of flavin reduction. Substrates are bound in an out-of-register mode and the HOH309 water molecule is absent in the enzymesubstrate complexes. K300 mutation brings about a 60 mV decrease in the FAD redox potential and a 30fold decrease in the FAD reoxidation rate, within a virtually unaltered geometry of the catalytic pocket
additional information
additional information
-
transgenic Mpao overexpressing tobacco plants show highly increased enzyme activity and 1,3-diaminopropane levels, also specific isoforms of the antioxidant machinery, i.e. peroxidase, superoxide dismutase and catalase, are induced in the transgenics but not in the wild-type, along with increase in activities of additional enzymes contributing to redox homeostasis. Nevertheless, further increase in the intracellular reactive oxygen species by exogenous H2O2, or addition of methylviologen or menadione to transgenic leaf discs, results in oxidative stress as evidenced by the lower quantum yield of PSII, the higher ion leakage, lipid peroxidation and induction of programmed cell death, overview
additional information
transgenic Mpao overexpressing tobacco plants show highly increased enzyme activity and 1,3-diaminopropane levels, also specific isoforms of the antioxidant machinery, i.e. peroxidase, superoxide dismutase and catalase, are induced in the transgenics but not in the wild-type, along with increase in activities of additional enzymes contributing to redox homeostasis. Nevertheless, further increase in the intracellular reactive oxygen species by exogenous H2O2, or addition of methylviologen or menadione to transgenic leaf discs, results in oxidative stress as evidenced by the lower quantum yield of PSII, the higher ion leakage, lipid peroxidation and induction of programmed cell death, overview
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Pichia pastoris strain X-33 by nickel affinity chromatography
-
recombinant His-tagged wild-type and mutant ZmPAO enzymes from Pichia pastoris strain X-33 bx nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
transgenic tobacco plants overexpressing polyamine oxidase from Zea mays exhibit high 1,3-diaminopropane content
overexpression of PAO in transgenic Nicotiana tabacum plants leading to dramatically increased expression levels of Mpao and high 1,3-diaminopropane content in the tobacco plant leaves, stems, and roots
recombinant expression of His-tagged wild-type and mutant ZmPAO enzymes in Pichia pastoris strain X-33
-
ZmPAO overexpression in tobacco cell wall greatly accelerates the phenomenon in wounded tobacco stem, that enzyme inhibition inhibits lignin and suberin polyphenolic domain deposition along the wound periderm in maize mesocoty
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
under drought stress, expression of polyamine oxidase genes PAO1, PAO2, PAO3, PAO4,PAO5, PAO6 and activity of enzymatic polyamine oxidation is increased in both relatively tolerant (Karoon) and sensitive (260) maize cultivars. The enhancement in PAO gene expression and enzyme activity is more prominent in Karoon cultivar compared to 260
medicine
-
exogenous spermine and PAO treatment decrease cell viability in a spermine dose- and time-dependent manner, particularly, the viability of the multidrug-resistant colon adenocarcinoma cells, LoVo DX, when compared with drug-sensitive ones. H2O2 derived from spermine is mainly responsible for the cytotoxicity. Treatment with PAO and spermine increases the apoptotic population of LoVo wild-type and multidrug-resistant LoVo cells. Treatment with PAO and spermine markedly reduces mitochondrial membrane potential in the multidrug-resistant LoVo cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Federico, R.; Ercolini, L.; Laurenzi, M.; Angelini, R.
Oxidation of acetylpolyamines by maize polyamine oxidase
Phytochemistry
43
339-341
1996
Zea mays (O64411)
-
Federico, R.; Leone, L.; Botta, M.; Binda, C.; Angelini, R.; Venturini, G.; Ascenzi, P.
Inhibition of pig liver and Zea mays L. polyamine oxidase: a comparative study
J. Enzyme Inhib.
16
147-155
2001
Zea mays (O64411)
Tavladoraki, P.; Schinina, M.E.; Cecconi, F.; Di Agostino, S.; Manera, F.; Rea, G.; Mariottini, P.; Federico, R.; Angelini, R.
Maize polyamine oxidase: primary structure from protein and cDNA sequencing
FEBS Lett.
426
62-66
1998
Zea mays (O64411), Zea mays
Cona, A.; Manetti, F.; Leone, R.; Corelli, F.; Tavladoraki, P.; Polticelli, F.; Botta, M.
