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Information on EC 1.5.3.16 - spermine oxidase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9FNA2

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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
                1.5.3.16 spermine oxidase
IUBMB Comments
The enzyme from Arabidopsis thaliana (AtPAO1) oxidizes norspermine to norspermidine with high efficiency . The mammalian enzyme, encoded by the SMOX gene, is a cytosolic enzyme that catalyses the oxidation of spermine at the exo (three-carbon) side of the tertiary amine. No activity with spermidine. Weak activity with N1-acetylspermine. A flavoprotein (FAD). Differs in specificity from EC 1.5.3.13 (N1-acetylpolyamine oxidase), 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) and EC 1.5.3.17 (non-specific polyamine oxidase).
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Arabidopsis thaliana
UNIPROT: Q9FNA2
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
spermine oxidase, smo(paoh1), atpao1, paoh1/smo, smo/paoh1, msmoalpha, msmomu, ghpao, fms1 protein, spm oxidase, more
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
spermidine:oxygen oxidoreductase (spermidine-forming)
The enzyme from Arabidopsis thaliana (AtPAO1) oxidizes norspermine to norspermidine with high efficiency [3]. The mammalian enzyme, encoded by the SMOX gene, is a cytosolic enzyme that catalyses the oxidation of spermine at the exo (three-carbon) side of the tertiary amine. No activity with spermidine. Weak activity with N1-acetylspermine. A flavoprotein (FAD). Differs in specificity from EC 1.5.3.13 (N1-acetylpolyamine oxidase), 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) 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
N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
show the reaction diagram
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetaminopropanal + H2O2
show the reaction diagram
norspermine + O2 + H2O
?
show the reaction diagram
norspermine + O2 + H2O
? + H2O2
show the reaction diagram
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
show the reaction diagram
spermine + O2 + H2O
spermidine + aminopropanal + H2O2
show the reaction diagram
thermospermine + O2 + H2O
? + H2O2
show the reaction diagram
thermospermine + O2 + H2O
norspermidine + ?
show the reaction diagram
-
-
-
?
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetamidopropanal + H2O2
show the reaction diagram
-
-
-
-
?
N1-acetylspermine + O2 + H2O
?
show the reaction diagram
the enzyme AtPAO5 has a better activity as a dehydrogenase rather than as an oxidase. With the best electron acceptor (ferricenium), the best in vitro substrate for recombinant AtPAO5 is N1-acetylspermine
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
show the reaction diagram
-
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetaminopropanal + H2O2
show the reaction diagram
-
-
-
?
norspermine + O2 + H2O
?
show the reaction diagram
norspermine + O2 + H2O
? + H2O2
show the reaction diagram
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
show the reaction diagram
spermine + O2 + H2O
spermidine + aminopropanal + H2O2
show the reaction diagram
thermospermine + O2 + H2O
?
show the reaction diagram
thermospermine + O2 + H2O
? + H2O2
show the reaction diagram
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
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
show the reaction diagram
enzyme is involved in a polyamine back-conversion pathway
-
-
?
norspermine + O2 + H2O
?
show the reaction diagram
-
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
show the reaction diagram
thermospermine + O2 + H2O
?
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
all FAD molecules in the purified enzyme are catalytically active
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,12-diaminododecane
-
1,8-diaminooctane
-
N-prenylagmatine
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.47
N1-acetylspermine
0.09 - 0.9
norspermine
0.11 - 0.12
spermine
0.02
thermospermine
pH 8.0, temperature not specified in the publication
0.47
N1-acetylspermine
-
pH 8.0, 25°C, recombinant AtPAO1
6.9
norspermine
-
pH 8.0, 25°C, recombinant AtPAO1
0.0046 - 11
O2
0.0256 - 0.23
spermine
5.7
thermospermine
-
pH 8.0, 25°C, recombinant AtPAO1
additional information
additional information
-
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
N1-acetylspermine
6.9
norspermine
2.5 - 2.7
spermine
5.7
thermospermine
pH 8.0, temperature not specified in the publication
0.014 - 0.2
N1-acetylspermine
0.09 - 0.45
norspermine
0.009 - 4.6
spermine
0.02 - 0.1
thermospermine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.43
N1-acetylspermine
pH 8.0, temperature not specified in the publication
7.7
norspermine
pH 8.0, temperature not specified in the publication
20.8
spermine
pH 8.0, temperature not specified in the publication
285
thermospermine
pH 8.0, temperature not specified in the publication
0.115 - 2.7
spermine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0117
1,12-diaminododecane
pH 8.0, substrate: spermine
0.293
1,8-diaminooctane
pH 8.0, substrate: spermine
