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N1-acetylspermidine + O2 + H2O
1,3-diaminopropane + H2O2 + ?
at pH 7.0, 37°C, spermine and spermidine are the preferred substrates for OsPAO7, followed by N1-acetylspermine, N1-acetylspermidine, norspermine, thermospermine and norspermidine. At pH 6.5, 30°C, OsPAO7 shows a similar polyamine preference; it favors spermine and spermidine, followed by N1-acetylspermine, norspermine, thermospermine, N1-acetylspermidine and norspermidine
-
-
?
N1-acetylspermidine + O2 + H2O
?
-
-
-
?
N1-acetylspermine + O2 + H2O
1,3-diaminopropane + H2O2 + ?
N8-acetylspermine + O2 + H2O
1,3-diaminopropane + H2O2 + ?
-
-
-
?
norspermidine + O2 + H2O
1,3-diaminopropane + H2O2 + ?
at pH 7.0, 37°C, spermine and spermidine are the preferred substrates for OsPAO7, followed by N1-acetylspermine, N1-acetylspermidine, norspermine, thermospermine and norspermidine. At pH 6.5, 30°C, OsPAO7 shows a similar polyamine preference; it favors spermine and spermidine, followed by N1-acetylspermine, norspermine, thermospermine, N1-acetylspermidine and norspermidine
-
-
?
norspermine + O2 + H2O
?
at pH 7.0, 37°C, spermine and spermidine are the preferred substrates for OsPAO7, followed by N1-acetylspermine, N1-acetylspermidine, norspermine, thermospermine and norspermidine. At pH 6.5, 30°C, OsPAO7 shows a similar polyamine preference; it favors spermine and spermidine, followed by N1-acetylspermine, norspermine, thermospermine, N1-acetylspermidine and norspermidine
-
-
?
spermidine + O2 + H2O
1,3-diaminopropane + 4-aminobutanal + H2O2
spermidine + O2 + H2O
1,3-diaminopropane + H2O2 + ?
-
-
-
?
spermidine + O2 + H2O
4-aminobutanal + propane-1,3-diamine + H2O2
at pH 7.0, 37°C, spermine and spermidine are the preferred substrates for OsPAO7, followed by N1-acetylspermine, N1-acetylspermidine, norspermine, thermospermine and norspermidine. At pH 6.5, 30°C, OsPAO7 shows a similar polyamine preference; it favors spermine and spermidine, followed by N1-acetylspermine, norspermine, thermospermine, N1-acetylspermidine and norspermidine
-
-
?
spermidine + O2 + H2O
propane-1,3-diamine + 4-aminobutanal + H2O2
spermine + O2 + H2O
1,3-diaminopropane + 1-(3-aminopropylidene)pyrrolidin-1-ium + H2O2
spermine + O2 + H2O
1,3-diaminopropane + H2O2 + ?
-
-
-
?
spermine + O2 + H2O
1-(3-aminopropyl)-4-aminobutanal + propane-1,3-diamine + H2O2
-
-
-
?
spermine + O2 + H2O
N-(3-aminopropyl)-4-aminobutanal + 1,3-diaminopropane + H2O2
at pH 7.0, 37°C, spermine and spermidine are the preferred substrates for OsPAO7, followed by N1-acetylspermine, N1-acetylspermidine, norspermine, thermospermine and norspermidine. At pH 6.5, 30°C, OsPAO7 shows a similar polyamine preference; it favors spermine and spermidine, followed by N1-acetylspermine, norspermine, thermospermine, N1-acetylspermidine and norspermidine
-
-
?
spermine + O2 + H2O
propane-1,3-diamine + N-(3-aminopropyl)-4-aminobutanal + H2O2
-
-
-
-
?
spermine + O2 + H2O
spermidine + propane-1,3-diamine + H2O2
-
-
-
-
?
thermospermine + O2 + H2O
1,3-diaminopropane + H2O2 + ?
at pH 7.0, 37°C, spermine and spermidine are the preferred substrates for OsPAO7, followed by N1-acetylspermine, N1-acetylspermidine, norspermine, thermospermine and norspermidine. At pH 6.5, 30°C, OsPAO7 shows a similar polyamine preference; it favors spermine and spermidine, followed by N1-acetylspermine, norspermine, thermospermine, N1-acetylspermidine and norspermidine
-
-
?
additional information
?
