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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
-
1.4.3.6
- diamine
-
ssaos
-
deamination
- leukocyte
- polyamines
- lymphocyte
- putrescine
- spermine
- vessel
- methylamine
-
lysyl
- arthrobacter
-
extravasation
- phenylhydrazine
-
2,4,5-trihydroxyphenylalanine
- globiformis
-
klinman
- elastin
- cadaverine
- aminoguanidine
- pargyline
-
transmigration
- semiquinone
-
half-reaction
- histaminase
-
pyrroloquinoline
- acrolein
- beta-aminopropionitrile
- allylamine
- clorgyline
- phenelzine
- 2-phenylethylamine
-
quinoproteins
- deprenyl
- aminoacetone
-
addressins
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
AGAO, AMAO2, AMAO3, amine oxidase 1, amine oxidase, copper containing, AO1, AO2, AOC2, AOC3, BAO, 
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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
semicarbazide-sensitive amine oxidases
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
-
the major SSAO form expressed in mouse adipocytes is encoded by the AOC3 gene
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
-
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
-
-
?
1,6-diamino-2,4-hexadiyne + 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
-
-
?
2-bromoethylamine + H2O + O2
bromoacetaldehyde + NH3 + H2O2
-
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
-
-
?
2-phenylethylamine + H2O + O2
2-phenylethanal + NH3 + H2O2
-
-
-
?
2-phenylethylamine + H2O + O2
2-phenylethanal + NH3 + H2O2
-
-
-
-
?
2-phenylethylamine + H2O + O2
2-phenylethanal + NH3 + H2O2
-
-
-
?
2-phenylethylamine + H2O + O2
2-phenylethanal + NH3 + H2O2
-
-
-
-
?
2-phenylethylamine + H2O + O2
phenylacetaldehyde + NH3 + H2O2
-
-
-
?
2-phenylethylamine + H2O + O2
phenylacetaldehyde + NH3 + H2O2
-
preferred substrate
-
-
?
2-phenylethylamine + H2O + O2
phenylacetaldehyde + NH3 + H2O2
-
enzyme II shows 134% activity and enzyme III 591% activity compared to 4-aminobutanamide
-
-
?
2-phenylethylamine + H2O + O2
phenylacetaldehyde + NH3 + H2O2
best substrate
-
-
?
3,3-bis(aminoethyl)-1-hydroxy-2-oxo-1-triazene + 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
-
-
?
4-(aminomethyl)-N-[3-(aminomethyl)benzyl]benzamide + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
4-(aminomethyl)-N-[3-(aminomethyl)benzyl]benzamide + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
4-aminomethylpyridine dihydrochloride + H2O + O2
?
45% substrate activity of 1 mM 4-aminomethylpyridine dihydrochloride as percentage of the activity of the best substrate (beta-phenylethylamine, 1 mM) for various amine oxidases
-
-
?
4-aminomethylpyridine dihydrochloride + H2O + O2
?
less than 0.1% substrate activity of 1 mM 4-aminomethylpyridine dihydrochloride as percentage of the activity of the best substrate (putrescine, 1 mM) for various amine oxidases
-
-
?
4-aminomethylpyridine dihydrochloride + H2O + O2
?
-
87% substrate activity of 1 mM 4-aminomethylpyridine dihydrochloride as percentage of the activity of the best substrate (benzylamine, 1 mM) for various amine oxidases
-
-
?
4-phenylbutylamine + H2O + O2
4-phenylbutanal + NH3 + H2O2
-
enzyme II shows 122% activity and enzyme III 493% activity compared to 4-aminobutanamide
-
-
?
4-phenylbutylamine + H2O + O2
4-phenylbutanal + NH3 + H2O2
-
enzyme II shows 122% activity and enzyme III 493% activity compared to 4-aminobutanamide
-
-
?
5-hydroxytryptamine + H2O + O2
?
-
enzyme II shows no activity and enzyme III 6% activity compared to 4-aminobutanamide
-
-
?
5-hydroxytryptamine + H2O + O2
?
-
enzyme II shows no activity and enzyme III 6% activity compared to 4-aminobutanamide
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
very poor substrate
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
enzyme II shows 4% activity and enzyme III 157% activity compared to 4-aminobutanamide
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
enzyme II shows 4% activity and enzyme III 157% activity compared to 4-aminobutanamide
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
low activity
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
best oxidized substrate
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
Mycobacterium sp. DSM 3803 / JC1
-
best oxidized substrate
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
main substrate for isoform AO1
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
main substrate for isoform AO1
-
-
?
dopamine + H2O + O2
(3,4-dihydroxyphenyl)acetaldehyde + NH3 + H2O2
-
-
-
-
?
dopamine + H2O + O2
(3,4-dihydroxyphenyl)acetaldehyde + NH3 + H2O2
-
-
-
-
?
ethylamine + H2O + O2
acetaldehyde + NH3 + H2O2
-
enzyme II shows 1124% activity and enzyme III 119% activity compared to 4-aminobutanamide
-
-
?
