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1,3-diaminopropane + H2O + O2
3-aminopropanal + NH3 + H2O2
-
-
-
-
?
1,4-diamino-2-butyne + H2O + O2
?
1,4-diamino-2-chloro-2-butene + H2O + O2
?
1,4-diaminobutane + H2O + O2
?
-
enzyme II shows 23% activity and enzyme III 12% activity compared to 4-aminobutanamide
-
-
?
1,5-diamino-2-pentyne + H2O + O2
?
1,5-diaminopentane + H2O + O2
?
-
enzyme II shows 5% activity and enzyme III 31% activity compared to 4-aminobutanamide
-
-
?
1,6-diamino-2,4-hexadiyne + H2O + O2
?
1,8-diaminooctane + H2O + O2
?
-
-
-
-
?
1-(3-fluoro-4-methylphenyl)methanamine + H2O + O2
? + NH3 + H2O2
1-(4-fluorophenyl)methanamine + H2O + O2
? + NH3 + H2O2
1-aminobutane + H2O + O2
butanal + NH3 + H2O2
-
-
-
-
?
1-aminoheptane + H2O + O2
heptanal + NH3 + H2O2
-
-
-
-
?
1-aminohexane + H2O + O2
hexanal + NH3 + H2O2
-
-
-
-
?
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-aminooctane + H2O + O2
octanal + NH3 + H2O2
-
-
-
-
?
1-aminopentane + H2O + O2
pentanal + NH3 + H2O2
-
-
-
-
?
1-methyl-3-phenylpropylamine + H2O + O2
4-phenylbutan-2-one + NH3 + H2O2
-
-
-
-
?
1-methylhistamine + O2 + H2O
?
-
-
-
?
2-aminoethylpyridine + H2O + O2
pyridine-2-carbaldehyde + NH3 + H2O2
-
-
-
?
2-bromoethylamine + H2O + O2
bromoacetaldehyde + NH3 + H2O2
2-phenylethanamine + H2O + O2
? + NH3 + H2O2
2-phenylethylamine + H2O + O2
2-phenylacetaldehyde + NH3 + H2O2
-
-
-
-
?
2-phenylethylamine + H2O + O2
2-phenylethanal + NH3 + H2O2
2-phenylethylamine + H2O + O2
?
-
-
-
?
2-phenylethylamine + H2O + O2
beta-phenylethanal + NH3 + H2O2
-
-
-
?
2-phenylethylamine + H2O + O2
phenylacetaldehyde + NH3 + H2O2
3,3-bis(aminoethyl)-1-hydroxy-2-oxo-1-triazene + H2O + O2
?
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
-
-
?
3-phenylpropan-1-amine + H2O + O2
? + NH3 + H2O2
4-(aminomethyl)-N-[3-(aminomethyl)benzyl]benzamide + H2O + O2
? + NH3 + H2O2
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-aminomethylpyridine dihydrochloride + H2O + O2
?
4-fluorobenzylamine + H2O + O2
4-fluorobenzaldehyde + NH3 + H2O2
-
-
-
-
?
4-N,N-dimethylaminomethyl benzylamine + H2O + O2
?
-
-
-
-
?
4-phenylbutan-1-amine + H2O + O2
? + NH3 + H2O2
4-phenylbutylamine + H2O + O2
4-phenylbutanal + NH3 + H2O2
4-tyramine + H2O + O2
(4-hydroxyphenyl)acetaldehyde + 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
-
-
?
5-hydroxytryptamine + H2O + O2
?
agmatine + H2O + O2
?
-
-
-
?
allyl [3-(aminomethyl)benzyl]carbamate + H2O + O2
? + NH3 + H2O2
alpha-casein + H2O + O2
?
-
the enzyme oxidizes the lysine residues in alpha-casein protein
-
-
?
aminoacetone + H2O + O2
methylglyoxal + NH3 + H2O2
amphetamine + H2O + O2
1-phenylpropan-2-one + NH3 + H2O2
-
-
-
-
?
amylamine + H2O + O2
pentanal + NH3 + H2O2
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
benzylamine + O2 + H2O
benzaldehyde + NH3 + H2O2
-
-
-
?
beta-phenylethylamine + H2O + O2
beta-phenylethanal + NH3 + H2O2
-
-
-
?
beta-phenylethylamine + O2 + H2O
beta-phenylethanal + NH3 + H2O2
-
-
-
?
butylamine + H2O + O2
butanal + NH3 + H2O2
cadaverine + H2O + O2
DELTA1-piperideine + NH3 + H2O2
best substrate
-
-
?
cyclohexanemethylamine + H2O + O2
cyclohexanecarbaldehyde + NH3 + H2O2
-
-
-
?
cysteamine + H2O + O2
sulfanylacetaldehyde + NH3 + H2O2
-
-
-
?
dopamine + H2O + O2
(3,4-dihydroxyphenyl)acetaldehyde + NH3 + H2O2
dopamine + H2O + O2
?
-
-
-
?
ethanolamine + H2O + O2
glycolaldehyde + NH3 + H2O2
ethylamine + H2O + O2
acetaldehyde + NH3 + H2O2
ethylamine + H2O + O2
ethanal + NH3 + H2O2
-
-
-
-
?
hexakis(benzylammonium) decavanadate (V) dihydrate + H2O + O2
?
histamine + H2O + O2
(imidazol-4-yl)acetaldehyde + NH3 + H2O2
histamine + H2O + O2
1H-imidazol-4-ylacetaldehyde + NH3 + H2O2
isoamylamine + H2O + O2
isoamylaldehyde + NH3 + H2O2
isobutylamine + H2O + O2
isobutyraldehyde + NH3 + H2O2
-
-
-
?
isopentylamine + H2O + O2
isopentylaldehyde + NH3 + H2O2
-
-
-
-
?
methyl 1-(2-methoxyethyl)-3-(trifluoroacetyl)-1H-indole-4-carboxylate + H2O + O2
?
-
-
-
-
?
methylamine + H2O + O2
formaldehyde + NH3 + H2O2
methylamine + H2O + O2
methanal + NH3 + H2O2
methylbenzylamine + H2O + O2
methylbenzaldehyde + NH3 + H2O2
-
-
-
-
?
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
-
-
?
N-[3-(aminomethyl)benzyl]-4-bromobenzamide + H2O + O2
? + NH3 + H2O2
N-[3-(aminomethyl)benzyl]acetamide + H2O + O2
? + NH3 + H2O2
N-[3-(aminomethyl)benzyl]benzamide + H2O + O2
? + NH3 + H2O2
N-[3-(aminomethyl)benzyl]propanamide + H2O + O2
? + NH3 + H2O2
N6-(4-aminobut-2-ynyl)adenine + H2O + O2
?
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
-
-
?
phenethylamine + H2O + O2
phenylacetaldehyde + NH3 + H2O2
-
-
-
?
phenylethyl amine + H2O + O2
phenylethanal + NH3 + H2O2
-
-
-
-
?
phenylethylamine + H2O + O2
phenylacetaldehyde + NH3 + H2O2
propylamine + H2O + O2
propanal + NH3 + H2O2
putrescine + H2O + O2
4-aminobutanal + NH3 + H2O2
putrescine + H2O + O2
4-aminobutyraldehyde + NH3 + H2O2
-
-
-
-
?
pyrrolidine + 2,4,5-trihydroxyphenylalanine quinone + H2O + O2
? + H2O2 + NH3
-
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
sec-butylamine + H2O + O2
butan-2-one + NH3 + H2O2
-
-
-
-
?
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
-
-
?
spermine + H2O + O2
? + NH3 + H2O2
good substrate
-
-
?
tropoelastin + H2O + O2
?
-
the enzyme oxidizes the lysine residues in tropoelastin protein
-
-
?
tryptamine + H2O + O2
(1H-indol-3-yl)acetaldehyde + NH3 + H2O2
tryptamine + H2O + O2
1H-indol-3-ylacetaldehyde + NH3 + H2O2
tyramine + H2O + O2
(4-hydroxyphenyl)acetaldehyde + NH3 + H2O2
tyramine + H2O + O2
4-hydroxyphenylacetaldehyde + NH3 + H2O2
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
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
-
-
?
tyramine + O2 + H2O
4-hydroxyphenylethanal + NH3 + H2O2
-
-
-
?
vanillylamine + H2O + O2
vanillic aldehyde + NH3 + H2O2
-
-
-
-
?
additional information
?
-
1,4-diamino-2-butyne + H2O + O2
?
-
-
-
?
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-butyne + H2O + O2
?
-
-
-
-
?
1,4-diamino-2-butyne + H2O + O2
?
-
-
-
?
1,4-diamino-2-chloro-2-butene + H2O + O2
?
-
-
-
?
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
-
-
?
1,4-diamino-2-chloro-2-butene + H2O + O2
?
-
-
-
-
?
1,4-diamino-2-chloro-2-butene + H2O + O2
?
-
-
-
?
1,5-diamino-2-pentyne + H2O + O2
?
-
-
-
?
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
-
-
?
1,5-diamino-2-pentyne + H2O + O2
?
-
-
-
-
?
1,5-diamino-2-pentyne + H2O + O2
?
-
-
-
?
1,6-diamino-2,4-hexadiyne + H2O + O2
?
-
-
-
?
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
-
-
?
1,6-diamino-2,4-hexadiyne + H2O + O2
?
-
-
-
-
?
1,6-diamino-2,4-hexadiyne + H2O + O2
?
-
-
-
?
1-(3-fluoro-4-methylphenyl)methanamine + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
1-(3-fluoro-4-methylphenyl)methanamine + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
1-(4-fluorophenyl)methanamine + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
1-(4-fluorophenyl)methanamine + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
2-bromoethylamine + H2O + O2
bromoacetaldehyde + NH3 + H2O2
-
-
-
?