0.147
agmatine
pH 8.0, substrate: spermine
0.0007
guazatine
pH 8.0, substrate: spermine
0.1373
MDL72527
pH 8.0, substrate: spermine
0.004
N-prenylagmatine
pH 8.0, substrate: spermine
0.546
spermidine
pH 8.0, substrate: spermine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
substrate: spermine or norspermine
7.5
substrate: spermine
7.5 - 8.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
7 - 9
pH 7.0: about 60% of maximal activity, pH 9.0: about 45% of maximal activity, substrate: spermine
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 42
substrate: spermine
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 50
25°C: about 55% of maximal activity, 50°C: about 45% of maximal activity, substrate: spermine
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
stress response
evolution
-
AtPAO2-AtPAO4 form a subfamily of polyamine oxidases different from AtPAO1, overview
malfunction
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PAO1_ARATH
472
0
52866
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
construction of a knock-out mutant that has a T-DNA insertion within the ninth exon of the AtPAO4 gene, and of a knock-down mutant Atpao4i with reduced expression by RNAi under control of the CMV 35S promoter. AtPAO4 deficiency induces alterations in the expression of genes related to the drought stress response and flavonoid biosynthesis
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein
recombinant His-tagged AtPAO4 from Escherichia coli strain BL21(DE3)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
AtPAO1 cDNA is isolated and cloned in a vector for heterologous expression in Escherichia coli
AtPAO1, 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
-
expression in Escherichia coli as a His-tagged protein
expression of His-tagged AtPAO4 in Escherichia coli strain BL21(DE3), transient expression of isozyme AtPAO4 in Arabidopsis thaliana root cell peroxisomes as monomeric red fluorescent protein fusion protein
gene AtPAO1, construction of AtPAO::GUS transgenic Arabidopsis thaliana plants
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
positive regulation of AtPAO5 expression by polyamines at the transcriptional and post-transcriptional level
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tavladoraki, P.; Rossi, M.N.; Saccuti, G.; Perez-Amador, M.A.; Polticelli, F.; Angelini, R.; Federico, R.
Heterologous expression and biochemical characterization of a polyamine oxidase from Arabidopsis involved in polyamine back conversion
Plant Physiol.
141
1519-1532
2006
Arabidopsis thaliana (Q9FNA2)
Manually annotated by BRENDA team
Kamada-Nobusada, T.; Hayashi, M.; Fukazawa, M.; Sakakibara, H.; Nishimura, M.
A putative peroxisomal polyamine oxidase, AtPAO4, is involved in polyamine catabolism in Arabidopsis thaliana
Plant Cell Physiol.
49
1272-1282
2008
Arabidopsis thaliana (Q8H191)
Manually annotated by BRENDA team
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.
6
1155-1168
2010
Arabidopsis thaliana (Q8H191), Arabidopsis thaliana (Q9FNA2), Arabidopsis thaliana
Manually annotated by BRENDA team
Takahashi, Y.; Cong, R.; Sagor, G.H.; Niitsu, M.; Berberich, T.; Kusano, T.
Characterization of five polyamine oxidase isoforms in Arabidopsis thaliana
Plant Cell Rep.
29
955-965
2010
Arabidopsis thaliana (Q8H191), Arabidopsis thaliana (Q9FNA2), Arabidopsis thaliana
Manually annotated by BRENDA team
Fincato, P.; Moschou, P.N.; Ahou, A.; Angelini, R.; Roubelakis-Angelakis, K.A.; Federico, R.; Tavladoraki, P.
The members of Arabidopsis thaliana PAO gene family exhibit distinct tissue- and organ-specific expression pattern during seedling growth and flower development
Amino Acids
42
831-841
2012
Arabidopsis thaliana
Manually annotated by BRENDA team
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
Arabidopsis thaliana, Arabidopsis thaliana Columbia-0
Manually annotated by BRENDA team
Tavladoraki, P.; Cona, A.; Angelini, R.
Copper-containing amine oxidases and FAD-dependent polyamine oxidases are key players in plant tissue differentiation and organ development
Front. Plant Sci.
7
824
2016
Arabidopsis thaliana (Q8H191), Arabidopsis thaliana (Q9FNA2)
Manually annotated by BRENDA team
Ahou, A.; Martignago, D.; Alabdallah, O.; Tavazza, R.; Stano, P.; Macone, A.; Pivato, M.; Masi, A.; Rambla, J.L.; Vera-Sirera, F.; Angelini, R.; Federico, R.; Tavladoraki, P.
A plant spermine oxidase/dehydrogenase regulated by the proteasome and polyamines
J. Exp. Bot.
65
1585-1603
2014
Arabidopsis thaliana (Q9SU79)
Manually annotated by BRENDA team
Hou, Z.; Liu, G.; Hou, L.; Wang, L.; Liu, X.
Regulatory function of polyamine oxidase-generated hydrogen peroxide in ethylene-induced stomatal closure in Arabidopsis thaliana
J. Integr. Agric.
12
251-262
2013
Arabidopsis thaliana (Q8H191)
-
Manually annotated by BRENDA team
Kim, D.W.; Watanabe, K.; Murayama, C.; Izawa, S.; Niitsu, M.; Michael, A.J.; Berberich, T.; Kusano, T.
Polyamine oxidase 5 regulates Arabidopsis growth through Thermospermine oxidase activity
Plant Physiol.
165
1575-1590
2014
Arabidopsis thaliana (Q9SU79)
Manually annotated by BRENDA team