ethylamine + H2O + O2
acetaldehyde + NH3 + H2O2
-
isoforms AO1 and AO2 show 100% activity with ethylamine
-
-
?
ethylamine + H2O + O2
acetaldehyde + NH3 + H2O2
Schizosaccharomyces pombe FY435 / ATCC 87284
-
-
-
-
?
histamine + H2O + O2
(imidazol-4-yl)acetaldehyde + NH3 + H2O2
-
-
-
?
histamine + H2O + O2
(imidazol-4-yl)acetaldehyde + NH3 + H2O2
Mycobacterium sp. DSM 3803 / JC1
-
-
-
-
?
histamine + H2O + O2
1H-imidazol-4-ylacetaldehyde + NH3 + H2O2
-
-
-
?
histamine + H2O + O2
1H-imidazol-4-ylacetaldehyde + NH3 + H2O2
-
enzyme II shows 6% activity and enzyme III 322% activity compared to 4-aminobutanamide
-
-
?
histamine + H2O + O2
1H-imidazol-4-ylacetaldehyde + NH3 + H2O2
-
enzyme II shows 6% activity and enzyme III 322% activity compared to 4-aminobutanamide
-
-
?
N6-(4-aminobut-2-ynyl)adenine + 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
-
-
?
phenylethylamine + H2O + O2
phenylacetaldehyde + NH3 + H2O2
-
main substrate for isoform AO2
-
-
?
putrescine + H2O + O2
?
putrescine can be oxidatively deaminated by the enzyme to corresponding aldehyde that spontaneously cyclizes yielding DELTA1-pyrroline
-
-
?
tryptamine + H2O + O2
(1H-indol-3-yl)acetaldehyde + NH3 + H2O2
-
-
-
-
?
tryptamine + H2O + O2
(1H-indol-3-yl)acetaldehyde + NH3 + H2O2
-
enzyme II shows 4% activity and enzyme III 175% activity compared to 4-aminobutanamide
-
-
?
tryptamine + H2O + O2
(1H-indol-3-yl)acetaldehyde + NH3 + H2O2
-
-
-
?
tryptamine + H2O + O2
(1H-indol-3-yl)acetaldehyde + NH3 + H2O2
high activity
-
-
?
tryptamine + H2O + O2
1H-indol-3-ylacetaldehyde + NH3 + H2O2
-
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
-
-
?
tyramine + H2O + O2
(4-hydroxyphenyl)acetaldehyde + NH3 + H2O2
-
preferred substrate
-
-
?
tyramine + H2O + O2
(4-hydroxyphenyl)acetaldehyde + NH3 + H2O2
-
-
-
?
tyramine + H2O + O2
(4-hydroxyphenyl)acetaldehyde + NH3 + H2O2
-
-
-
?
tyramine + H2O + O2
(4-hydroxyphenyl)acetaldehyde + NH3 + H2O2
-
-
-
-
?
tyramine + H2O + O2
4-hydroxyphenylacetaldehyde + NH3 + H2O2
during this reaction, an irreversible inactivation of the enzyme occurs
-
-
?
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
quantum mechanical hydrogen tunneling can be enhanced by an enzyme protein scaffold including the catalytic base that directly mediates the hydrogen transfer
-
-
?
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
high activity
-
-
?
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
-
-
-
-
?
additional information
?
-
-
no activity with dopamine, 2-aminoacetic acid, 3-aminopropanoic aid, L-Arg, L-Orn, L-Lys, L-Phe, and D-Lys
-
-
?
additional information
?
-
-
no activity with dopamine, 2-aminoacetic acid, 3-aminopropanoic aid, L-Arg, L-Orn, L-Lys, L-Phe, and D-Lys
-
-
?
additional information
?
-
-
MAO-N is a flavoenzyme that catalyses the oxidative deamination of primary amines, substrate specificity, overview
-
-
?
additional information
?
-
-
MAO-N is an FAD-dependent enzyme that catalyses the conversion of terminal amines to their corresponding aldehyde
-
-
?
additional information
?
-
-
Semicarbazide-sensitive amine oxidase acts as a vascular-adhesion protein, mediating the adhesion of lymphocytes to vascular endothelial cells under inflammatory conditions
-
-
?
additional information
?
-
the catalytic reaction proceeds via two half-reactions; the aldehyde product is released at the end of the reductive half-reaction before reduction of molecular oxygen in the oxidative half-reaction. Mechanism of molecular oxygen entry into the buried active site of the copper amine oxidase, the N-terminal domain does not affect oxygen entry, overview. The protein-derived cofactor TPQ and the off-metal O2-binding site are located in the vicinity of a conserved active-site Met699
-
-
?
additional information
?
-
-
the catalytic reaction proceeds via two half-reactions; the aldehyde product is released at the end of the reductive half-reaction before reduction of molecular oxygen in the oxidative half-reaction. Mechanism of molecular oxygen entry into the buried active site of the copper amine oxidase, the N-terminal domain does not affect oxygen entry, overview. The protein-derived cofactor TPQ and the off-metal O2-binding site are located in the vicinity of a conserved active-site Met699
-
-
?
additional information
?