-
N1-acetylspermine + O2 + H2O
1,3-diaminopropane + H2O2 + ?
at pH 7.0, 37°C, spermine and spermidine are the preferred substrates for OsPAO7, followed by N1-acetylspermine, N1-acetylspermidine, norspermine, thermospermine and norspermidine. At pH 6.5, 30°C, OsPAO7 shows a similar polyamine preference; it favors spermine and spermidine, followed by N1-acetylspermine, norspermine, thermospermine, N1-acetylspermidine and norspermidine
-
-
?
N1-acetylspermine + O2 + H2O
1,3-diaminopropane + H2O2 + ?
-
-
-
?
spermidine + O2 + H2O
1,3-diaminopropane + 4-aminobutanal + H2O2
-
-
-
-
?
spermidine + O2 + H2O
1,3-diaminopropane + 4-aminobutanal + H2O2
-
preferred substrate
-
-
?
spermidine + O2 + H2O
1,3-diaminopropane + 4-aminobutanal + H2O2
-
-
-
-
?
spermidine + O2 + H2O
1,3-diaminopropane + 4-aminobutanal + H2O2
-
-
-
-
?
spermidine + O2 + H2O
1,3-diaminopropane + 4-aminobutanal + H2O2
-
preferred substrate
-
-
?
spermidine + O2 + H2O
?
-
-
-
?
spermidine + O2 + H2O
?
-
-
-
-
?
spermidine + O2 + H2O
?
-
-
-
?
spermidine + O2 + H2O
propane-1,3-diamine + 4-aminobutanal + H2O2
-
-
-
?
spermidine + O2 + H2O
propane-1,3-diamine + 4-aminobutanal + H2O2
-
-
-
-
?
spermidine + O2 + H2O
propane-1,3-diamine + 4-aminobutanal + H2O2
-
-
-
?
spermidine + O2 + H2O
propane-1,3-diamine + 4-aminobutanal + H2O2
-
best substrate
-
-
?
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
-
-
?
spermine + O2 + H2O
1,3-diaminopropane + 1-(3-aminopropylidene)pyrrolidin-1-ium + H2O2
-
-
-
-
?
spermine + O2 + H2O
1,3-diaminopropane + 1-(3-aminopropylidene)pyrrolidin-1-ium + H2O2
-
-
-
-
?
spermine + O2 + H2O
?
-
-
-
?
spermine + O2 + H2O
?
-
-
-
?
additional information
?
-
-
H2O2 is the co-substrate for the peroxidase-driven reactions during cell-wall maturation and a key signalling molecule in defence mechanisms
-
-
?
additional information
?
-
no activity with the diamines putrescine and cadaverine
-
-
?
additional information
?
-
-
no activity with the diamines putrescine and cadaverine
-
-
?
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
-
-
?
additional information
?
-
-
the aminoaldehydes 4-aminobutanal and N-(3-aminopropyl)-4-aminobutanal are produced during ZmPAO reaction with spermidine and spermine, respectively
-
-
?
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spermidine + O2 + H2O
1,3-diaminopropane + 4-aminobutanal + H2O2
spermidine + O2 + H2O
propane-1,3-diamine + 4-aminobutanal + H2O2
spermine + O2 + H2O
1,3-diaminopropane + 1-(3-aminopropylidene)pyrrolidin-1-ium + H2O2
spermine + O2 + H2O
propane-1,3-diamine + N-(3-aminopropyl)-4-aminobutanal + H2O2
-
-
-
-
?
additional information
?
-
spermidine + O2 + H2O
1,3-diaminopropane + 4-aminobutanal + H2O2
-
-
-
-
?
spermidine + O2 + H2O
1,3-diaminopropane + 4-aminobutanal + H2O2
-
-
-
-
?
spermidine + O2 + H2O
1,3-diaminopropane + 4-aminobutanal + H2O2
-
-
-
-
?
spermidine + O2 + H2O
propane-1,3-diamine + 4-aminobutanal + H2O2
-
-
-
?
spermidine + O2 + H2O
propane-1,3-diamine + 4-aminobutanal + H2O2
-
-
-
-
?
spermidine + O2 + H2O
propane-1,3-diamine + 4-aminobutanal + H2O2
-
-
-
?
spermine + O2 + H2O
1,3-diaminopropane + 1-(3-aminopropylidene)pyrrolidin-1-ium + H2O2
-
-
-
-
?
spermine + O2 + H2O
1,3-diaminopropane + 1-(3-aminopropylidene)pyrrolidin-1-ium + H2O2
-
-
-
-
?
additional information
?