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-bromoethylamine + H2O + O2
bromoacetaldehyde + NH3 + H2O2
-
-
-
-
?
2-bromoethylamine + H2O + O2
bromoacetaldehyde + NH3 + H2O2
-
-
-
?
2-phenylethanamine + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
2-phenylethanamine + H2O + O2
? + 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
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
?
-
-
-
?
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
-
-
?
3,3-bis(aminoethyl)-1-hydroxy-2-oxo-1-triazene + H2O + O2
?
-
-
-
-
?
3,3-bis(aminoethyl)-1-hydroxy-2-oxo-1-triazene + H2O + O2
?
-
-
-
?
3-phenylpropan-1-amine + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
3-phenylpropan-1-amine + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
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-phenylbutan-1-amine + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
4-phenylbutan-1-amine + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
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
-
-
?
allyl [3-(aminomethyl)benzyl]carbamate + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
allyl [3-(aminomethyl)benzyl]carbamate + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
aminoacetone + H2O + O2
methylglyoxal + NH3 + H2O2
-
-
-
-
?
aminoacetone + H2O + O2
methylglyoxal + NH3 + H2O2
-
-
-
?
amylamine + H2O + O2
pentanal + NH3 + H2O2
-
-
-
?
amylamine + H2O + O2
pentanal + NH3 + H2O2
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
-
-
?
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
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
best substrate
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
low activity
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
best oxidized substrate
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
best oxidized substrate
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
-
686052, 686264, 687077, 688484, 688489, 688553, 688603, 689375, 689376, 705350, 712188 -
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
main substrate for isoform AO1
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
main substrate for isoform AO1
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
-
-
-
?
butylamine + H2O + O2
butanal + NH3 + H2O2
-
-
-
?
butylamine + H2O + O2
butanal + NH3 + H2O2
-
-
-
-
?
cadaverine + H2O + O2
?
-
-
-
?
cadaverine + H2O + O2
?
-
-
-
?
cadaverine + H2O + O2
?
-
-
-
-
?
dopamine + H2O + O2
(3,4-dihydroxyphenyl)acetaldehyde + NH3 + H2O2
-
-
-
-
?
dopamine + H2O + O2
(3,4-dihydroxyphenyl)acetaldehyde + NH3 + H2O2
-
-
-
-
?
ethanolamine + H2O + O2
glycolaldehyde + NH3 + H2O2
-
-
-
-
?
ethanolamine + H2O + O2
glycolaldehyde + NH3 + H2O2
-
-
-
-
?
ethanolamine + H2O + O2
glycolaldehyde + NH3 + H2O2
-
-
-
-
?
ethylamine + H2O + O2
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
-
-
-
?
ethylamine + H2O + O2
acetaldehyde + NH3 + H2O2
-
-
-
-
?
ethylamine + H2O + O2
acetaldehyde + NH3 + H2O2
-
-
-
?
ethylamine + H2O + O2
acetaldehyde + NH3 + H2O2
-
isoforms AO1 and AO2 show 100% activity with ethylamine
-
-
?
ethylamine + H2O + O2
acetaldehyde + NH3 + H2O2
-
-
-
-
?
ethylamine + H2O + O2
acetaldehyde + NH3 + H2O2
-
-
-
-
?
hexakis(benzylammonium) decavanadate (V) dihydrate + H2O + O2
?
-
-
-
-
?
hexakis(benzylammonium) decavanadate (V) dihydrate + H2O + O2
?
-
-
-
-
?
hexakis(benzylammonium) decavanadate (V) dihydrate + H2O + O2
?
-
-
-
-
?
histamine + H2O + O2
(imidazol-4-yl)acetaldehyde + NH3 + H2O2
-
-
-
?
histamine + H2O + O2
(imidazol-4-yl)acetaldehyde + NH3 + H2O2
-
-
-
-
?
histamine + H2O + O2
(imidazol-4-yl)acetaldehyde + NH3 + H2O2
-
-
-
-
?
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
-
-
?
histamine + H2O + O2
1H-imidazol-4-ylacetaldehyde + NH3 + H2O2
-
-
-
-
?
histamine + H2O + O2
?
-
-
-
?
histamine + H2O + O2
?
-
-
-
?
isoamylamine + H2O + O2
isoamylaldehyde + NH3 + H2O2
-
-
-
-
?
isoamylamine + H2O + O2
isoamylaldehyde + NH3 + H2O2
-
-
-
?
methylamine + H2O + O2
formaldehyde + NH3 + H2O2
-
-
-
-
?
methylamine + H2O + O2
formaldehyde + NH3 + H2O2
-
-
-
?
methylamine + H2O + O2
formaldehyde + NH3 + H2O2
-
-
-
?
methylamine + H2O + O2
formaldehyde + NH3 + H2O2
-
-
-
-
?
methylamine + H2O + O2
formaldehyde + NH3 + H2O2
-
-
-
r
methylamine + H2O + O2
formaldehyde + NH3 + H2O2
-
-
-
?
methylamine + H2O + O2
formaldehyde + NH3 + H2O2
-
-
-
-
?
methylamine + H2O + O2
methanal + NH3 + H2O2
-
-
-
-
?
methylamine + H2O + O2
methanal + NH3 + H2O2
-
-
-
?
methylamine + H2O + O2
methanal + NH3 + H2O2
-
-
-
-
?
methylamine + H2O + O2
methanal + NH3 + H2O2
-
-
-
-
?
methylamine + H2O + O2
methanal + NH3 + H2O2
-
-
-
?
methylamine + H2O + O2
methanal + NH3 + H2O2
-
-
-
-
?
N-[3-(aminomethyl)benzyl]-4-bromobenzamide + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
N-[3-(aminomethyl)benzyl]-4-bromobenzamide + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
N-[3-(aminomethyl)benzyl]acetamide + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
N-[3-(aminomethyl)benzyl]acetamide + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
N-[3-(aminomethyl)benzyl]benzamide + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
N-[3-(aminomethyl)benzyl]benzamide + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
N-[3-(aminomethyl)benzyl]propanamide + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
N-[3-(aminomethyl)benzyl]propanamide + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
N6-(4-aminobut-2-ynyl)adenine + H2O + O2
?
-
-
-
?
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
-
-
?
N6-(4-aminobut-2-ynyl)adenine + H2O + O2
?
-
-
-
-
?
N6-(4-aminobut-2-ynyl)adenine + H2O + O2
?
-
-
-
?
phenylethylamine + H2O + O2
phenylacetaldehyde + NH3 + H2O2
-
-
-
-
?
phenylethylamine + H2O + O2
phenylacetaldehyde + NH3 + H2O2
-
main substrate for isoform AO2
-
-
?
phenylethylamine + H2O + O2
phenylacetaldehyde + NH3 + H2O2
-
-
-
-
?
propylamine + H2O + O2
propanal + NH3 + H2O2
-
-
-
-
?
propylamine + H2O + O2
propanal + NH3 + H2O2
-
-
-
?
propylamine + H2O + O2
propanal + NH3 + H2O2
-
-
-
-
?
putrescine + H2O + O2
4-aminobutanal + NH3 + H2O2
-
best substrate
-
-
?
putrescine + H2O + O2
4-aminobutanal + NH3 + H2O2
-
-
-
?
putrescine + H2O + O2
?
-
-
-
-
?
putrescine + H2O + O2
?
-
-
-
?
putrescine + H2O + O2
?
best substrate
-
-
?
putrescine + H2O + O2
?
-
-
-
?
putrescine + H2O + O2
?
putrescine can be oxidatively deaminated by the enzyme to corresponding aldehyde that spontaneously cyclizes yielding DELTA1-pyrroline
-
-
?
putrescine + H2O + O2
?
-
-
-
?
putrescine + H2O + O2
?
-
-
-
?
putrescine + H2O + O2
?
-
-
-
?
putrescine + H2O + O2
?
-
-
-
?
putrescine + H2O + O2
?
-
-
-
-
?
putrescine + H2O + O2
?
-
-
-
?
putrescine + H2O + O2
?
-
best substrate
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
-
-
?
spermidine + H2O + O2
?
-
-
-
-
?
spermidine + H2O + O2
?
-
-
-
?
spermidine + H2O + O2
?
-
-
-
?
spermidine + H2O + O2
?
-
-
-
?
spermidine + H2O + O2
?
-
-
-
?
spermidine + H2O + O2
?
-
-
-
?
spermidine + H2O + O2
?
-
-
-
-
?
spermine + H2O + O2
?
-
-
-
-
?
spermine + H2O + O2
?
-
-
-
?
spermine + H2O + O2
?
-
-
-
-
?
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
-
-
-
?
tryptamine + H2O + O2
(1H-indol-3-yl)acetaldehyde + NH3 + H2O2
high activity
-
-
?
tryptamine + H2O + O2
1H-indol-3-ylacetaldehyde + NH3 + H2O2
-
-
-
?
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
-
-
?
tryptamine + H2O + O2
1H-indol-3-ylacetaldehyde + NH3 + H2O2
-
-
-
-
?
tryptamine + H2O + O2
1H-indol-3-ylacetaldehyde + NH3 + H2O2
-
-
-
?
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-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
-
-
-
-
?
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
-
-
-
?
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
high activity
-
-
?
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
-
-
-
?
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
-
-
-
-
?
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
-
-
-
-
?
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
-
-
-
-
?
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
-
-
-
?
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 Alzheimers 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
?
-
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
?
-
-
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
?