-
-
the enzyme can use human granulocytes as a substrate
-
-
?
additional information
?
-
the enzyme oxidizes arginine to ammonia, urea, hydrogen peroxide and glutamate-5-semialdehyde which spontaneously cyclizes yielding DELTA1-pyrroline-5-carboxylic acid
-
-
?
additional information
?
-
-
the enzyme oxidizes arginine to ammonia, urea, hydrogen peroxide and glutamate-5-semialdehyde which spontaneously cyclizes yielding DELTA1-pyrroline-5-carboxylic acid
-
-
?
additional information
?
-
-
physiologic role for SSAO in elastin maturation
-
-
?
additional information
?
-
-
SSAO may contribute to the vascular damage associated to Alzheimer’s disease
-
-
?
additional information
?
-
synergistic interaction between semicarbazide-sensitive amine oxidase and angiotensin-converting enzyme in diabetes. Semicarbazide-sensitive amine oxidase is involved in the following biological processes: vision, inflammatory response, biogenic amine metabolism, catecholamine metabolism, amine metabolism, cell adhesion
-
-
?
additional information
?
-
semicarbazide-sensitive amine oxidases constitute a group of copper-dependent enzymes, which oxidatively deaminate primary endo- and exogenous amines
-
-
?
additional information
?
-
semicarbazide-sensitive amine oxidases constitute a group of copper-dependent enzymes, which oxidatively deaminate primary endo- and exogenous amines
-
-
?
additional information
?
-
-
semicarbazide-sensitive amine oxidases constitute a group of copper-dependent enzymes, which oxidatively deaminate primary endo- and exogenous amines
-
-
?
additional information
?
-
AOC2 is an enzymatically active cell surface SSAO with distinct substrate specificity, the preferred in vitro substrates of AOC2 are 2-phenylethylamine, tryptamine and p-tyramine, cf. EC 1.4.3.4, instead of methylamine and benzylamine, the favored substrates of AOC3. Substrate docking, molecular modeling and comparison of AOC2 and AOC3, overview. No activity of AOC2 with methylamine, polyamine spermidine, or histamine
-
-
?
additional information
?
-
AOC2 is an enzymatically active cell surface SSAO with distinct substrate specificity, the preferred in vitro substrates of AOC2 are 2-phenylethylamine, tryptamine and p-tyramine, cf. EC 1.4.3.4, instead of methylamine and benzylamine, the favored substrates of AOC3. Substrate docking, molecular modeling and comparison of AOC2 and AOC3, overview. No activity of AOC2 with methylamine, polyamine spermidine, or histamine
-
-
?
additional information
?
-
-
AOC2 is an enzymatically active cell surface SSAO with distinct substrate specificity, the preferred in vitro substrates of AOC2 are 2-phenylethylamine, tryptamine and p-tyramine, cf. EC 1.4.3.4, instead of methylamine and benzylamine, the favored substrates of AOC3. Substrate docking, molecular modeling and comparison of AOC2 and AOC3, overview. No activity of AOC2 with methylamine, polyamine spermidine, or histamine
-
-
?
additional information
?
-
substrate docking, molecular modeling and comparison of AOC2 and AOC3, overview. No activity of AOC3 with polyamine spermidine or histamine
-
-
?
additional information
?
-
substrate docking, molecular modeling and comparison of AOC2 and AOC3, overview. No activity of AOC3 with polyamine spermidine or histamine
-
-
?
additional information
?
-
-
substrate docking, molecular modeling and comparison of AOC2 and AOC3, overview. No activity of AOC3 with polyamine spermidine or histamine
-
-
?
additional information
?
-
-
the catalytic center is deeply buried within the enzyme and is accessible only through a narrow channel with a diameter of about 4.5 A. This channel is gated by the side chain of L469 which, along with the copper-TPQ coordination, controls the catalytic activity of SSAO. While specific interactions with residues lining the surface of the accessing channel are important for substrate specificity, the flexibility of substrates also plays an important role, molecular dynamics and induced docking studies, detailed overview
-
-
?
additional information
?
-
VAP-1/SSAOs convert amines into aldehydes. SSAOs are distinct from the mammalian monoamine oxidases, MAOs, but their substrate specificities are partly overlapping
-
-
?
additional information
?
-
-
VAP-1/SSAOs convert amines into aldehydes. SSAOs are distinct from the mammalian monoamine oxidases, MAOs, but their substrate specificities are partly overlapping
-
-
?
additional information
?
-
-
no activity with dimethylamide substituted indole 3-((4-[5-(aminomethyl)-2-fluorophenyl]piperidin-1-yl)carbonyl)-1-(2-methoxyethyl)-N,N-dimethyl-1H-indole-4-carboxamide
-
-
?
additional information
?
-
-
alkylamines 2-bromoethylamine and 2-chloroethylamine, and the short diamine 1,2-diaminoethane are both poor substrates and irreversible inactivators of LSAO
-
-
?
additional information
?