-
-
H2O2 is the co-substrate for the peroxidase-driven reactions during cell-wall maturation and a key signalling molecule in defence mechanisms
-
-
?
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
-
-
?
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(N1-5-aminopentyl)-N3-(cyclohexylethyl)-N1,N2,N3-tris(tert-butoxycarbonyl)guanidine
-
1,19-bis(ethylamino)-5,10,15-triazanonadecane
-
i.,e. SL-11061, 68% inhibition at 0.5 mM
1-(4-aminobutyl)-3-(4-fluorobenzyl)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-(4-aminobutyl)-3-prop-2-en-1-ylguanidine
-
1-(4-aminobutyl)-3-prop-2-yn-1-ylguanidine
-
1-(4-carbamimidamidobutyl)-3-(3-methylbut-2-en-1-yl)guanidine
-
1-(5-aminopentyl)-3-(2-cyclohexylethyl)guanidine
-
1-(5-aminopentyl)-3-(2-cyclopropylethyl)guanidine
-
1-(5-aminopentyl)-3-(3-methoxybenzyl)guanidine
-
1-(5-aminopentyl)-3-(3-methylbut-2-en-1-yl)guanidine
-
1-(5-aminopentyl)-3-(4-methylpent-3-en-1-yl)guanidine
competitive inhibition of spermidine oxidation
1-(5-aminopentyl)-3-[(2E)-3-phenylprop-2-en-1-yl]guanidine
-
1-(6-aminohexyl)-3-(3-methylbut-2-en-1-yl)guanidine
-
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-[3-[(3-aminopropyl)amino]propyl]-3-(3-methylbut-2-en-1-yl)guanidine
-
1-[7-[(9-carbamimidamidononyl)amino]heptyl]-3-(2-cyclopropylethyl)guanidine
-
1-[7-[(9-carbamimidamidononyl)amino]heptyl]-3-(2-phenylethyl)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-but-3-yn-1-yl-1-[7-[(9-carbamimidamidononyl)amino]heptyl]guanidine
-
3-[(2E)-but-2-en-1-yl]-1-[7-[(9-carbamimidamidononyl)amino]heptyl]guanidine
-
DELTA1-pyrroline
competitive
diazabicyclononane
competitive
diphenylene iodonium
-
slight inhibition of PAO
N,N'''-butane-1,4-diylbis[3-(3-methylbut-2-en-1-yl)guanidine]
N,N'-bis(2,3-butadienyl)-1,4-butane-diamine
i.e. MDL72527
N,N'-diaminoguanidine
-
about 25% inmhibition at 0.5 mM
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
N1,N2-bis(tert-butoxycarbonyl)-N1-(cyclohexylethyl)-S-methylisothiourea
-
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-acetyl-3-aminopropyl-4-aminobutanal
competitive
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
-
SL-11061
-
i.e. 1,19-bis-(ethylamine)-5,10,15 triazanonadecane
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
-
1,8-diaminooctane
-
1-(4-aminobutyl)-3-(4-fluorobenzyl)guanidine
-
1-(4-aminobutyl)-3-(4-fluorobenzyl)guanidine
competitive inhibition of spermidine oxidation
agmatine
-
agmatine
competitive inhibition of spermidine oxidation
guazatine
-
75% inhibition at 0.5 mM
N,N'''-butane-1,4-diylbis[3-(3-methylbut-2-en-1-yl)guanidine]
-
N,N'''-butane-1,4-diylbis[3-(3-methylbut-2-en-1-yl)guanidine]
competitive inhibition of spermidine oxidation
N1-acetylspermine
non-competitive
N1-acetylspermine
poor competitive inhibitor
additional information
not diaminopropane, H2O2 or in combination
-
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
-
no inhibition by 1,3-diaminopropane
-
additional information
computational structure-function analysis of inhibitors, overview
-
additional information
-
computational structure-function analysis of inhibitors, overview
-
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0.0006
1,10-Diaminodecane
pH 6.0, 25°C
0.00017
1,12-diaminododecane
pH 6.0, 25°C
0.1
1,3-diaminopropane
pH 6.0, 25°C
0.13
1,4-diaminobutane
pH 6.0, 25°C
0.038
1,5-Diaminopentane
pH 6.0, 25°C
0.003
1,6-diaminohexane
pH 6.0, 25°C
0.0004
1,7-Diaminoheptane
pH 6.0, 25°C
0.0012
1,9-diaminononane
pH 6.0, 25°C
0.00063
1-(4-aminobutyl)-3-(4-fluorobenzyl)guanidine
0.00013
1-(4-aminobutyl)-3-but-3-en-1-ylguanidine
pH 6.5, 25°C
0.00025
1-(4-aminobutyl)-3-but-3-yn-1-ylguanidine
pH 6.5, 25°C
0.00013
1-(4-aminobutyl)-3-prop-2-en-1-ylguanidine
-
0.00025
1-(4-aminobutyl)-3-prop-2-yn-1-ylguanidine
-
0.0007
1-(4-carbamimidamidobutyl)-3-(3-methylbut-2-en-1-yl)guanidine
pH 6.5, 25°C