-
-
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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(1R,2S)-2-(1-methylhydrazino)-1-phenylbutan-1-ol
-
(1R,2S)-2-(1-methylhydrazino)-1-phenylpentan-1-ol
-
(1R,2S)-2-(1-methylhydrazino)-1-phenylpropan-1-ol
-
(2-methylprop-2-en-1-yl)hydrazine
-
-
(2-phenylprop-2-en-1-yl)hydrazine
(2E)-3-chloroprop-2-en-1-amine
-
-
(2E)-3-fluoro-4-phenoxybut-2-en-1-amine
-
-
(2E)-4-phenoxybut-2-en-1-amine
-
-
(2Z)-3-chloroprop-2-en-1-amine
-
-
(2Z)-3-fluoro-4-phenoxybut-2-en-1-amine
-
-
(2Z)-4-phenoxybut-2-en-1-amine
-
-
(4-[[(2E)-4-amino-2-fluorobut-2-en-1-yl]oxy]phenyl)(pyrrolidin-1-yl)methanone
-
-
(Z)-3-fluoro-2-(4-methoxybenzyl)allylamine hydrochloride
1,4-diamino-2-chloro-2-butene
1,6-diamino-2,4-hexadiyne
1-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-2-(1-methylhydrazino)-ethanol
-
1-(2,5-dihydro-1H-pyrrol-3-yl)isoquinoline
-
-
1-(2-(3-chlorophenyl)-2-methoxyethyl)-1-methylhydrazine
-
1-(2-chlorophenyl)-2-(1-methylhydrazino)ethanol
-
1-(2-phenylpropyl)hydrazine
-
1-(3,5-diethoxypyridin-4-yl)methanamine dihydrochloride
1-(3-methoxyphenyl)-2-(1-methylhydrazino)ethanol
-
1-(4-chlorophenyl)-2-(1-methylhydrazino)ethanol
-
1-(4-fluorophenyl)-2-(1-methylhydrazino)ethanol
-
1-(4-methoxyphenyl)-2-(1-methylhydrazino)ethanol
-
1-(isoquinolin-1-ylcarbonyl)pyrrolidine-2-carboxamide
-
-
1-benzyl-1-methylhydrazine
-
1-ethyl-1-(2-phenylethyl)hydrazine
-
1-ethyl-1-[2-(3,4,5-trimethoxyphenyl)ethyl]hydrazine
-
1-ethyl-1-[2-(4-methoxyphenyl)ethyl]hydrazine
-
1-ethyl-2-[2-(4-fluorophenyl)prop-2-en-1-yl]hydrazine
-
-
1-isobutyl-1-(2-phenylethyl)hydrazine
-
1-isobutyl-1-[2-(4-methoxyphenyl)ethyl]hydrazine
-
1-methyl-1-(2-phenylethyl)hydrazine
-
1-methyl-1-(2-phenylpropyl)hydrazine
-
1-methyl-1-(3-phenylpropyl)hydrazine
-
1-[2-(2,3,4-trimethoxyphenyl)ethyl]-1-methylhydrazine
-
1-[2-(2,5-dimethoxyphenyl)ethyl]-1-methylhydrazine
-
1-[2-(2-chlorophenyl)ethyl]-1-methylhydrazine
-
1-[2-(2-fluorophenyl)ethyl]-1-methylhydrazine
-
1-[2-(2-methoxyphenyl)ethyl]-1-methylhydrazine
-
1-[2-(3,4,5-trimethoxyphenyl)ethyl]-1-methylhydrazine
-
1-[2-(3,4-dimethoxyphenyl)ethyl]-1-methylhydrazine
-
1-[2-(3-chlorophenyl)ethyl]-1-methylhydrazine
-
1-[2-(3-fluorophenyl)-2-methoxyethyl]-1-methylhydrazine
-
1-[2-(3-methoxyphenyl)ethyl]-1-methylhydrazine
-
1-[2-(4-chlorophenyl)-2-methoxyethyl]-1-methylhydrazine
-
1-[2-(4-chlorophenyl)ethyl]-1-methylhydrazine
-
1-[2-(4-fluorophenyl)-2-methoxyethyl]-1-methylhydrazine
-
1-[2-(4-fluorophenyl)ethyl]-1-methylhydrazine
-
1-[2-(4-fluorophenyl)prop-2-en-1-yl]-2-methylhydrazine
-
-
1-[2-(4-methoxyphenyl)ethyl]-1-methylhydrazine
-
1-[2-benzyloxy-2-(4-methoxyphenyl)ethyl]-1-methylhydrazine
-
1-[2-methoxy-1-(3-tolyl)ethyl]-1-methylhydrazine
-
1-[2-methoxy-1-(4-methoxyphenyl)ethyl]-1-methylhydrazine
-
1-[2-methoxy-2-(1-naphthyl)ethyl]-1-methylhydrazine
-
1-[2-methoxy-2-(2,3,4-trimethoxyphenyl)ethyl]-1-methylhydrazine
-
1-[2-methoxy-2-(2-naphthyl)ethyl]-1-methylhydrazine
-
1-[2-methoxy-2-(3-methoxyphenyl)ethyl]-1-methylhydrazine
-
1-[3,5-bis(ethylsulfanyl)pyridin-4-yl]methanamine dihydrochloride
-
-
1-[3,5-bis(tert-butylsulfanyl)pyridin-4-yl]methanamine dihydrochloride
-
-
1-[3-(benzyloxy)-5-ethoxypyridin-4-yl]methanamine dihydrochloride
-
-
2,2-dimethyl-2-(1-methylhydrazino)-1-phenylethanol
-
2,6-bis(1-methylethoxy)benzylamine
-
-
2,6-bis(2-hydroxyethoxy)benzylamine
-
-
2,6-bis(3-hydroxypropoxy)benzylamine
-
-
2,6-bis(4-hydroxybutoxy)benzylamine
-
-
2,6-bis(ethoxymethyl)benzylamine
-
-
2,6-bis(methoxymethyl)benzylamine
-
-
2,6-dibutoxybenzylamine
-
-
2,6-dibutylbenzylamine
-
-
2,6-diethoxybenzylamine
-
-
2,6-diethylbenzylamine
-
-
2,6-dihydroxybenzylamine
-
-
2,6-dimethoxybenzylamine
-
-
2,6-dipropoxybenzylamine
-
-
2,6-dipropylbenzylamine
-
-
2-(1-isobutylhydrazino)-1-phenylethanol
-
2-(1-methylhydrazino)-1-(2,3,4-trimethoxyphenyl)ethanol
-
2-(1-methylhydrazino)-1-(2-naphthyl)ethanol
-
2-(1-methylhydrazino)-1-phenylethanol
-
2-(2,5-dihydro-1H-pyrrol-3-yl)pyridine
-
-
2-(4-methoxyphenyl)-1-(1-methylhydrazino)-2-propanol
-
2-(4-[2-[2-(acetylamino)-2,3-dihydro-1,3-thiazol-4-yl]ethyl]phenyl)-N-[amino(imino)methyl]acetamide
-
-
2-(aminooxy)-1-(3,4-dimethoxyphenyl)ethanol
-
-
2-(aminooxy)-1-phenylethanol
-
-
2-(methylamino)ethanethiol
-
reversible inhibition
2-(methylthio)ethylamine
-
weak irreversible inhibitor
2-([[4-(1,1-dimethylpropyl)phenyl]sulfonyl]amino)-N,3-dihydroxybutanamide
-
-
2-amino-N-[2-fluoro-3-(trifluoromethyl)benzyl]acetamide
-
-
2-amino-N-[2-fluoro-5-(trifluoromethyl)benzyl]acetamide
-
-
2-amino-N-[3-fluoro-5-(trifluoromethyl)benzyl]acetamide
-
-
2-amino-N-[4-fluoro-3-(trifluoromethyl)benzyl]acetamide
-
-
2-ethylaminobenzylamine dihydrochloride
2-hydrazino-1-(3-methoxyphenyl)ethanol
-
2-hydrazino-1-(4-methoxyphenyl)ethanol
-
2-hydrazino-1-phenylethanol
-
2-hydroxymethylbenzylamine
-
-
2-methylaminobenzylamine dihydrochloride
2-[(biphenyl-4-ylacetyl)amino]pentanedioic acid
-
-
3,3'-[[4-(aminomethyl)pyridine-3,5-diyl]bis(oxy)]dipropan-1-ol dihydrochloride
-
-
3,3-bis(aminoethyl)-1-hydroxy-2-oxo-1-triazene
3-(1-piperidinyl)-4-aminomethylpyridine dihydrochloride hemihydrate
3-(2,5-dihydro-1H-pyrrol-3-yl)pyridine
-
-
3-(2-naphthyl)-3-pyrroline
-
0.2 mM, inactivation of BPAO by 3-aryl-3-pyrrolines
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-amino-4-aminomethylpyridine dihydrochloride
-
-
3-aminopropanethiol
-
reversible inhibition
3-biphenyl-4-yl-2,5-dihydro-1H-pyrrole hydrochloride
-
0.1 mM, inactivation of BPAO by 3-aryl-3-pyrrolines
3-bromoprop-2-yn-1-amine
-
-
3-cycloheptylamino-4-aminomethylpyridine dihydrochloride monohydrate
3-cyclohexylamino-4-aminomethylpyridine dihydrochloride monohydrate
3-cyclohexylmethylamino-4-aminomethylpyridine dihydrochloride monohydrate
3-cyclopentylamino-4-aminomethylpyridine dihydrochloride hemihydrate
3-cyclopropylamino-4-aminomethylpyridine dihydrochloride sesquihydrate
3-ethylamino-4-aminomethylpyridine dihydrochloride
3-methylamino-4-aminomethylpyridine dihydrochloride
3-naphthalen-1-yl-2,5-dihydro-1H-pyrrole hydrochloride
-
0.4 mM, inactivation of BPAO by 3-aryl-3-pyrrolines
3-phenyl-3-pyrroline
-
0.4 mM, inactivation of BPAO by 3-aryl-3-pyrrolines
3-[(1-methylethyl)amino]-4-aminomethylpyridine dihydrochloride
3-[2-(3-methoxyphenyl)ethyl]-2,5-dihydro-1H-pyrrole
-
-
4,4'-[[4-(aminomethyl)pyridine-3,5-diyl]bis(oxy)]dibutan-1-ol dihydrochloride
-
-
4-(2,5-dihydro-1H-pyrrol-3-yl)-N,N-dimethylaniline hydrochloride
-
0.4 mM, inactivation of BPAO by 3-aryl-3-pyrrolines
4-(2-naphthyloxy)but-2-yn-1-amine
-
-
4-(4-methoxyphenoxy)but-2-yn-1-amine
-
-
4-(4-methylphenoxy)but-2-yn-1-amine
-
-
4-(4-nitrophenoxy)but-2-yn-1-amine
-
-
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
4-(aminomethyl)-N,N'-bis(1-methylethyl)pyridine-3,5-diamine dihydrochloride
-
-
4-(aminomethyl)-N,N'-dibutylpyridine-3,5-diamine dihydrochloride
-
-
4-(aminomethyl)-N,N'-diethylpyridazine-3,5-diamine
-
-
4-(aminomethyl)-N,N'-diethylpyridine-3,5-diamine dihydrochloride
4-(aminomethyl)-N,N'-dimethylpyridine-3,5-diamine dihydrochloride
4-(aminomethyl)-N-butylpyridazin-3-amine
-
27% inhibition at 0.5 mM
4-(aminomethyl)-N-ethylpyridazin-3-amine
-
29% inhibition at 0.5 mM
4-(aminomethyl)-N-methylpyridazin-3-amine
-
47% inhibition at 0.5 mM
4-(aminomethyl)-N-methylpyridine-3,5-diamine dihydrochloride
-
-
4-(aminomethyl)-N-propylpyridazin-3-amine
-
44% inhibition at 0.5 mM
4-amino-3-hydroxy-N-(3-phenylpropyl)benzamide
-
-
4-aminobut-2-ynenitrile