-
-
ethylenediamine and methylamine are no substrates for isoform AO2
-
-
?
additional information
?
-
-
T0901317 inhibits SSAO gene expression and its activity in atherogenic apoE-/- mice. The atheroprotective effect of LXR agonist T0901317 is related to the inhibition of SSAO gene expression and its activity
-
-
?
additional information
?
-
the catalytic mechanism can be divided into two half-reactions: a reductive half-reaction in which a primary amine substrate is oxidized to its corresponding aldehyde with the concomitant reduction of the organic cofactor 2,4,5-trihydroxyphenylalanine quinone and an oxidative half-reaction in which reduced 2,4,5-trihydroxyphenylalanine quinone is re-oxidized with the reduction of molecular oxygen to hydrogen peroxide
-
-
?
additional information
?
-
-
the catalytic mechanism can be divided into two half-reactions: a reductive half-reaction in which a primary amine substrate is oxidized to its corresponding aldehyde with the concomitant reduction of the organic cofactor 2,4,5-trihydroxyphenylalanine quinone and an oxidative half-reaction in which reduced 2,4,5-trihydroxyphenylalanine quinone is re-oxidized with the reduction of molecular oxygen to hydrogen peroxide
-
-
?
additional information
?
-
isoform HPAO-2 shows a clear preference for bulkier aromatic amines and isoform HPAO-1 shows a preference for short aliphatic amines
-
-
?
additional information
?
-
-
isoform HPAO-2 shows a clear preference for bulkier aromatic amines and isoform HPAO-1 shows a preference for short aliphatic amines
-
-
?
additional information
?
-
-
docking of substrates to the enzyme, the enzyme shows electrostatic control of the docking process, overview. The active site contains two negatively charged amino acid residues which seem to interact with positively charged groups of the substrate molecules
-
-
?
additional information
?
-
-
isoform AO1 isolated from butylamine-induced cells with a distinct specificity towards benzylamine (relative to phenylethylamine), acts on a broad range of aliphatic monoamines (C1-C5). Isoform AO2 isolated from phenylethylamine-treated cells displays activity towards phenylethylamine as well as tyramine and heterocyclic amines but negligible conversion of benzylamine and short chain aliphatic amines. Neither AO1 nor AO2 exhibit any measurable activity when using diamines (putrescine or cadaverine) as substrate
-
-
?
additional information
?
-
-
isoform AO1 isolated from butylamine-induced cells with a distinct specificity towards benzylamine (relative to phenylethylamine), acts on a broad range of aliphatic monoamines (C1-C5). Isoform AO2 isolated from phenylethylamine-treated cells displays activity towards phenylethylamine as well as tyramine and heterocyclic amines but negligible conversion of benzylamine and short chain aliphatic amines. Neither AO1 nor AO2 exhibit any measurable activity when using diamines (putrescine or cadaverine) as substrate
-
-
?
additional information
?
-
-
three histidine residues within the C-terminal region of Cao1 that are necessary for amine oxidase activity
-
-
?
additional information
?
-
Schizosaccharomyces pombe FY435 / ATCC 87284
-
three histidine residues within the C-terminal region of Cao1 that are necessary for amine oxidase activity
-
-
?
additional information
?
-
-
no activity with propylamine and hexylamine
-
-
?
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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
2-phenylethylamine + H2O + O2
beta-phenylethanal + NH3 + H2O2
-
-
-
?
alpha-casein + H2O + O2
?
-
the enzyme oxidizes the lysine residues in alpha-casein protein
-
-
?
tropoelastin + H2O + O2
?
-
the enzyme oxidizes the lysine residues in tropoelastin protein
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
low activity
-
-
?
ethylamine + H2O + O2
acetaldehyde + NH3 + H2O2
Schizosaccharomyces pombe FY435 / ATCC 87284
-
-
-
-
?
tryptamine + H2O + O2
(1H-indol-3-yl)acetaldehyde + NH3 + H2O2
-
-
-
-
?
tryptamine + H2O + O2
(1H-indol-3-yl)acetaldehyde + NH3 + H2O2
-
-
-
?
additional information
?
-
-
MAO-N is a flavoenzyme that catalyses the oxidative deamination of primary amines, substrate specificity, overview
-
-
?
additional information
?
-
-
Semicarbazide-sensitive amine oxidase acts as a vascular-adhesion protein, mediating the adhesion of lymphocytes to vascular endothelial cells under inflammatory conditions
-
-
?
additional information
?
-
-
physiologic role for SSAO in elastin maturation
-
-
?
additional information
?
-
-
SSAO may contribute to the vascular damage associated to Alzheimer’s disease
-
-
?
additional information
?
-
synergistic interaction between semicarbazide-sensitive amine oxidase and angiotensin-converting enzyme in diabetes. Semicarbazide-sensitive amine oxidase is involved in the following biological processes: vision, inflammatory response, biogenic amine metabolism, catecholamine metabolism, amine metabolism, cell adhesion
-
-
?
additional information
?
