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Information on EC 1.5.3.17 - non-specific polyamine oxidase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P50264
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1.5.3.17 non-specific polyamine oxidaseIUBMB Comments
A flavoprotein (FAD). The non-specific polyamine oxidases may differ from each other considerably. The enzyme from Saccharomyces cerevisiae shows a rather broad specificity and also oxidizes N8-acetylspermidine . The enzyme from Ascaris suum shows high activity with spermine and spermidine, but also oxidizes norspermine . The enzyme from Arabidopsis thaliana shows high activity with spermidine, but also oxidizes other polyamines .
The specific polyamine oxidases are classified as 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 1.5.3.16 (spermine oxidase).
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Word Map
- 1.5.3.17
- spermidine
-
back-conversion
- putrescine
- peroxisomal
- sativa
- seedling
-
tetraamines
-
abscisic
- anther
- pollen
- medicine
- analysis
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
atpao5, atpao2, atpao3, ospao1, atpao4, polyamine oxidase 1, selpao5, bjpao1, slr5093, t-spm oxidase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
polyamine:oxygen oxidoreductase (3-aminopropanal or 3-acetamidopropanal-forming)
A flavoprotein (FAD). The non-specific polyamine oxidases may differ from each other considerably. The enzyme from Saccharomyces cerevisiae shows a rather broad specificity and also oxidizes N8-acetylspermidine [3]. The enzyme from Ascaris suum shows high activity with spermine and spermidine, but also oxidizes norspermine [2]. The enzyme from Arabidopsis thaliana shows high activity with spermidine, but also oxidizes other polyamines [1].
The specific polyamine oxidases are classified as 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 1.5.3.16 (spermine 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
N1-acetylspermine + O2 + H2O
spermidine + N-acetyl-3-aminopropanal + H2O2
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
-
-
?
(3R,3'R)-dimethylspermine + 2 O2 + 2 H2O
putrescine + 2 3-aminobutanal + 2 H2O2
-
-
-
-
?
(3S,3'S)-dimethylspermine + 2 O2 + 2 H2O
putrescine + 2 3-aminobutanal + 2 H2O2
-
-
-
-
?
additional information
?
-
flavoprotein oxidase Fms1 catalyzes the oxidation of spermine and N1-acetylspermine to spermidine and 3-aminopropanal or N-acetyl-3-aminopropanal
-
-
?
additional information
?
-
-
Fms1 prefers (S,S)- to (R,R)-diastereoisomer, but with notably lower kcat in comparison with spermine. Fms1 is prone to aldehyde supplementation in its regioselectivity, i.e. the cleavage site of spermidine
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-
-
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
N1-acetylspermine + O2 + H2O
spermidine + N-acetyl-3-aminopropanal + H2O2
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
-
-
?
additional information
?
-
flavoprotein oxidase Fms1 catalyzes the oxidation of spermine and N1-acetylspermine to spermidine and 3-aminopropanal or N-acetyl-3-aminopropanal
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.011
N1-acetylspermine
pH 9.0, 25°C, recombinant wild-type Fms1
0.104
N1-acetylspermine
pH 9.0, 25°C, recombinant mutant N195A
0.015
O2
pH 9.0, 25°C, recombinant mutant N195A, with spermine
0.02
O2
pH 9.0, 25°C, recombinant mutant N195A, with N1-acetylspermine
0.0436
O2
pH 9.0, 25°C, recombinant wild-type Fms1, with N1-acetylspermine
0.091
O2
pH 9.0, 25°C, recombinant wild-type Fms1, with spermine
0.097
O2
pH 9.0, 25°C, recombinant mutant D94N, with N1-acetylspermine
0.192
O2
pH 9.0, 25°C, recombinant mutant D94N, with spermine
additional information
additional information
seady-state kinetics and rapid-reaction kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
steady-state kinetics and rapid-reaction kinetics of wild-type and mutant enzymes, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
15.1
N1-acetylspermine
pH 9.0, 25°C, recombinant wild-type Fms1
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1400
N1-acetylspermine
pH 9.0, 25°C, recombinant wild-type Fms1
100
O2
pH 9.0, 25°C, recombinant mutant D94N, with N1-acetylspermine
358
O2
pH 9.0, 25°C, recombinant wild-type Fms1, with N1-acetylspermine