-
-
4-bromo-N-[2-(hydroxyamino)-2-oxoethyl]benzamide
-
-
4-hydroxybenzylhydrazine
-
-
4-phenoxybut-2-yn-1-amine
-
-
4-[[(2E)-4-amino-2-fluorobut-2-en-1-yl]oxy]-N,N-dimethylbenzamide
-
-
4-[[(2E)-4-amino-2-fluorobut-2-en-1-yl]oxy]-N-(1-phenylethyl)benzamide
-
-
4-[[(2E)-4-amino-2-fluorobut-2-en-1-yl]oxy]-N-benzyl-N-methylbenzamide
-
-
4-[[(2E)-4-amino-2-fluorobut-2-en-1-yl]oxy]-N-benzylbenzamide
-
-
4-[[(2E)-4-amino-2-fluorobut-2-en-1-yl]oxy]-N-cyclohexylbenzamide
-
-
4-[[(2E)-4-amino-2-fluorobut-2-en-1-yl]oxy]-N-cyclopentylbenzamide
-
-
4-[[(2E)-4-amino-2-fluorobut-2-en-1-yl]oxy]benzamide
-
-
5-amino-2-hydroxy-N-(3-phenylpropyl)benzamide
-
-
alkylamino derivatives of 4-aminomethylpyridine
-
-
amikacin
-
about 60% residual activity at 1 mM
Br-
uncompetitive inhibitor with respect to the substrate amine and noncompetitive inhibitor with respect to dissolved oxygen
buta-2,3-dien-1-amine
-
-
Cl-
uncompetitive inhibitor with respect to the substrate amine and noncompetitive inhibitor with respect to dissolved oxygen
CuCl2
-
strong inhibition at 1 mM
cysteamine
-
reversible inhibition
EDTA
treatment with EDTA reduces the activity of wild type enzyme
extract from Taiwanofungus camphoratus
-
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
hydrazine
-
complete inhibition at 1 mM
I-
uncompetitive inhibitor with respect to the substrate amine and noncompetitive inhibitor with respect to dissolved oxygen
Iproniazid
-
nearly complete inhibition at 1 mM
kanamycin
-
about 70% residual activity at 1 mM
KCl
-
100 mM, 88% inhibition of dimeric and tetrameric enzyme
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,3-dihydroxy-2-[(2-naphthylsulfonyl)amino]butanamide
-
-
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-[2-(hydroxyamino)-2-oxoethyl]-2-(2-methyl-1H-indol-3-yl)acetamide
-
-
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
-
-
N6-(4-aminobut-2-ynyl)adenine
NaCl
-
100 mM, 88% inhibition of dimeric and tetrameric enzyme
Neocuproine
-
0.033 mM, 61% inhibition
nitric oxide
irreversible inhibitor
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
rasagiline ethanedisulfonate
-
inhibits MAO-B
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
-
sisomycin
-
about 45% residual activity at 1 mM
Sodium thioglycolate
-
slight
tobramycin
-
about 40% residual activity at 1 mM
[(2E)-3-fluoro-2-phenylprop-2-en-1-yl]hydrazine
-
-
[2-(2-methylphenyl)prop-2-en-1-yl]hydrazine
-
-
[2-(4-chlorophenyl)prop-2-en-1-yl]hydrazine
-
-
[2-(4-fluorophenyl)prop-2-en-1-yl]hydrazine
-
-
(2-phenylprop-2-en-1-yl)hydrazine
-
-
(2-phenylprop-2-en-1-yl)hydrazine
-
-
(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
1,4-phenanthroline
-
0.0075 mM, 41% inhibition
1,4-phenanthroline
-
0.33 mM, 65% inhibition
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
1-(3,5-diethoxypyridin-4-yl)methanamine dihydrochloride
-
1-(3,5-diethoxypyridin-4-yl)methanamine dihydrochloride
-
1-(3,5-diethoxypyridin-4-yl)methanamine dihydrochloride
-
-
2-Bromoethylamine
-
-
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
2-Bromoethylamine
-
irreversible inhibitor
2-ethylaminobenzylamine dihydrochloride
-
2-ethylaminobenzylamine dihydrochloride
-
2-ethylaminobenzylamine dihydrochloride
-
-
2-methylaminobenzylamine dihydrochloride
-
2-methylaminobenzylamine dihydrochloride
-
2-methylaminobenzylamine dihydrochloride
-
-
2-Phenylethylamine
substrate inhibition
2-Phenylethylamine
substrate inhibition
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-(1-piperidinyl)-4-aminomethylpyridine dihydrochloride hemihydrate
-
3-(1-piperidinyl)-4-aminomethylpyridine dihydrochloride hemihydrate
-
-
3-cycloheptylamino-4-aminomethylpyridine dihydrochloride monohydrate
-
3-cycloheptylamino-4-aminomethylpyridine dihydrochloride monohydrate
-
3-cycloheptylamino-4-aminomethylpyridine dihydrochloride monohydrate
-
-
3-cyclohexylamino-4-aminomethylpyridine dihydrochloride monohydrate
-
3-cyclohexylamino-4-aminomethylpyridine dihydrochloride monohydrate
-
-
3-cyclohexylmethylamino-4-aminomethylpyridine dihydrochloride monohydrate
-
3-cyclohexylmethylamino-4-aminomethylpyridine dihydrochloride monohydrate
-
3-cyclohexylmethylamino-4-aminomethylpyridine dihydrochloride monohydrate
-
-
3-cyclopentylamino-4-aminomethylpyridine dihydrochloride hemihydrate
-
3-cyclopentylamino-4-aminomethylpyridine dihydrochloride hemihydrate
-
-
3-cyclopropylamino-4-aminomethylpyridine dihydrochloride sesquihydrate
-
3-cyclopropylamino-4-aminomethylpyridine dihydrochloride sesquihydrate
-
-
3-ethylamino-4-aminomethylpyridine dihydrochloride
-
3-ethylamino-4-aminomethylpyridine dihydrochloride
-
3-ethylamino-4-aminomethylpyridine dihydrochloride
-
-
3-methylamino-4-aminomethylpyridine dihydrochloride
-
3-methylamino-4-aminomethylpyridine dihydrochloride
-
3-methylamino-4-aminomethylpyridine dihydrochloride
-
-
3-[(1-methylethyl)amino]-4-aminomethylpyridine dihydrochloride
-
3-[(1-methylethyl)amino]-4-aminomethylpyridine dihydrochloride
-
-
4-(aminomethyl)-N,N'-diethylpyridine-3,5-diamine dihydrochloride
-
4-(aminomethyl)-N,N'-diethylpyridine-3,5-diamine dihydrochloride
-
4-(aminomethyl)-N,N'-diethylpyridine-3,5-diamine dihydrochloride
-
-
4-(aminomethyl)-N,N'-dimethylpyridine-3,5-diamine dihydrochloride
-
4-(aminomethyl)-N,N'-dimethylpyridine-3,5-diamine dihydrochloride
-
4-(aminomethyl)-N,N'-dimethylpyridine-3,5-diamine dihydrochloride
-
-
8-hydroxyquinoline
non-competitive inhibitor; non-competitive inhibitor; non-competitive inhibitor
8-hydroxyquinoline
-
strong inhibition at 1 mM
8-hydroxyquinoline
-
0.0075 mM, 27% inhibition
aminoguanidine
irreversible competitive inhibitor; irreversible competitive inhibitor; irreversible competitive inhibitor
aminoguanidine
irreversible inhibition
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
aminoguanidine
-
irreversible inhibitor
benzylamine
substrate inhibition
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
Cuprizone
-
competitive binding to enzyme copper is suggested
cyanide
-
0.1 mM, 76% inhibition
cyanide
-
uncompetitive vs. benzylamine, non-competititve vs. O2
diethyldithiocarbamate
-
3.3 mM, 74% inhibition
diethyldithiocarbamate
-
no inhibition
extract from Taiwanofungus camphoratus
-
-
-
extract from Taiwanofungus camphoratus
-
-
-
hydroxylamine
-
complete inhibition at 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
hydroxylamine
-
3.3 mM, 30% inhibition
isoniazid
-
nearly complete inhibition at 1 mM
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
-
3.3 mM, 48% inhibition
NaN3
-
uncompetitive inhibition
NaN3
-
azide binds to Cu2+ ions, competitive inhibition vs. O2, uncompetitive vs. benzylamine
Phenelzine
-
Phenelzine
-
0.001 mM, complete inhibition of enzyme from cultured aortic smooth muscle cells
phenylhydrazine
-
-
phenylhydrazine
-
complete inhibition at 1 mM
phenylhydrazine
-
irreversible inactivation most likely due to hydrazone formation
Semicarbazide
-
nearly complete inhibition at 1 mM
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
-
isoform AO1 shows 1% residual activity at 0.1 mM, isoform AO2 shows 2% residual activity at 0.1 mM
Semicarbazide
-
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
tranylcypromine
-
fully reversible competitive onhibitor
tryptamine
substrate inhibition
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
-
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
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
irreversible inhibitor