-
semicarbazide-sensitive amine oxidases constitute a group of copper-dependent enzymes, which oxidatively deaminate primary endo- and exogenous amines
-
-
?
additional information
?
-
semicarbazide-sensitive amine oxidases constitute a group of copper-dependent enzymes, which oxidatively deaminate primary endo- and exogenous amines
-
-
?
additional information
?
-
-
semicarbazide-sensitive amine oxidases constitute a group of copper-dependent enzymes, which oxidatively deaminate primary endo- and exogenous amines
-
-
?
additional information
?
-
-
the catalytic center is deeply buried within the enzyme and is accessible only through a narrow channel with a diameter of about 4.5 A. This channel is gated by the side chain of L469 which, along with the copper-TPQ coordination, controls the catalytic activity of SSAO. While specific interactions with residues lining the surface of the accessing channel are important for substrate specificity, the flexibility of substrates also plays an important role, molecular dynamics and induced docking studies, detailed overview
-
-
?
additional information
?
-
VAP-1/SSAOs convert amines into aldehydes. SSAOs are distinct from the mammalian monoamine oxidases, MAOs, but their substrate specificities are partly overlapping
-
-
?
additional information
?
-
-
VAP-1/SSAOs convert amines into aldehydes. SSAOs are distinct from the mammalian monoamine oxidases, MAOs, but their substrate specificities are partly overlapping
-
-
?
additional information
?
-
-
T0901317 inhibits SSAO gene expression and its activity in atherogenic apoE-/- mice. The atheroprotective effect of LXR agonist T0901317 is related to the inhibition of SSAO gene expression and its activity
-
-
?
additional information
?
-
the catalytic mechanism can be divided into two half-reactions: a reductive half-reaction in which a primary amine substrate is oxidized to its corresponding aldehyde with the concomitant reduction of the organic cofactor 2,4,5-trihydroxyphenylalanine quinone and an oxidative half-reaction in which reduced 2,4,5-trihydroxyphenylalanine quinone is re-oxidized with the reduction of molecular oxygen to hydrogen peroxide
-
-
?
additional information
?
-
-
the catalytic mechanism can be divided into two half-reactions: a reductive half-reaction in which a primary amine substrate is oxidized to its corresponding aldehyde with the concomitant reduction of the organic cofactor 2,4,5-trihydroxyphenylalanine quinone and an oxidative half-reaction in which reduced 2,4,5-trihydroxyphenylalanine quinone is re-oxidized with the reduction of molecular oxygen to hydrogen peroxide
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,4,5-trihydroxyphenylalanine quinone
-
i.e. TPQ, covalently bound cofactor, one per monomer, generated by posttranslational modification of the first conserved tyrosine residue in the consensus sequence Asn-Tyr-(Glu/Asp)-Tyr
2,4,5-trihydroxyphenylalaninequinone
i.e. TPQ cofactor, the cofactor is spontaneously formed by post-translational modifications of active site amino-acid residues
FAD
-
flavoenzyme, a hydrophobic cavity extends from the protein surface to the active site, where a noncovalently bound FAD sits at the base of an aromatic cage, the sides of which are formed by Trp430 and Phe466, binding structure, overview
additional information
-
no evidences of topaquinone cofactor involvement
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
calcium is the normal ligand of these peripheral sites. Enzyme activity is stimulated by 3 mM. Removal of the not solvent exposed calcium ion with EDTA results in a 60-90% reduction in enzyme activity
Co2+
Cobalt
-
the Km-value for O2 of the cobalt-substituted enzyme form is approximately 70fold higher than that of the copper-containing wild-type enzyme
copper
Cu
-
only the copper-containing homodimer is capable of rapid reoxidation and the zinc-copper heterodimers are incapable of rapid turnover at either subunit
Cu2+
Ni2+
Zn
-
the presence of substantial amount of zinc results in two distinctive enzyme species, designated as the fast and slow enzymes. Both forms are rapidly reduced by substrate methylamine with a rate constant of 199/s but behave differently in their oxidation rates. The fast enzyme is oxidized by dioxygen at a rate of 22.1/s, whereas the slow enzyme reacts at a rate of 0.00018/s. An investigation of the relationship between the copper content and the extent of the fast enzyme shows that only the copper-containing homodimer is capable of rapid reoxidation and the zinc-copper heterodimers are incapable of rapid turnover at either subunit
Zn2+
additional information
Co2+
enzyme reconstituted with Co2+ exhibits 2.2% of the activity of the original Cu2+ -enzyme, KM-values for amine substrate and dioxygen are comparable
Co2+
besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently. Although these noncupric metal ions can not initiate topaquinone formation under the atmospheric conditions, slow spectral changes are observed in the enzyme bound with Co2+ or Ni2+ ion under the dioxygen-saturating conditions. X-ray crystallographic analysis reveals structural identity of the active sites of Co- and Ni-activated enzymes with Cu-enzyme. Co2+ and Ni2+ ions are also capable of forming topaquinone, though much less efficiently than Cu2+
copper
-
the purified enzyme contains 2.39 mol of copper per mol of subunit
copper
-
