Information on EC 1.5.3.14 - polyamine oxidase (propane-1,3-diamine-forming)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.5.3.14
-
RECOMMENDED NAME
GeneOntology No.
polyamine oxidase (propane-1,3-diamine-forming)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
spermidine + O2 + H2O = propane-1,3-diamine + 4-aminobutanal + H2O2
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
-
-
beta-Alanine metabolism
-
-
Metabolic pathways
-
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spermine and spermidine degradation II
-
-
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).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain W38
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N1-acetylspermidine + O2 + H2O
?
show the reaction diagram
-
-
-
?
N1-acetylspermine + O2 + H2O
1,3-diaminopropane + H2O2 + ?
show the reaction diagram
-
-
-
?
N8-acetylspermine + O2 + H2O
1,3-diaminopropane + H2O2 + ?
show the reaction diagram
-
-
-
?
spermidine + O2 + H2O
1,3-diaminopropane + 4-aminobutanal + H2O2
show the reaction diagram
spermidine + O2 + H2O
1,3-diaminopropane + H2O2 + ?
show the reaction diagram
-
-
-
?
spermidine + O2 + H2O
?
show the reaction diagram
-
-
-
-
?
spermidine + O2 + H2O
propane-1,3-diamine + 4-aminobutanal + H2O2
show the reaction diagram
spermine + O2 + H2O
1,3-diaminopropane + aminoaldehyde + H2O2
show the reaction diagram
spermine + O2 + H2O
1,3-diaminopropane + H2O2 + ?
show the reaction diagram
-
-
-
?
spermine + O2 + H2O
1-(3-aminopropyl)-4-aminobutanal + propane-1,3-diamine + H2O2
show the reaction diagram
-
-
-
-
?
spermine + O2 + H2O
?
show the reaction diagram
-
-
-
-
?
spermine + O2 + H2O
propane-1,3-diamine + N-(3-aminopropyl)-4-aminobutanal + H2O2
show the reaction diagram
-
-
-
-
?
spermine + O2 + H2O
spermidine + propane-1,3-diamine + H2O2
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
spermidine + O2 + H2O
1,3-diaminopropane + 4-aminobutanal + H2O2
show the reaction diagram
spermidine + O2 + H2O
propane-1,3-diamine + 4-aminobutanal + H2O2
show the reaction diagram
-
-
-
-
?
spermine + O2 + H2O
1,3-diaminopropane + aminoaldehyde + H2O2
show the reaction diagram
spermine + O2 + H2O
propane-1,3-diamine + N-(3-aminopropyl)-4-aminobutanal + H2O2
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NaCl
-
salt increases PAO activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(N1-5-aminopentyl)-N3-(cyclohexylethyl)-N1,N2,N3-tris(tert-butoxycarbonyl)guanidine
-
-
1,10-Diaminodecane
-
-
1,12-diaminododecane
-
-
1,19-bis(ethylamino)-5,10,15-triazanonadecane
-
i.,e. SL-11061, 68% inhibition at 0.5 mM
1,3-Diaminopropane
-
-
1,4-diaminobutane
-
-
1,5-Diaminopentane
-
-
1,6-diaminohexane
-
-
1,7-Diaminoheptane
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-
1,8-diaminooctane
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-
1,9-diaminononane
-
-
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
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-
1-(4-aminobutyl)-3-prop-2-yn-1-ylguanidine
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-
1-(4-carbamimidamidobutyl)-3-(3-methylbut-2-en-1-yl)guanidine
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-
1-(5-aminopentyl)-3-(2-cyclohexylethyl)guanidine
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-
1-(5-aminopentyl)-3-(2-cyclopropylethyl)guanidine
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-
1-(5-aminopentyl)-3-(3-methoxybenzyl)guanidine
-
-
1-(5-aminopentyl)-3-(3-methylbut-2-en-1-yl)guanidine
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-
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
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-
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
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-
1-[7-[(9-carbamimidamidononyl)amino]heptyl]-3-(2-cyclopropylethyl)guanidine
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1-[7-[(9-carbamimidamidononyl)amino]heptyl]-3-(2-phenylethyl)guanidine
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1-[7-[(9-carbamimidamidononyl)amino]heptyl]-3-(3-methylbut-3-en-1-yl)guanidine
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-
3-(4-methylpent-3-en-1-yl)-1-[9-([7-[(4-methylpent-3-en-1-yl)carbamimidamido]heptyl]amino)nonyl]guanidine
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3-but-3-yn-1-yl-1-[7-[(9-carbamimidamidononyl)amino]heptyl]guanidine
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3-[(2E)-but-2-en-1-yl]-1-[7-[(9-carbamimidamidononyl)amino]heptyl]guanidine
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-
agmatine
DELTA1-pyrroline
-
competitive
diazabicyclononane
-
competitive
diphenylene iodonium
-
slight inhibition of PAO
guazatine
iminoctadine
-
-
N,N'''-butane-1,4-diylbis[3-(3-methylbut-2-en-1-yl)guanidine]
N,N'-bis(2,3-butadienyl)-1,4-butane-diamine
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i.e. MDL72527
N,N'-diaminoguanidine
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about 25% inmhibition at 0.5 mM