0.00172
1-(5-aminopentyl)-3-(2-cyclohexylethyl)guanidine
pH 6.5, 25°C
0.00258
1-(5-aminopentyl)-3-(2-cyclopropylethyl)guanidine
pH 6.5, 25°C
0.00115
1-(5-aminopentyl)-3-(3-methoxybenzyl)guanidine
pH 6.5, 25°C
0.00001
1-(5-aminopentyl)-3-(3-methylbut-2-en-1-yl)guanidine
-
0.00001
1-(5-aminopentyl)-3-(4-methylpent-3-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
0.00022
1-(6-aminohexyl)-3-(3-methylbut-2-en-1-yl)guanidine
-
0.000022
1-(6-aminohexyl)-3-(4-methylpent-3-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
0.0000075
iminoctadine
pH 6.5, 25°C
0.0015
N,N'''-butane-1,4-diylbis[3-(3-methylbut-2-en-1-yl)guanidine]
0.00055
N,N'-bis(2,3-butadienyl)-1,4-butane-diamine
pH 6.5, 25°C
0.000015
N-prenylagmatine
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
0.000015
prenylagmatine
-
0.0003
1,8-diaminooctane
pH 6.5, 25°C
0.0003
1,8-diaminooctane
pH 6.0, 25°C
0.00063
1-(4-aminobutyl)-3-(4-fluorobenzyl)guanidine
-
0.00063
1-(4-aminobutyl)-3-(4-fluorobenzyl)guanidine
pH 6.5, 25°C
0.003
agmatine
-
0.003
agmatine
pH 6.5, 25°C
0.0015
N,N'''-butane-1,4-diylbis[3-(3-methylbut-2-en-1-yl)guanidine]
-
0.0015
N,N'''-butane-1,4-diylbis[3-(3-methylbut-2-en-1-yl)guanidine]
pH 6.5, 25°C
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malfunction
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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
additional information
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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
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accumulation and further oxidation of free PAs in the leaf apoplast of tobacco plants occurs in a similar, although not identical way during tobacco defense against infection by microorganisms with contrasting pathogenesis strategies. This response affects the pathogens ability to colonize host tissues and results are detrimental for plant defense against necrotrophic pathogens that feed on necrotic tissue
physiological function
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involvement of ZmPA-mediated H2O2 production in wound-healing events
physiological function
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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
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role of MPAO in abscisic acid-induced antioxidant defense in leaves of maize plants
physiological function
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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
a likely role for OsPAO7 during anther development is to deliver H2O2 for secondary wall thickening through lignin formation
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
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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
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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
physiological function
-
accumulation and further oxidation of free PAs in the leaf apoplast of tobacco plants occurs in a similar, although not identical way during tobacco defense against infection by microorganisms with contrasting pathogenesis strategies. This response affects the pathogens ability to colonize host tissues and results are detrimental for plant defense against necrotrophic pathogens that feed on necrotic tissue
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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
Y298F
specific activity or KM-values are not substantially altered
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
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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
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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
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