copper depleted enzyme can be reconstituted with either Cu2+, Zn2+, Co2+, or Ni2+, 79% of activity is restored with Cu2+, 19% is restored with Co2+, 1.7% with Zn2+ or Ni2+
copper
-
study of cupric ions by magnetic-resonance and kinetic methods, native enzyme contains 2 tightly bound Cu2+ ions
copper
-
contains 8 Cu2+ per 1200000 Da, Co2+, Zn2+ and Ni2+ can replace Cu2+, no effect of Mn2+
Cu2+
copper protein. The native Cu2+ has essential roles such as catalyzing the electron transfer between the aminoresorcinol form of the reduced topaquinone cofactor and dioxygen, in part by providing a binding site for 1e- and 2e- reduced dioxygen species to be efficiently protonated and released and also preventing the back reaction between the product aldehyde and the aminoresorcinol form of the reduced topaquinone cofactor and dioxygen
Cu2+
besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently. Although these noncupric metal ions can not initiate topaquinone formation under the atmospheric conditions, slow spectral changes are observed in the enzyme bound with Co2+ or Ni2+ ion under the dioxygen-saturating conditions. X-ray crystallographic analysis reveals structural identity of the active sites of Co- and Ni-activated enzymes with Cu-enzyme. Co2+ and Ni2+ ions are also capable of forming topaquinone, though much less efficiently than Cu2+
Cu2+
the wild type enzyme contains 1 mol copper per mol of subunit, copper is the most efficient catalytic metal
Cu2+
the enzyme contains one non-blue copper type 2 ion as an inorganic cofactor
Cu2+
required for activity, the zinc content is 0.4 mol per mole of AOC3 monomer
Cu2+
required for activity, after overnight incubation with 0.1 mM CuSO4, isoform AMAO3 shows slightly enhanced activity (114% of untreated enzyme activity)
Cu2+
required for activity, after overnight incubation with 0.1 mM CuSO4, there is no change in the activity of isoform AMAO2
Ni2+
enzyme reconstituted with Co2+ exhibits 0.9% of the activity of the original Cu2+ -enzyme, KM-values for amine substrate and dioxygen are comparable
Ni2+
besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently. Although these noncupric metal ions can not initiate topaquinone formation under the atmospheric conditions, slow spectral changes are observed in the enzyme bound with Co2+ or Ni2+ ion under the dioxygen-saturating conditions. X-ray crystallographic analysis reveals structural identity of the active sites of Co- and Ni-activated enzymes with Cu-enzyme. Co2+ and Ni2+ ions are also capable of forming topaquinone, though much less efficiently than Cu2+
Zn2+
besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(4-[[(2E)-4-amino-2-fluorobut-2-en-1-yl]oxy]phenyl)(pyrrolidin-1-yl)methanone
-
-
2-(4-[2-[2-(acetylamino)-2,3-dihydro-1,3-thiazol-4-yl]ethyl]phenyl)-N-[amino(imino)methyl]acetamide
-
-
3,3'-[[4-(aminomethyl)pyridine-3,5-diyl]bis(oxy)]dipropan-1-ol dihydrochloride
-
-
3-(4-methoxy-3-nitrophenyl)-3-pyrroline
-
0.015 mM, inactivation of BPAO by 3-aryl-3-pyrrolines
3-(4-methoxyphenyl)-2,5-dihydro-1H-pyrrole hydrochloride
-
0.4 mM, inactivation of BPAO by 3-aryl-3-pyrrolines
3-(4-methoxyphenyl)-N-methyl-5-(1H-pyrrol-2-yl)-4,5-dihydro-1H-pyrazole-1-carbothioamide
-
-
3-biphenyl-4-yl-2,5-dihydro-1H-pyrrole hydrochloride
-
0.1 mM, inactivation of BPAO by 3-aryl-3-pyrrolines
3-naphthalen-1-yl-2,5-dihydro-1H-pyrrole hydrochloride
-
0.4 mM, inactivation of BPAO by 3-aryl-3-pyrrolines
4-(2,5-dihydro-1H-pyrrol-3-yl)-N,N-dimethylaniline hydrochloride
-
0.4 mM, inactivation of BPAO by 3-aryl-3-pyrrolines
4-(aminomethyl)-2-benzyl-5-(ethylamino)pyridazin-3(2H)-one
-
below 10% inhibition at 0.5 mM
4-(aminomethyl)-2-methyl-5-(morpholin-4-yl)pyridazin-3(2H)-one
-
93% inhibition at 0.5 mM
4-(aminomethyl)-2-methyl-5-(pyrrolidin-1-yl)pyridazin-3(2H)-one
-
below 10% inhibition at 0.5 mM
4-(aminomethyl)-5-(ethylamino)-2-methylpyridazin-3(2H)-one
-
13% inhibition at 0.5 mM
4-(aminomethyl)-N,N-diethylpyridazine-3,5-diamine
-
over 99% inhibition at 0.5 mM
Br-
uncompetitive inhibitor with respect to the substrate amine and noncompetitive inhibitor with respect to dissolved oxygen
Cl-
uncompetitive inhibitor with respect to the substrate amine and noncompetitive inhibitor with respect to dissolved oxygen
F-
uncompetitive inhibitor with respect to the substrate amine and noncompetitive inhibitor with respect to dissolved oxygen
geraniin
-
competitive inhibition. Inhibitory activities of 10.87%, 37.24%, 77.67%, and 95.77%, respectively, for 0.00066, 0.00164, 0.00328, and 0.00656 mM of geraniin
histamine
substrate inhibition; substrate inhibition
I-
uncompetitive inhibitor with respect to the substrate amine and noncompetitive inhibitor with respect to dissolved oxygen
L-Lys
-
the presence of L-lysine during the oxidation of benzylamine results in time- and dose-dependent inhibition of SSAO activity, in a process that is dependent on the H2O2 formed during benzylamine oxidation
N-allyl-3-(4-methoxyphenyl)-5-(1H-pyrrol-2-yl)-4,5-dihydro-1H-pyrazole-1-carbothioamide
-
-
N-ethyl-3-(4-methoxyphenyl)-5-(1H-pyrrol-2-yl)-4,5-dihydro-1H-pyrazole-1-carbothioamide
-
-
N-[4-(2-[4-[(2-amino-1H-imidazol-5-yl)methyl]phenyl]ethyl)-1,3-thiazol-2-yl]acetamide
-
-
N-[4-[2-(4-carbamimidamidophenyl)ethyl]-5-(4-sulfamoylbenzyl)-1,3-thiazol-2-yl]acetamide
-
-
N-[4-[2-(4-[[amino(imino)methyl]amino]phenyl)ethyl]-1,3-thiazol-2-yl]acetamide
-
-
o-phenylenediamine
-
0.2 mM, 33% inhibition of dimeric enzyme, 26% inhibition of tetrameric enzyme
p-chloromercuriphenylsulfonate
-