Molecular basis for the binding of competitive inhibitors of maize polyamine oxidase
Biochemistry
43
3426-3435
2004
Zea mays (O64411), Zea mays
Polticelli, F.; Basran, J.; Faso, C.; Cona, A.; Minervini, G.; Angelini, R.; Federico, R.; Scrutton, N.S.; Tavladoraki, P.
Lys300 plays a major role in the catalytic mechanism of maize polyamine oxidase
Biochemistry
44
16108-16120
2005
Zea mays (O64411), Zea mays
Corelli, F.; Federico, R.; Cona, A.; Venturini, G.; Schenone, S.; Botta, M.
Solution and solid-phase synthesis of aminoalkylguanidines inhibiting polyamine oxidase and nitric oxide synthase
Med. Chem. Res.
11
309-321
2002
Zea mays (O64411)
-
Moschou, P.N.; Delis, I.D.; Paschalidis, K.A.; Roubelakis-Angelakis, K.A.
Transgenic tobacco plants overexpressing polyamine oxidase are not able to cope with oxidative burst generated by abiotic factors
Physiol. Plant.
133
140-156
2008
Zea mays, Zea mays (O64411)
Federico, R.; Cona, A.; Angelini. R.; Schinina, M.E.; Giartosio, A.
Characterization of maize polyamine oxidase
Phytochemistry
29
2411-2414
1990
Zea mays, Zea mays (O64411)
Binda, C.; Coda, A.; Angelini, R.; Federico, R.; Ascenzi, P.; Mattevi, A.
A 30-angstrom-long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase
Structure
7
265-276
1999
Zea mays (O64411)
Rodriguez, A.A.; Maiale, S.J.; Menendez, A.B.; Ruiz, O.A.
Polyamine oxidase activity contributes to sustain maize leaf elongation under saline stress
J. Exp. Bot.
60
4249-4262
2009
Zea mays
Xue, B.; Zhang, A.; Jiang, M.
Involvement of polyamine oxidase in abscisic acid-induced cytosolic antioxidant defense in leaves of maize
J. Integr. Plant Biol.
51
225-234
2009
Zea mays
Manetti, F.; Cona, A.; Angeli, L.; Mugnaini, C.; Raffi, F.; Capone, C.; Dreassi, E.; Zizzari, A.T.; Tisi, A.; Federico, R.; Botta, M.
Synthesis and biological evaluation of guanidino compounds endowed with subnanomolar affinity as competitive inhibitors of maize polyamine oxidase
J. Med. Chem.
52
4774-4785
2009
Zea mays (O64411), Zea mays
Tisi, A.; Angelini, R.; Cona, A.
Wound healing in plants: Cooperation of copper amine oxidase and flavin-containing polyamine oxidase
Plant Signal. Behav.
3
204-206
2008
Nicotiana tabacum, Zea mays
Fiorillo, A.; Federico, R.; Polticelli, F.; Boffi, A.; Mazzei, F.; Di Fusco, M.; Ilari, A.; Tavladoraki, P.
The structure of maize polyamine oxidase K300M mutant in complex with the natural substrates provides a snapshot of the catalytic mechanism of polyamine oxidation
FEBS J.
278
809-821
2011
Zea mays
Fincato, P.; Moschou, P.N.; Spedaletti, V.; Tavazza, R.; Angelini, R.; Federico, R.; Roubelakis-Angelakis, K.A.; Tavladoraki, P.
Functional diversity inside the Arabidopsis polyamine oxidase gene family
J. Exp. Bot.
62
1155-1168
2011
Zea mays
Ohkubo, S.; Mancinelli, R.; Miglietta, S.; Cona, A.; Angelini, R.; Canettieri, G.; Spandidos, D.A.; Gaudio, E.; Agostinelli, E.
Maize polyamine oxidase in the presence of spermine/spermidine induces the apoptosis of LoVo human colon adenocarcinoma cells
Int. J. Oncol.
54
2080-2094
2019
Zea mays
Pakdel, H.; Hassani, S.B.; Ghotbi-Ravandi, A.A.; Bernard, F.
Contrasting the expression pattern change of polyamine oxidase genes and photosynthetic efficiency of maize (Zea mays L.) genotypes under drought stress
J. Biosci.
45
73
2020
Zea mays
Gemes, K.; Mellidou, N.; Karamanoli, K.; Beris, D.; Park, K.Y.; Matsi, T.; Haralampidis, K.; Constantinidou, H.I.; Roubelakis-Angelakis, K.A.
Deregulation of apoplastic polyamine oxidase affects development and salt response of tobacco plants
J. Plant Physiol.
211
1-12
2017
Zea mays
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