N-prenyl agmatine
-
-
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
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-
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-acetylspermine
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
-
-
prenylagmatine
-
-
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
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-
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
-
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additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.274
N1-acetylspermidine
-
-
0.062
N1-acetylspermine
-
-
1.13
N8-acetylspermine
-
-
0.0007 - 0.04
spermidine
0.0012 - 0.038
spermine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004 - 55.1
spermidine
0.0053 - 39.3
spermine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0006
1,10-Diaminodecane
-
pH 6.0, 25C
0.00017
1,12-diaminododecane
-
pH 6.0, 25C
0.1
1,3-Diaminopropane
-
pH 6.0, 25C
0.13
1,4-diaminobutane
-
pH 6.0, 25C
0.038
1,5-Diaminopentane
-
pH 6.0, 25C
0.003
1,6-diaminohexane
-
pH 6.0, 25C
0.0004
1,7-Diaminoheptane
-
pH 6.0, 25C
0.0003
1,8-diaminooctane
0.0012
1,9-diaminononane
-
pH 6.0, 25C
0.00063
1-(4-aminobutyl)-3-(4-fluorobenzyl)guanidine
0.00013
1-(4-aminobutyl)-3-but-3-en-1-ylguanidine
-
pH 6.5, 25C
0.00025
1-(4-aminobutyl)-3-but-3-yn-1-ylguanidine
-
pH 6.5, 25C
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, 25C
0.00172
1-(5-aminopentyl)-3-(2-cyclohexylethyl)guanidine
-
pH 6.5, 25C
0.00258
1-(5-aminopentyl)-3-(2-cyclopropylethyl)guanidine
-
pH 6.5, 25C
0.00115
1-(5-aminopentyl)-3-(3-methoxybenzyl)guanidine
-
pH 6.5, 25C
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, 25C
0.00153
1-(5-aminopentyl)-3-[(2E)-3-phenylprop-2-en-1-yl]guanidine
-
pH 6.5, 25C
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, 25C
0.000003
1-(guanidino)-17-(N1-(gamma,gamma-dimethylallyl)guanidino)-9-azaheptadecane tris(trifluoroacetate)
-
pH 6.5, 25C
0.00121
1-[3-[(3-aminopropyl)amino]propyl]-3-(3-methylbut-2-en-1-yl)guanidine
-
pH 6.5, 25C
0.00000008
1-[7-[(9-carbamimidamidononyl)amino]heptyl]-3-(2-cyclopropylethyl)guanidine
-
pH 6.5, 25C
0.000001
1-[7-[(9-carbamimidamidononyl)amino]heptyl]-3-(2-phenylethyl)guanidine
-
pH 6.5, 25C
0.0000005
1-[7-[(9-carbamimidamidononyl)amino]heptyl]-3-(3-methylbut-3-en-1-yl)guanidine
-
pH 6.5, 25C
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, 25C
0.0000007
3-but-3-yn-1-yl-1-[7-[(9-carbamimidamidononyl)amino]heptyl]guanidine
-
pH 6.5, 25C
0.0000011
3-[(2E)-but-2-en-1-yl]-1-[7-[(9-carbamimidamidononyl)amino]heptyl]guanidine
-
pH 6.5, 25C
0.003
agmatine
0.4
DELTA1-pyrroline
-
-
0.1
diazabicyclononane
-
-
0.0000075
guazatine
-
-
0.0000075
iminoctadine
-
pH 6.5, 25C
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, 25C
0.000015
N-prenylagmatine
-
pH 6.5, 25C
0.018
N1-benzylamine-N3-(gamma,gamma-dimethylallyl)guanidine bis-(trifluoroacetate)
-
pH 6.5, 25C
0.000015
prenylagmatine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
PAO activity in unsalinized and salt-treated plants, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
assay at
7.5
-
assay at
7.8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
30
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
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, 20C, two weeks, X-ray diffraction structure determination and analysis at 2.9 A resolution,mlecular displacement, modelling
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
single two-state transition at pH 6 with Tm 49.8C. At pH 5 the thermal stability is increased by more than 14C
694595
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
single two-state transition at pH 6 with Tm 49.8C. At pH 5 the thermal stability is increased by more than 14C. DELTA1-pyrroline and diazabicyclononane improve the thermal stability of the enzyme
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme from apoplastic fluids of leaf blade segments
-
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
expression in Pichia pastoris, wild-type and mutant enzymes
-
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; transgenic tobacco plants overexpressing polyamine oxidase from Zea mays exhibit high 1,3-diaminopropane content
-
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
-
ZmPAO, DNA and amino acid sequence determination and analysis, intron/exon organization, sequence comparisons, expression of His-tagged enzyme in Pichia pastoris
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
abscisic acid enhances the MPAO gene expression
-
infections with pathogens biotrophic bacterium Pseudomonas viridiflava and necrotrophic fungus Sclerotinia sclerotiorum lead to increased enzyme expression and activity with an increase of apoplastic spermine levels
wounding induces the enzyme
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
Y298F
-
specific activity or KM-values are not substantially altered
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