0.1 mM, complete inhibition of enzyme from cultured aortic smooth muscle cells
ruthenium(II) molecular wires
the enzyme is reversibly inhibited by molecular wires comprising a Ru(II) complex head group and an aromatic tail group joined by an alkane linker
-
(Z)-3-fluoro-2-(4-methoxybenzyl)allylamine hydrochloride
-
i.e. LJP 1586. Potent, specific, and orally available inhibitor of SSAO activity is an effective anti-inflammatory compound in vivo
(Z)-3-fluoro-2-(4-methoxybenzyl)allylamine hydrochloride
-
i.e. LJP 1586. Potent, specific, and orally available inhibitor of SSAO activity is an effective anti-inflammatory compound in vivo
(Z)-3-fluoro-2-(4-methoxybenzyl)allylamine hydrochloride
-
i.e. LJP 1586. Potent, specific, and orally available inhibitor of SSAO activity is an effective anti-inflammatory compound in vivo
1,4-diamino-2-butyne
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
-
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
-
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
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
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
-
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
-
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
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
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
-
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
-
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
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
1,6-diamino-2,4-hexadiyne
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
1,6-diamino-2,4-hexadiyne
-
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
1,6-diamino-2,4-hexadiyne
-
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
1,6-diamino-2,4-hexadiyne
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
2-Bromoethylamine
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
2-Bromoethylamine
-
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
2-Bromoethylamine
-
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
2-Bromoethylamine
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
3,3-bis(aminoethyl)-1-hydroxy-2-oxo-1-triazene
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
3,3-bis(aminoethyl)-1-hydroxy-2-oxo-1-triazene
-
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
3,3-bis(aminoethyl)-1-hydroxy-2-oxo-1-triazene
-
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
3,3-bis(aminoethyl)-1-hydroxy-2-oxo-1-triazene
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
3-cycloheptylamino-4-aminomethylpyridine dihydrochloride monohydrate
-
3-cyclohexylmethylamino-4-aminomethylpyridine dihydrochloride monohydrate
-
3-cyclohexylmethylamino-4-aminomethylpyridine dihydrochloride monohydrate
-
3-cyclopentylamino-4-aminomethylpyridine dihydrochloride hemihydrate
-
3-cyclopropylamino-4-aminomethylpyridine dihydrochloride sesquihydrate
-
8-hydroxyquinoline
non-competitive inhibitor; non-competitive inhibitor; non-competitive inhibitor
aminoguanidine
irreversible competitive inhibitor; irreversible competitive inhibitor; irreversible competitive inhibitor
aminoguanidine
-
strongly inhibits adipocyte semicarbazide-sensitive amine oxidase and slightly reduces fat deposition in obese Zucker rats. Aminoguanidine may be useful for treating obesity via its SSAO blocking properties
aminoguanidine
-
isoform AO1 shows 18% residual activity at 0.1 mM, isoform AO2 shows 17% residual activity at 0.1 mM
benzylhydrazine
forms adducts with the TPQ cofactor, binding structure, overview
Cuprizone
-
copper chelating, 0.006 mM, 98% inhibition, competitive vs. benzylamine
Cuprizone
-
isoform AO1 shows 2% residual activity at 0.1 mM, isoform AO2 shows 1% residual activity at 0.1 mM
hydroxylamine
-
elicits hypotension in the rat. This effect is due in part to its conversion to nitric oxide and in part to a hydralazine-like action involving SSAO inhibition
isoniazid
-
0.2 mM, 42% inhibition of dimeric enzyme, 39% inhibition of tetrameric enzyme
isoniazid
-
isoform AO1 shows 14% residual activity at 0.1 mM, isoform AO2 shows 16% residual activity at 0.1 mM
N6-(4-aminobut-2-ynyl)adenine
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
N6-(4-aminobut-2-ynyl)adenine
-
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
N6-(4-aminobut-2-ynyl)adenine
-
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
N6-(4-aminobut-2-ynyl)adenine
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
NaN3
-
azide binds to Cu2+ ions, competitive inhibition vs. O2, uncompetitive vs. benzylamine
Phenelzine
-
0.001 mM, complete inhibition of enzyme from cultured aortic smooth muscle cells
phenylhydrazine
-
irreversible inactivation most likely due to hydrazone formation
Semicarbazide
-
0.2 mM, 49% inhibition of dimeric enzyme, 45% inhibition of tetrameric enzyme
Semicarbazide
causes significant decreases in the oxidative deamination activity of four among the five substrates catalyzed by SSAO
Semicarbazide
-
irreversible inhibitor. Pargyline + semicarbazide-induced reduction of fat deposition results from decreased food intake and from impaired MAO (EC 1.4.3.4) and SSAO-dependent lipogenic and antilipolytic actions of endogenous or alimentary amines
Semicarbazide
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isoform AO1 shows 1% residual activity at 0.1 mM, isoform AO2 shows 2% residual activity at 0.1 mM
Semicarbazide
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0.01 mM, complete inhibition of enzyme from cultured aortic smooth muscle cells
