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Information on EC 1.4.3.21 - primary-amine oxidase
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1.4.3.21 primary-amine oxidaseIUBMB Comments
A group of enzymes that oxidize primary monoamines but have little or no activity towards diamines, such as histamine, or towards secondary and tertiary amines. They are copper quinoproteins (2,4,5-trihydroxyphenylalanine quinone) and, unlike EC 1.4.3.4, monoamine oxidase, are sensitive to inhibition by carbonyl-group reagents, such as semicarbazide. In some mammalian tissues the enzyme also functions as a vascular-adhesion protein (VAP-1).
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Word Map
- 1.4.3.21
- endothelial
- diamine
-
1.4.3.6
-
ssaos
-
deamination
- polyamines
- leukocyte
- putrescine
- lymphocyte
- spermine
- methylamine
-
lysyl
- vessel
- arthrobacter
-
extravasation
- phenylhydrazine
-
2,4,5-trihydroxyphenylalanine
- globiformis
- elastin
- cadaverine
-
klinman
-
biogenic
- aminoguanidine
-
half-reaction
- histaminase
- semiquinone
- pargyline
- acrolein
-
pyrroloquinoline
-
transmigration
- allylamine
- clorgyline
- beta-aminopropionitrile
- aminoacetone
-
copper-binding
-
self-processing
-
quinoproteins
- 2-phenylethylamine
-
addressins
- deprenyl
- phenelzine
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
vap-1, vascular adhesion protein-1, copper amine oxidase, benzylamine oxidase, bovine serum amine oxidase, plasma amine oxidase, ssao/vap-1, bovine plasma amine oxidase, copper-containing amine oxidase, primary amine oxidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AMAO2
AMAO3
AO1
AO2
AOC3
CAO
Copper amine oxidase
copper amine oxidase 1
copper-containing amine oxidase
copper-containing monoamine oxidase
copper-dependent amine oxidase
Cu/TPQ amine oxidase
CuAO
EC 1.4.3.6
HPAO
hPAO-1
primary amine oxidase
PSAO
quinoprotein copper-containing amine oxidase
semicarbazide-sensitive amine oxidase
SSAO
SSAO/VAP-1
VAP-1
vascular adhesion protein 1
vascular adhesion protein-1
additional information
VAP-1 belongs to the semicarbazide-sensitive amine oxidases, SSAOs
AOC3
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the major SSAO form expressed in mouse adipocytes is encoded by the AOC3 gene
semicarbazide-sensitive amine oxidase
-
-
semicarbazide-sensitive amine oxidase
-
-
SSAO
-
-
SSAO
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2
-
-
-
-
RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2
proposed mechanism, crystal structure
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RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2
proposed mechanism, crystal structure
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
primary-amine:oxygen oxidoreductase (deaminating)
A group of enzymes that oxidize primary monoamines but have little or no activity towards diamines, such as histamine, or towards secondary and tertiary amines. They are copper quinoproteins (2,4,5-trihydroxyphenylalanine quinone) and, unlike EC 1.4.3.4, monoamine oxidase, are sensitive to inhibition by carbonyl-group reagents, such as semicarbazide. In some mammalian tissues the enzyme also functions as a vascular-adhesion protein (VAP-1).
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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
1,4-diaminobutane + H2O + O2
?
-
enzyme II shows 23% activity and enzyme III 12% activity compared to 4-aminobutanamide
-
-
?
1,5-diaminopentane + H2O + O2
?
-
enzyme II shows 5% activity and enzyme III 31% activity compared to 4-aminobutanamide
-
-
?
1-aminononane + H2O + O2
nonanal + NH3 + H2O2
-
the aliphatic chain of 1-aminononane induces a shift in the pKa-value of the product Schiff base, the hydrolysis of which appears to be a rate-determining step of the reaction
-
-
?
1-methyl-3-phenylpropylamine + H2O + O2
4-phenylbutan-2-one + NH3 + H2O2
-
-
-
-
?
2-aminoethylpyridine + H2O + O2
pyridine-2-carbaldehyde + NH3 + H2O2
-
-
-
?
2-phenylethylamine + H2O + O2
beta-phenylethanal + NH3 + H2O2
-
-
-
?
3-aminomethylpyridine + H2O + O2
pyridine-3-carbaldehyde + NH3 + H2O2
-
-
-
?
3-aminopentanamide + H2O + O2
3-oxopentanamide + NH3 + H2O2
-
enzyme II shows 214% activity and enzyme III 11% activity compared to 4-aminobutanamide
-
-
?