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
-
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
substrate inhibition; substrate inhibition
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
-
not inhibited by MgCl2, MnCl2, CoCl2, ZnCl2, FeCl3, sodium azide, N-ethylmaleimide, and iodoacetate
-
additional information
-
3-pyrrolines are mechanism-based inactivators of the quinone-dependent amine oxidases but only substrates of the flavin-dependent amine oxidases
-
additional information
-
not inhibited by 2-aminoethanol and 2-(N,N-dimethylamino)ethanethiol
-
additional information
-
not inhibited by gentamycin
-
additional information
-
inhibitor synthesis and screening, overview
-
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
-
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
-
additional information
-
no effect: DTT or EDTA at 1 mM, 1,4-diamino-2-butanone, sodium azide or KCN
-
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
-
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
-
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
-
additional information
clorgyline and deprenyl do not significantly inhibit the activities
-
additional information
-
no inhibition by pargyline. SSAO activity remains unchanged during starvation
-
additional information
-
not inhibited by pargyline, clorgyline, and neocupine
-
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0.196
1,8-diaminooctane
-
at pH 7.0 and 37°C
1.7
2-aminoethylpyridine
in 50 mM Tris-HCl buffer, pH 8.0, at 25°C
0.0012 - 1.94
2-Phenylethylamine
1.2
3-aminomethylpyridine
in 50 mM Tris-HCl buffer, pH 8.0, at 25°C
1.9
4-aminomethylpyridine
in 50 mM Tris-HCl buffer, pH 8.0, at 25°C
0.016
4-aminomethylpyridine dihydrochloride
-
-
0.13
4-fluorobenzylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
0.066
aminoacetone
at pH 7.4, 37°C
0.00128 - 2.38
benzylamine
0.00088 - 0.028
beta-phenylethylamine
16.5
cyclohexanemethylamine
at pH 7.4, 37°C
0.031
cysteamine
at pH 7.4, 37°C
2.05
ethanolamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
0.014 - 0.213
hexakis(benzylammonium) decavanadate (V) dihydrate
4.56
Isoamylamine
at pH 7.4, 37°C
3.42
Isobutylamine
at pH 7.4, 37°C
0.03
octopamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
2.05
phenethylamine
at pH 7.4, 37°C
0.02 - 5
Phenylethylamine
0.698
spermine
-
at pH 7.0 and 37°C
0.02
vanillylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
additional information
additional information
-
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
0.0021
2-Phenylethylamine
pH 6.8, 30°C, mutant enzyme D298A
0.0025
2-Phenylethylamine
pH 6.8, 30°C, native copper protein
0.0025
2-Phenylethylamine
pH 6.8, 30°C, wild-type enzyme
0.0025
2-Phenylethylamine
pH 6.8, 30°C, Co-activated enzyme
0.0025
2-Phenylethylamine
pH 6.8, 30°C, Cu-activated enzyme
0.0025
2-Phenylethylamine
-
in 50mM HEPES buffer, pH 6.8, at 15°C
0.0034
2-Phenylethylamine
pH 6.8, 30°C, Ni-activated enzyme
0.0038
2-Phenylethylamine
pH 6.8, 30°C, Ni2+-substituted enzyme
0.0055
2-Phenylethylamine
isoform AMAO3, in 100 mM potassium phosphate buffer (pH 7.0), at 37°C
0.012
2-Phenylethylamine
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37°C
0.077
2-Phenylethylamine
recombinant enzyme expressed in CHO cells
1.94
2-Phenylethylamine
recombinant enzyme expressed in CHO cells
0.11
amylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
0.16
amylamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
5.71
amylamine
at pH 7.4, 37°C
0.00128
benzylamine
-
at pH 9.0
0.0045
benzylamine
-
dimeric enzyme
0.005
benzylamine
-
tetrameric enzyme
0.0051
benzylamine
-
enzyme from cultured aortic smooth muscle cells, Km decreases with increasing pH
0.0127
benzylamine
-
37°C
0.013
benzylamine
mutant enzyme L469G, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C
0.017
benzylamine
-
benzylamine oxidase
0.0174
benzylamine
-
at pH 7.2
0.018
benzylamine
mutant enzyme M211V/Y394N/L469G, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C
0.025
benzylamine
mutant enzyme M211V, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C
0.04
benzylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
0.075 - 0.095
benzylamine
-
-
0.084
benzylamine
mutant enzyme T212A, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C
0.0845
benzylamine
at pH 7.4, 37°C
0.1
benzylamine
-
in 50mM HEPES buffer, pH 6.8, at 15°C
0.167
benzylamine
recombinant enzyme expressed in CHO cells
0.184
benzylamine
wild type enzyme, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C
0.215
benzylamine
mutant enzyme Y394N, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C
0.5
benzylamine
in 50 mM Tris-HCl buffer, pH 8.0, at 25°C
0.682
benzylamine
-
recombinant enzyme
2.38
benzylamine
-
at pH 7.0 and 37°C
0.00088
beta-phenylethylamine
-
pH 8.0, mutant enzyme D383E
0.0012
beta-phenylethylamine
-
pH 7.0, wild-type enzyme
0.0017
beta-phenylethylamine
-
pH 7.5, wild-type enzyme
0.0017
beta-phenylethylamine
-
pH 6.5, wild-type enzyme
0.0018
beta-phenylethylamine
-
pH 6.0, wild-type enzyme
0.0023
beta-phenylethylamine
-
pH 8.0, wild-type enzyme
0.0023
beta-phenylethylamine
-
pH 5.75, wild-type enzyme
0.00247
beta-phenylethylamine
-
pH 7.0, mutant enzyme D383E
0.0078
beta-phenylethylamine
-
pH 5.5, wild-type enzyme
0.00962
beta-phenylethylamine
-
pH 6.0, mutant enzyme D383E
0.028
beta-phenylethylamine
-
pH 5.5, mutant enzyme D383E
0.32
Butylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
0.32
Butylamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
2.83
Butylamine
at pH 7.4, 37°C
0.089
cadaverine
-
at pH 7.0 and 37°C
0.3
cadaverine
in 50 mM Tris-HCl buffer, pH 8.0, at 25°C
12.7
cadaverine
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37°C
0.099
dopamine
at pH 7.4, 37°C
0.1
dopamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
0.86
ethylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
12.8
ethylamine
at pH 7.4, 37°C
0.014
hexakis(benzylammonium) decavanadate (V) dihydrate
-
37°C
0.0865
hexakis(benzylammonium) decavanadate (V) dihydrate
-
37°C
0.213
hexakis(benzylammonium) decavanadate (V) dihydrate
-
37°C
0.28
histamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
0.41
histamine
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37°C
0.7
histamine
in 50 mM Tris-HCl buffer, pH 8.0, at 25°C
0.88
histamine
isoform AMAO3, in 100 mM potassium phosphate buffer (pH 7.0), at 37°C
0.01
methylamine
-
native enzyme
0.146
methylamine
-
recombinant enzyme
0.18
methylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
0.236
methylamine
mutant enzyme L469G, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C
0.28
methylamine
mutant enzyme M211V, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C
0.331
methylamine
wild type enzyme, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C
0.502
methylamine
mutant enzyme T212A, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C
0.652
methylamine
at pH 7.4, 37°C
0.67
methylamine
recombinant enzyme expressed in CHO cells
0.68
methylamine
-
Co2+ reconstituted enzyme
1.26
methylamine
mutant enzyme Y394N, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C
1.7
methylamine
recombinant enzyme expressed in CHO cells
2.043
methylamine
mutant enzyme M211V/Y394N/L469G, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C
0.0163
O2
pH 6.8, 30°C, Co2+-substituted enzyme
0.0183
O2
pH 6.8, 30°C, Ni2+-substituted enzyme
0.0208
O2
pH 6.8, 30°C, native copper protein
0.021
O2
-