tranylcypromine
forms adducts with the TPQ cofactor, also termed (1R,2S)-rel-2-phenylcyclopropanamine, is a mixture of (1R,2S)-2-phenylcyclopropanamine and (1S,2R)-2-phenylcyclopropanamine, binding structure, overview
tryptamine
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
tryptamine
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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
tryptamine
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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
tryptamine
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
tyramine
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
tyramine
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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
tyramine
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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
tyramine
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
additional information
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not inhibited by MgCl2, MnCl2, CoCl2, ZnCl2, FeCl3, sodium azide, N-ethylmaleimide, and iodoacetate
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additional information
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3-pyrrolines are mechanism-based inactivators of the quinone-dependent amine oxidases but only substrates of the flavin-dependent amine oxidases
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additional information
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not inhibited by 2-aminoethanol and 2-(N,N-dimethylamino)ethanethiol
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additional information
synthesis and in vitro activities of a series of VAP-1 selective inhibitors, molecular dynamics simulations and docking studies, pIC50 values, overview. Movements of Met211, Ser496, and especially Leu469 can enlarge the ligand-binding pocket, allowing larger ligands than those seen in the crystal structures to bind. Three-dimensional quantitative structure-activity relationship models for VAP-1 in comparison to MAOs, overview
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additional information
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synthesis and in vitro activities of a series of VAP-1 selective inhibitors, molecular dynamics simulations and docking studies, pIC50 values, overview. Movements of Met211, Ser496, and especially Leu469 can enlarge the ligand-binding pocket, allowing larger ligands than those seen in the crystal structures to bind. Three-dimensional quantitative structure-activity relationship models for VAP-1 in comparison to MAOs, overview
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additional information
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no effect: DTT or EDTA at 1 mM, 1,4-diamino-2-butanone, sodium azide or KCN
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additional information
the enzyme activity is not significantly affected in the presence of 5 mM EDTA; the enzyme activity is not significantly affected in the presence of 5 mM EDTA
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additional information
the enzyme activity is not significantly affected in the presence of 5 mM EDTA; the enzyme activity is not significantly affected in the presence of 5 mM EDTA
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additional information
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the enzyme activity is not significantly affected in the presence of 5 mM EDTA; the enzyme activity is not significantly affected in the presence of 5 mM EDTA
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additional information
clorgyline and deprenyl do not significantly inhibit the activities
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additional information
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no inhibition by pargyline. SSAO activity remains unchanged during starvation
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additional information
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not inhibited by pargyline, clorgyline, and neocupine
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Atx1-like protein
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required for the synthesis of fully active Cao1
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additional information
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SSAO activity remains unchanged during starvation
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additional information
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active Cao1 requires Ctr4/5-mediated copper transport and the transcription factor Cuf1
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.13
4-fluorobenzylamine
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isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
2.05
ethanolamine
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isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
0.03
octopamine
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isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
0.02
vanillylamine
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isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
0.0012
2-Phenylethylamine
wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 25°C
0.0019
2-Phenylethylamine
pH 6.8, 30°C, Co2+-substituted enzyme