405
O2
pH 9.0, 25°C, recombinant mutant N195A, with N1-acetylspermine
428
O2
pH 9.0, 25°C, recombinant wild-type Fms1, with spermine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH profile for the reductive half-reaction of Fms1, a moiety with a pKa value of 7.2-8.3 must be unprotonated for amine oxidation, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
flavoprotein Fms1 catalyzes the oxidation of spermine in the biosynthetic pathway for pantothenic acid
additional information
additional information
the active site of Fms1 contains three amino acid residues positioned to interact with the polyamine substrate, His67, Asn195, and Asp94. These three residues form a hydrogen-bonding triad with Asn195 being the central residue. His67 is important both for interacting with the substrate and for maintaining the hydrogen bonds in the triad
additional information
the overall catalytic reactions of flavoprotein oxidases such as Fms1 can be divided into reductive and oxidative half-reactions. In the reductive half-reaction, binding of the oxidized substrate is followed by transfer of a hydride equivalent to the flavin to form reduced flavin and oxidized substrate. In the oxidative half-reaction, the reduced flavin is oxidized by molecular oxygen to form H2O2, the oxidized amine then dissociates from the enzyme. A moiety with a pKa value of 7.2-8.3 must be unprotonated for amine oxidation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme mutant H67Q, sitting drop vapor diffusion method, mixing of protein solution, in 25 mM HEPES, pH 7.5, in a 1:1 ratio with buffer containing 20% w/v PEG 3350, 0.2 M sodium acetate, and 0.1 M bis-Tris propane, pH 7.5, X-ray diffraction structure determination and analysis at 2.4 A resolution, molecular replacement
purified recombinant enzyme mutant N195A, sitting drop vapour diffusion method, mixing of protein solution, containing 25 mM HEPES, 25 mM NaCl, and 2% glycerol, pH 7.5, in a 1:1 ratio with buffer containing 30 mM diethylene glycol, 30 mM triethylene glycol, 30 mM tetraethylene glycol, 30 mM pentaethylene glycol, 10% ethylene glycol, 20% PEG 8000, and 0.1 MES-imidazole, pH 6.5, 1 week, X-ray diffraction structure determination and analysis at 2.0 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D94N
site-directed mutagenesis, the mutation primarily affects the reductive half-reaction. The mutant shows 20-40fold reduced rate constant for flavin reduction with spermine and 450fold with N1-acetylspermine compared to the wild-type enzyme
H67A
site-directed mutagenesis, the mutant shows a 2-3fold reduced first-order rate constant for flavin reduction and slightly altered kinetics compared to the wild-type enzyme
H67N
site-directed mutagenesis, the mutant shows a 2-3fold reduced first-order rate constant for flavin reduction and slightly altered kinetics compared to the wild-type enzyme
H67Q
site-directed mutagenesis, the mutant shows a 2-3fold reduced first-order rate constant for flavin reduction and slightly altered kinetics compared to the wild-type enzyme
N195A
site-directed mutagenesis, the mutation primarily affects the reductive half-reaction. The mutant shows 20-40fold reduced rate constant for flavin reduction with spermine and 450fold with N1-acetylspermine compared to the wild-type enzyme. Mutant N195A enzyme shows structure with a molecule of tetraethylene glycol in the active site, the mutation has no effect on the protein structure
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes by nickel affinity chhromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of His-tagged wild-type and mutant enzymes
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
Adachi, M.; Taylor, A.; Hart, P.; Fitzpatrick, P.
Mechanistic and structural analyses of the role of His67 in the yeast polyamine oxidase Fms1
Biochemistry
51
4888-4897
2012
Saccharomyces cerevisiae (P50264)
Adachi, M.; Taylor, A.; Hart, P.; Fitzpatrick, P.
Mechanistic and structural analyses of the roles of active site residues in yeast polyamine oxidase Fms1: characterization of the N195A and D94N enzymes
Biochemistry
51
8690-8697
2012
Saccharomyces cerevisiae (P50264)
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
Saccharomyces cerevisiae
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