copper-reconstituted wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
0.026
O2
-
wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
1
O2
-
cobalt-substituted wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
0.02
Phenylethylamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
3.7 - 5
Phenylethylamine
-
at pH 7.0 and 37°C
0.49
Propylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
2.65
Propylamine
at pH 7.4, 37°C
0.038
putrescine
-
at pH 7.0 and 37°C
0.29
putrescine
-
copper-reconstituted wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
0.57
putrescine
-
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
1.2
putrescine
in 50 mM Tris-HCl buffer, pH 8.0, at 25°C
0.348
spermidine
-
at pH 7.0 and 37°C
0.8
spermidine
in 50 mM Tris-HCl buffer, pH 8.0, at 25°C
7.04
spermidine
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37°C
0.0104
tyramine
-
in 50mM HEPES buffer, pH 6.8, at 15°C
0.02
tyramine
isoform AMAO3, in 100 mM potassium phosphate buffer (pH 7.0), at 37°C
0.03
tyramine
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37°C
0.05
tyramine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
0.056
tyramine
recombinant enzyme expressed in CHO cells
0.178
tyramine
recombinant enzyme expressed in CHO cells
1.92
tyramine
-
at pH 7.0 and 37°C
additional information
additional information
-
the Km-value for O2 of the cobalt-substituted enzyme form is approximately 70fold higher than that of the copper-containing wild-type enzyme
-
additional information
additional information
comparison of steady-state kinetics of enzyme expressed in CHO and HEK-293 EBNA cells, overview
-
additional information
additional information
comparison of steady-state kinetics of enzyme expressed in CHO and HEK-293 EBNA cells, overview
-
additional information
additional information
-
kinetic analysis at different ionic strength and pH, overview
-
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0.000055
(2-methylprop-2-en-1-yl)hydrazine
Bos taurus
-
-
0.000002 - 0.000035
(2-phenylprop-2-en-1-yl)hydrazine
0.002
(2E)-3-chloroprop-2-en-1-amine
Bos taurus
-
-
0.00029
(2E)-3-fluoro-4-phenoxybut-2-en-1-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.082
(2E)-4-phenoxybut-2-en-1-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.011
(2Z)-3-chloroprop-2-en-1-amine
Bos taurus
-
-
0.02
(2Z)-3-fluoro-4-phenoxybut-2-en-1-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.1
(2Z)-4-phenoxybut-2-en-1-amine
Homo sapiens
-
IC 50 above 0.1 mM, pH and temperature not specified in the publication
0.00014
(4-[[(2E)-4-amino-2-fluorobut-2-en-1-yl]oxy]phenyl)(pyrrolidin-1-yl)methanone
Homo sapiens
-
pH and temperature not specified in the publication
0.000004 - 0.000043
(Z)-3-fluoro-2-(4-methoxybenzyl)allylamine hydrochloride
0.00086
1-(2,5-dihydro-1H-pyrrol-3-yl)isoquinoline
Bos taurus
-
-
0.00017 - 0.33
1-(3,5-diethoxypyridin-4-yl)methanamine dihydrochloride
0.000078
1-(isoquinolin-1-ylcarbonyl)pyrrolidine-2-carboxamide
Homo sapiens
-
-
0.00023
1-ethyl-2-[2-(4-fluorophenyl)prop-2-en-1-yl]hydrazine
Rattus norvegicus
-
-
0.0000017
1-[2-(4-fluorophenyl)prop-2-en-1-yl]-2-methylhydrazine
Rattus norvegicus
-
-
0.00013
1-[3,5-bis(ethylsulfanyl)pyridin-4-yl]methanamine dihydrochloride
Sus scrofa
-
-
0.0016
1-[3,5-bis(tert-butylsulfanyl)pyridin-4-yl]methanamine dihydrochloride
Sus scrofa
-
-
0.005
1-[3-(benzyloxy)-5-ethoxypyridin-4-yl]methanamine dihydrochloride
Sus scrofa
-
-
0.00075
2-(2,5-dihydro-1H-pyrrol-3-yl)pyridine
Bos taurus
-
-
0.0000026
2-(4-[2-[2-(acetylamino)-2,3-dihydro-1,3-thiazol-4-yl]ethyl]phenyl)-N-[amino(imino)methyl]acetamide
Homo sapiens
-
-
0.00009
2-(aminooxy)-1-(3,4-dimethoxyphenyl)ethanol
Bos taurus
-
-
0.00005
2-(aminooxy)-1-phenylethanol
Bos taurus
-
-
5
2-(methylamino)ethanethiol
Bos taurus
-
in 100 mM potassium phosphate buffer, pH 7.2, at 30°C
1.3
2-(methylthio)ethylamine
Bos taurus
-
in 100 mM potassium phosphate buffer, pH 7.2, at 30°C
0.000004
2-([[4-(1,1-dimethylpropyl)phenyl]sulfonyl]amino)-N,3-dihydroxybutanamide
Homo sapiens
-
-
0.000015
2-amino-N-[2-fluoro-3-(trifluoromethyl)benzyl]acetamide
Rattus norvegicus
-
-
0.00001
2-amino-N-[2-fluoro-5-(trifluoromethyl)benzyl]acetamide
Rattus norvegicus
-
-
0.000033
2-amino-N-[3-fluoro-5-(trifluoromethyl)benzyl]acetamide
Rattus norvegicus
-
-
0.00018
2-amino-N-[4-fluoro-3-(trifluoromethyl)benzyl]acetamide
Rattus norvegicus
-
-
1.5
2-ethylaminobenzylamine dihydrochloride
Ogataea angusta
-
0.75
2-methylaminobenzylamine dihydrochloride
Ogataea angusta
-
0.000125
2-[(biphenyl-4-ylacetyl)amino]pentanedioic acid
Homo sapiens
-
-
0.0032
3,3'-[[4-(aminomethyl)pyridine-3,5-diyl]bis(oxy)]dipropan-1-ol dihydrochloride
Sus scrofa
-
-
0.1
3-(1-piperidinyl)-4-aminomethylpyridine dihydrochloride hemihydrate
Sus scrofa
-
-
0.0015
3-(2,5-dihydro-1H-pyrrol-3-yl)pyridine
Bos taurus
-
-
0.042
3-(4-methoxyphenyl)-N-methyl-5-(1H-pyrrol-2-yl)-4,5-dihydro-1H-pyrazole-1-carbothioamide
Rattus norvegicus
-
-
0.016
3-amino-4-aminomethylpyridine dihydrochloride
Sus scrofa
-
-
0.3
3-aminopropanethiol
Bos taurus
-
in 100 mM potassium phosphate buffer, pH 7.2, at 30°C
0.01
3-bromoprop-2-yn-1-amine
Bos taurus
-
-
0.079 - 1
3-cycloheptylamino-4-aminomethylpyridine dihydrochloride monohydrate
0.0056
3-cyclohexylamino-4-aminomethylpyridine dihydrochloride monohydrate
Sus scrofa
-
-
0.0056 - 0.89
3-cyclohexylmethylamino-4-aminomethylpyridine dihydrochloride monohydrate
0.016 - 0.7
3-cyclopentylamino-4-aminomethylpyridine dihydrochloride hemihydrate
0.002 - 0.087
3-ethylamino-4-aminomethylpyridine dihydrochloride
0.00071 - 0.053
3-methylamino-4-aminomethylpyridine dihydrochloride
0.1
3-[(1-methylethyl)amino]-4-aminomethylpyridine dihydrochloride
Sus scrofa
-
-
0.0005
3-[2-(3-methoxyphenyl)ethyl]-2,5-dihydro-1H-pyrrole
Rattus norvegicus
-
-
0.00015
4,4'-[[4-(aminomethyl)pyridine-3,5-diyl]bis(oxy)]dibutan-1-ol dihydrochloride
Sus scrofa
-
-
0.025
4-(2-naphthyloxy)but-2-yn-1-amine
Bos taurus
-
-
0.02
4-(4-methoxyphenoxy)but-2-yn-1-amine
Bos taurus
-
-
0.022
4-(4-methylphenoxy)but-2-yn-1-amine
Bos taurus
-
-
0.02
4-(4-nitrophenoxy)but-2-yn-1-amine
Bos taurus
-
-
0.35
4-(aminomethyl)-N,N'-dibutylpyridine-3,5-diamine dihydrochloride
Sus scrofa
-
-
0.03
4-(aminomethyl)-N,N'-diethylpyridazine-3,5-diamine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00002 - 0.35
4-(aminomethyl)-N,N'-diethylpyridine-3,5-diamine dihydrochloride
0.00044 - 0.1
4-(aminomethyl)-N,N'-dimethylpyridine-3,5-diamine dihydrochloride
0.0017
4-(aminomethyl)-N-methylpyridine-3,5-diamine dihydrochloride
Sus scrofa
-
-
0.000146
4-amino-3-hydroxy-N-(3-phenylpropyl)benzamide
Homo sapiens
-
-
0.013
4-aminobut-2-ynenitrile
Bos taurus
-
-
0.0001
4-bromo-N-[2-(hydroxyamino)-2-oxoethyl]benzamide
Homo sapiens
-
-
0.2
4-phenoxybut-2-yn-1-amine
Bos taurus
-
-
0.00037
4-[[(2E)-4-amino-2-fluorobut-2-en-1-yl]oxy]-N,N-dimethylbenzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00004
4-[[(2E)-4-amino-2-fluorobut-2-en-1-yl]oxy]-N-(1-phenylethyl)benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00026
4-[[(2E)-4-amino-2-fluorobut-2-en-1-yl]oxy]-N-benzyl-N-methylbenzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00008
4-[[(2E)-4-amino-2-fluorobut-2-en-1-yl]oxy]-N-benzylbenzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00001
4-[[(2E)-4-amino-2-fluorobut-2-en-1-yl]oxy]-N-cyclohexylbenzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00002