4-amino-1-butanol + H2O + O2
4-hydroxybutanal + NH3 + H2O2
-
enzyme II shows 525% activity and enzyme III 267% activity compared to 4-aminobutanamide
-
-
?
4-aminobutanamide + H2O + O2
4-oxobutanamide + NH3 + H2O2
-
100% activity
-
-
?
4-aminobutyric acid + H2O + O2
4-oxobutanoate + NH3 + H2O2
-
enzyme II shows no activity and enzyme III 10% activity compared to 4-aminobutanamide
-
-
?
4-aminomethylpyridine + H2O + O2
pyridine-4-carbaldehyde + NH3 + H2O2
-
-
-
?
4-fluorobenzylamine + H2O + O2
4-fluorobenzaldehyde + NH3 + H2O2
-
-
-
-
?
5-amino-1-pentanol + H2O + O2
5-hydroxypentanal + NH3 + H2O2
-
enzyme II shows 86% activity and enzyme III 388% activity compared to 4-aminobutanamide
-
-
?
5-aminopentanoic acid + H2O + O2
5-oxopentanoate + NH3 + H2O2
-
enzyme II shows 3% activity and enzyme III 7% activity compared to 4-aminobutanamide
-
-
?
alpha-casein + H2O + O2
?
-
the enzyme oxidizes the lysine residues in alpha-casein protein
-
-
?
beta-phenylethylamine + H2O + O2
beta-phenylethanal + NH3 + H2O2
-
-
-
?
beta-phenylethylamine + O2 + H2O
beta-phenylethanal + NH3 + H2O2
-
-
-
?
cadaverine + H2O + O2
DELTA1-piperideine + NH3 + H2O2
best substrate
-
-
?
cyclohexanemethylamine + H2O + O2
cyclohexanecarbaldehyde + NH3 + H2O2
-
-
-
?
methyl 1-(2-methoxyethyl)-3-(trifluoroacetyl)-1H-indole-4-carboxylate + H2O + O2
?
-
-
-
-
?
n-butylamine + H2O + O2
butanal + NH3 + H2O2
-
enzyme II shows 368% activity and enzyme III 454% activity compared to 4-aminobutanamide
-
-
?
n-hexylamine + H2O + O2
hexanal + NH3 + H2O2
-
enzyme II shows 244% activity and enzyme III 589% activity compared to 4-aminobutanamide
-
-
?
n-pentylamine + H2O + O2
pentanal + NH3 + H2O2
-
enzyme II shows 314% activity and enzyme III 596% activity compared to 4-aminobutanamide
-
-
?
n-propylamine + H2O + O2
propanal + NH3 + H2O2
-
enzyme II shows 515% activity and enzyme III 201% activity compared to 4-aminobutanamide
-
-
?
Nalpha-benzyloxycarbony-L-lysine + H2O + O2
?
-
enzyme II shows 3% activity and enzyme III 12% activity compared to 4-aminobutanamide
-
-
?
Nalpha-Z-D-lysine + H2O + O2
?
-
enzyme II shows no activity and enzyme III 10% activity compared to 4-aminobutanamide
-
-
?
octopamine + H2O + O2
hydroxy(hydroxyphenyl)acetaldehyde + NH3 + H2O2
-
-
-
-
?
ornithine + H2O + O2
?
ornithine can be transformed in glutamate-5-semialdehyde spontaneously cyclizes yielding DELTA1-pyrroline-5-carboxylic acid
-
-
?
pyrrolidine + 2,4,5-trihydroxyphenylalanine quinone + H2O + O2
? + H2O2 + NH3
-
-
-
-
?
serotonin + O2 + H2O
(5-hydroxy-1H-indol-3yl)acetaldehyde + NH3 + H2O2
-
-
-
?
spermidine + H2O + O2
? + NH3 + H2O2
good substrate. The oxidation of spermidine yields to the liberation of ammonia, hydrogen peroxide and the corresponding aldehyde that spontaneously cyclizes yielding first 1-(3-aminopropyl)pyrroliniun and, thereafter, 1,5-diazobicyclononane
-
-
?
tropoelastin + H2O + O2
?
-
the enzyme oxidizes the lysine residues in tropoelastin protein
-
-
?
tyramine + H2O + O2
?
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
-
-
?
1,4-diamino-2-butyne + H2O + O2
?
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
-
-
?
1,4-diamino-2-chloro-2-butene + H2O + O2
?
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
-
-
?
1,5-diamino-2-pentyne + H2O + O2
?
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
-
-
?