4-[[(2E)-4-amino-2-fluorobut-2-en-1-yl]oxy]-N-cyclopentylbenzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00107
4-[[(2E)-4-amino-2-fluorobut-2-en-1-yl]oxy]benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000575
5-amino-2-hydroxy-N-(3-phenylpropyl)benzamide
Homo sapiens
-
-
1
amikacin
Escherichia coli
-
at pH 7.4 and 30°C
0.00024
BTT-2052
Escherichia coli
-
at pH 7.4 and 30°C
0.0029
but-3-yn-1-amine
Bos taurus
-
-
0.00125
buta-2,3-dien-1-amine
Bos taurus
-
-
0.0125
cysteamine
Bos taurus
-
in 100 mM potassium phosphate buffer, pH 7.2, at 30°C
0.00658
geraniin
Bos taurus
-
pH 7.4, 37°C
3.8
kanamycin
Escherichia coli
-
at pH 7.4 and 30°C
0.00002
mofegiline
Homo sapiens
-
pH and temperature not specified in the publication
0.000054
N,3-dihydroxy-2-[(2-naphthylsulfonyl)amino]butanamide
Homo sapiens
-
-
0.225
N-allyl-3-(4-methoxyphenyl)-5-(1H-pyrrol-2-yl)-4,5-dihydro-1H-pyrazole-1-carbothioamide
Rattus norvegicus
-
-
0.17
N-ethyl-3-(4-methoxyphenyl)-5-(1H-pyrrol-2-yl)-4,5-dihydro-1H-pyrazole-1-carbothioamide
Rattus norvegicus
-
-
0.000033
N-[2-(hydroxyamino)-2-oxoethyl]-2-(2-methyl-1H-indol-3-yl)acetamide
Homo sapiens
-
-
0.0000053
N-[4-(2-[4-[(2-amino-1H-imidazol-5-yl)methyl]phenyl]ethyl)-1,3-thiazol-2-yl]acetamide
Homo sapiens
-
-
0.0000045
N-[4-[2-(4-carbamimidamidophenyl)ethyl]-5-(4-sulfamoylbenzyl)-1,3-thiazol-2-yl]acetamide
Homo sapiens
-
-
0.00015
N-[4-[2-(4-[[amino(imino)methyl]amino]phenyl)ethyl]-1,3-thiazol-2-yl]acetamide
Homo sapiens
-
-
0.0007
Semicarbazide
Escherichia coli
-
at pH 7.4 and 30°C
0.8
tobramycin
Escherichia coli
-
at pH 7.4 and 30°C
0.000005
[(2E)-3-fluoro-2-phenylprop-2-en-1-yl]hydrazine
Rattus norvegicus
-
-
0.000004
[2-(2-methylphenyl)prop-2-en-1-yl]hydrazine
Rattus norvegicus
-
-
0.000003
[2-(4-chlorophenyl)prop-2-en-1-yl]hydrazine
Rattus norvegicus
-
-
0.000006
[2-(4-fluorophenyl)prop-2-en-1-yl]hydrazine
Rattus norvegicus
-
-
additional information
additional information
-
0.000002
(2-phenylprop-2-en-1-yl)hydrazine
Rattus norvegicus
-
-
0.000035
(2-phenylprop-2-en-1-yl)hydrazine
Bos taurus
-
-
0.000004
(Z)-3-fluoro-2-(4-methoxybenzyl)allylamine hydrochloride
Mus musculus
-
-
0.000009
(Z)-3-fluoro-2-(4-methoxybenzyl)allylamine hydrochloride
Rattus norvegicus
-
-
0.000027
(Z)-3-fluoro-2-(4-methoxybenzyl)allylamine hydrochloride
Homo sapiens
-
enzyme from umbilical cord
0.000043
(Z)-3-fluoro-2-(4-methoxybenzyl)allylamine hydrochloride
Homo sapiens
-
lysates of human SSAO-expressing CHO cells
0.00017
1-(3,5-diethoxypyridin-4-yl)methanamine dihydrochloride
Sus scrofa
-
-
0.33
1-(3,5-diethoxypyridin-4-yl)methanamine dihydrochloride
Pisum sativum
-
0.079
3-cycloheptylamino-4-aminomethylpyridine dihydrochloride monohydrate
Sus scrofa
-
-
1
3-cycloheptylamino-4-aminomethylpyridine dihydrochloride monohydrate
Pisum sativum
-
0.0056
3-cyclohexylmethylamino-4-aminomethylpyridine dihydrochloride monohydrate
Sus scrofa
-
-
0.54
3-cyclohexylmethylamino-4-aminomethylpyridine dihydrochloride monohydrate
Ogataea angusta
-
0.89
3-cyclohexylmethylamino-4-aminomethylpyridine dihydrochloride monohydrate
Pisum sativum
-
0.016
3-cyclopentylamino-4-aminomethylpyridine dihydrochloride hemihydrate
Sus scrofa
-
-
0.7
3-cyclopentylamino-4-aminomethylpyridine dihydrochloride hemihydrate
Ogataea angusta
-
0.002
3-ethylamino-4-aminomethylpyridine dihydrochloride
Sus scrofa
-
-
0.0093
3-ethylamino-4-aminomethylpyridine dihydrochloride
Pisum sativum
-
0.087
3-ethylamino-4-aminomethylpyridine dihydrochloride
Ogataea angusta
-
0.00071
3-methylamino-4-aminomethylpyridine dihydrochloride
Pisum sativum
-
0.008
3-methylamino-4-aminomethylpyridine dihydrochloride
Sus scrofa
-
-
0.053
3-methylamino-4-aminomethylpyridine dihydrochloride
Ogataea angusta
-
0.00002
4-(aminomethyl)-N,N'-diethylpyridine-3,5-diamine dihydrochloride
Sus scrofa
-
-
0.055
4-(aminomethyl)-N,N'-diethylpyridine-3,5-diamine dihydrochloride
Pisum sativum
-
0.35
4-(aminomethyl)-N,N'-diethylpyridine-3,5-diamine dihydrochloride
Ogataea angusta
-
0.00044
4-(aminomethyl)-N,N'-dimethylpyridine-3,5-diamine dihydrochloride
Sus scrofa
-
-
0.017
4-(aminomethyl)-N,N'-dimethylpyridine-3,5-diamine dihydrochloride
Pisum sativum
-
0.1
4-(aminomethyl)-N,N'-dimethylpyridine-3,5-diamine dihydrochloride
Ogataea angusta
-
additional information
additional information
Sus scrofa
-
above 0.1 for 2-methylaminobenzylamine dihydrochloride, 3-cyclopropylamino-4-aminomethylpyridine dihydrochloride sesquihydrate, and 2-ethylaminobenzylamine dihydrochloride, above 0.0001 for 3d
-
additional information
additional information
Pisum sativum
above 0.1 mM for 2-methylaminobenzylamine dihydrochloride and 2-ethylaminobenzylamine dihydrochloride
-
additional information
additional information
Pisum sativum
-
above 0.1 mM for 2-methylaminobenzylamine dihydrochloride and 2-ethylaminobenzylamine dihydrochloride
-
additional information
additional information
Ogataea angusta
above 1.0 mM for 1-(3,5-diethoxypyridin-4-yl)methanamine dihydrochloride, 3-[(1-methylethyl)amino]-4-aminomethylpyridine dihydrochloride, 3-cyclopropylamino-4-aminomethylpyridine dihydrochloride sesquihydrate, 3-cyclohexylamino-4-aminomethylpyridine dihydrochloride monohydrate, 3-(1-piperidinyl)-4-aminomethylpyridine dihydrochloride hemihydrate, and above 0.3 mM for 3-cycloheptylamino-4-aminomethylpyridine dihydrochloride monohydrate
-
additional information
additional information
Ogataea angusta
-
above 1.0 mM for 1-(3,5-diethoxypyridin-4-yl)methanamine dihydrochloride, 3-[(1-methylethyl)amino]-4-aminomethylpyridine dihydrochloride, 3-cyclopropylamino-4-aminomethylpyridine dihydrochloride sesquihydrate, 3-cyclohexylamino-4-aminomethylpyridine dihydrochloride monohydrate, 3-(1-piperidinyl)-4-aminomethylpyridine dihydrochloride hemihydrate, and above 0.3 mM for 3-cycloheptylamino-4-aminomethylpyridine dihydrochloride monohydrate
-
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Yamada, H.; Yasunobu, K.T.
Monoamine oxidase II. Copper, one of the prosthetic groups of plasma monamine oxidase
J. Biol. Chem.
237
3077-3082
1962
Bos taurus
brenda
Carper, W.R.; Stoddard, D.D.; Martin, D.F.
Pig liver monoamine oxidase I: isolation and characterization
Biochim. Biophys. Acta
334
287-296
1974
Sus scrofa
-
brenda
Falk, M.C.; Staton, A.J.; Williams, T.J.
Heterogeneity of pig plasma amine oxidase: molecular and catalytic properties of chromatographically isolated forms
Biochemistry
22
3746-3751
1983
Sus scrofa
brenda
Lindstrm, A.; Olsson, B.; Petterson, G.
Effect of azide on some spectral and kinetic properties of pig-plasma benzylamine oxidase
Eur. J. Biochem.
48
237-243
1974
Sus scrofa
brenda
Lindstrm, A.; Olsson, B.; Petterson, G.
Kinetics of the interaction between pig-plasma benzylamine oxidase and hydrazine derivatives
Eur. J. Biochem.
42
177-182
1974
Sus scrofa
brenda
Barker, R.; Boden, N.; Cayley, G.; Charlton, S.C.; Henson, R.; Holmes, M.C.; Kelly, I.D.; Knowles, P.F.
Properties of cupric ions in benzylamine oxidase from pig plasma as studied by magnetic-resonance and kinetic methods
Biochem. J.
177
289-302
1979
Sus scrofa
brenda
Hysmith, R.M.; Boor, P.J.
Purification of benzylamine oxidase from cultured porcine aortic smooth muscle cells
Biochem. Cell Biol.
66
821-829
1988
Sus scrofa
brenda
Cai, D.; Klinman, J.P.
Copper amine oxidase: heterologous expression, purification, and characterization of an active enzyme in Saccharomyces cerevisiae
Biochemistry
33
7647-7653
1994
Ogataea angusta, Ogataea angusta 1A2V
brenda
Li, R.; Klinman, J.P.; Mathews, F.S.
Copper amine oxidase from Hansenula polymorpha: the crystal structure determined at 2.4 A resolution reveals the active conformation
Structure
6
293-307
1998
Ogataea angusta, Ogataea angusta 1A2V
brenda
Mills, S.A.; Klinman, J.P.
Evidence against reduction of Cu2+ to Cu+ during dioxygen activation in a copper amine oxidase from Yeast
J. Am. Chem. Soc.
122
9897-9904
2000
Ogataea angusta, Ogataea angusta 1A2V
-
brenda
Saysell, C.G.; Tambyrajah, W.S.; Murray, J.M.; Phillips, S.V.; McPherson, M.J.; Knowles, P.F.
Probing the catalytic mechanism of Escherichia coli amine oxidase using mutational variants and a reversible inhibitor as a substrate analogue
Biochem. J.
365
809-816
2002
Escherichia coli
brenda
Mills, S.A.; Goto, Y.; Su, Q.; Plastino, J.; Klinman, J.P.
Mechanistic comparison of the cobalt-substituted and wild-type copper amine oxidase from Hansenula polymorpha
Biochemistry
41
10577-10584
2002
Ogataea angusta
brenda
Lee, Y.; Ling, K.Q.; Lu, X.; Silverman, R.B.; Shepard, E.M.; Dooley, D.M.; Sayre, L.M.
3-Pyrrolines are mechanism-based inactivators of the quinone-dependent amine oxidases but only substrates of the flavin-dependent amine oxidases
J. Am. Chem. Soc.
124
12135-12143
2002
Bos taurus
brenda
Kishishita, S.; Okajima, T.; Kim, M.; Yamaguchi, H.; Hirota, S.; Suzuki, S.; Kuroda, S.; Tanizawa, K.; Mure, M.
Role of copper ion in bacterial copper amine oxidase: spectroscopic and crystallographic studies of metal-substituted enzymes
J. Am. Chem. Soc.
125
1041-1055
2003
Arthrobacter globiformis (P46881), Arthrobacter globiformis
brenda
Murakawa, T.; Okajima, T.; Kuroda, S.; Nakamoto, T.; Taki, M.; Yamamoto, Y.; Hayashi, H.; Tanizawa, K.
Quantum mechanical hydrogen tunneling in bacterial copper amine oxidase reaction
Biochem. Biophys. Res. Commun.
342
414-423
2006
Arthrobacter globiformis (P46881)
brenda
Okajima, T.; Kishishita, S.; Chiu, Y.C.; Murakawa, T.; Kim, M.; Yamaguchi, H.; Hirota, S.; Kuroda, S.; Tanizawa, K.
Reinvestigation of metal ion specificity for quinone cofactor biogenesis in bacterial copper amine oxidase
Biochemistry
44
12041-12048
2005
Arthrobacter globiformis (P46881), Arthrobacter globiformis
brenda
DuBois, J.L.; Klinman, J.P.
Role of a strictly conserved active site tyrosine in cofactor genesis in the copper amine oxidase from Hansenula polymorpha
Biochemistry
45
3178-3188
2006
Ogataea angusta
brenda
Chiu, Y.C.; Okajima, T.; Murakawa, T.; Uchida, M.; Taki, M.; Hirota, S.; Kim, M.; Yamaguchi, H.; Kawano, Y.; Kamiya, N.; Kuroda, S.; Hayashi, H.; Yamamoto, Y.; Tanizawa, K.
Kinetic and structural studies on the catalytic role of the aspartic acid residue conserved in copper amine oxidase
Biochemistry
45
4105-4120
2006
Arthrobacter globiformis (P46881), Arthrobacter globiformis
brenda
Takahashi, K.; Klinman, J.P.
Relationship of stopped flow to steady state parameters in the dimeric copper amine oxidase from Hansenula polymorpha and the role of zinc in inhibiting activity at alternate copper-containing subunits
Biochemistry
45
4683-4694
2006
Ogataea angusta
brenda
Ochiai, Y.; Itoh, K.; Sakurai, E.; Adachi, M.; Tanaka, Y.
Substrate selectivity of monoamine oxidase A, monoamine oxidase B, diamine oxidase, and semicarbazide-sensitive amine oxidase in COS-1 expression systems
Biol. Pharm. Bull.
29
2362-2366
2006
Rattus norvegicus (O08590)
brenda
Bertini, V.; Buffoni, F.; Ignesti, G.; Picci, N.; Trombino, S.; Iemma, F.; Alfei, S.; Pocci, M.; Lucchesini, F.; De Munno, A.
Alkylamino derivatives of 4-aminomethylpyridine as inhibitors of copper-containing amine oxidases
J. Med. Chem.
48
664-670
2005
Sus scrofa, Ogataea angusta (P12807), Ogataea angusta, Pisum sativum (Q42432), Pisum sativum
brenda
Longu, S.; Mura, A.; Padiglia, A.; Medda, R.; Floris, G.
Mechanism-based inactivators of plant copper/quinone containing amine oxidases
Phytochemistry
66
1751-1758
2005
Lens culinaris, Onobrychis viciifolia, Pisum sativum (Q43077), Lathyrus sativus (Q6A174)
brenda
Dai, X.; Ou, X.; Hao, X.; Cao, D.; Tang, Y.; Hu, Y.; Li, X.; Tang, C.
Synthetic liver X receptor agonist T0901317 inhibits semicarbazide-sensitive amine oxidase gene expression and activity in apolipoprotein E knockout mice
Acta Biochim. Biophys. Sin. (Shanghai)
40
261-268
2008
Mus musculus
brenda
Gokturk, C.; Sugimoto, H.; Blomgren, B.; Roomans, G.M.; Forsberg-Nilsson, K.; Oreland, L.; Sjoquist, M.
Macrovascular changes in mice overexpressing human semicarbazide-sensitive amine oxidase in smooth muscle cells
Am. J. Hypertens.
20
743-750
2007
Homo sapiens
brenda
Di Paolo, M.L.; Pesce, C.; Lunelli, M.; Scarpa, M.; Rigo, A.
N-alkanamines as substrates to probe the hydrophobic region of bovine serum amine oxidase active site: a kinetic and spectroscopic study
Arch. Biochem. Biophys.
465
50-60
2007
Bos taurus
brenda
Wang, G.J.; Lin, S.Y.; Wu, W.C.; Hou, W.C.
DPPH radical scavenging and semicarbazide-sensitive amine oxidase inhibitory and cytotoxic activities of Taiwanofungus camphoratus (Chang-chih)
Biosci. Biotechnol. Biochem.
71
1873-1878
2007
Homo sapiens, Mus musculus
brenda
Yraola, F.; Garcia-Vicente, S.; Marti, L.; Albericio, F.; Zorzano, A.; Royo, M.
Understanding the mechanism of action of the novel SSAO substrate (C7NH10)6(V10O28).2H2O, a prodrug of peroxovanadate insulin mimetics
Chem. Biol. Drug Des.
69
423-428
2007
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Dunkel, P.; Gelain, A.; Barlocco, D.; Haider, N.; Gyires, K.; Sperlagh, B.; Magyar, K.; Maccioni, E.; Fadda, A.; Matyus, P.
Semicarbazide-sensitive amine oxidase/vascular adhesion protein 1: recent developments concerning substrates and inhibitors of a promising therapeutic target
Curr. Med. Chem.
15
1827-1839
2008
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Roessner, V.; Weber, A.; Becker, A.; Beck, G.; Frieling, H.; Bleich, S.
Decreased serum activity of semicarbazide-sensitive amine oxidase (SSAO) in patients treated with second generation antipsychotics: a link to impaired glucose metabolism ?
Eur. J. Clin. Pharmacol.
63
425-429
2007
Homo sapiens
brenda
Lin, S.Y.; Wang, C.C.; Lu, Y.L.; Wu, W.C.; Hou, W.C.
Antioxidant, anti-semicarbazide-sensitive amine oxidase, and anti-hypertensive activities of geraniin isolated from Phyllanthus urinaria
Food Chem. Toxicol.
46
2485-2492
2008
Bos taurus
brenda
Fracassini, L.; Alfarano, C.; Romagnani, B.; Pirisino, R.; Raimondi, L.
Endogenous substrates of the semicarbazide-sensitive amine oxidase increased nitric oxide production in rat white adipocytes
Inflamm. Res.
57
S53-S54
2008
Rattus norvegicus
brenda
Moore, R.H.; Spies, M.A.; Culpepper, M.B.; Murakawa, T.; Hirota, S.; Okajima, T.; Tanizawa, K.; Mure, M.
Trapping of a dopaquinone intermediate in the TPQ cofactor biogenesis in a copper-containing amine oxidase from Arthrobacter globiformis
J. Am. Chem. Soc.
129
11524-11534
2007
Arthrobacter globiformis (P46881), Arthrobacter globiformis
brenda
Langley, D.B.; Brown, D.E.; Cheruzel, L.E.; Contakes, S.M.; Duff, A.P.; Hilmer, K.M.; Dooley, D.M.; Gray, H.B.; Guss, J.M.; Freeman, H.C.
Enantiomer-specific binding of ruthenium(II) molecular wires by the amine oxidase of Arthrobacter globiformis
J. Am. Chem. Soc.
130
8069-8078
2008
Arthrobacter globiformis (P46881), Arthrobacter globiformis
brenda
Hernandez-Guillamon, M.; Bolea, I.; Sole, M.; Boada, M.; Tipton, K.F.; Unzeta, M.
Sodium bicarbonate enhances membrane-bound and soluble human semicarbazide-sensitive amine oxidase activity in vitro
J. Biochem.
142
571-576
2007
Homo sapiens
brenda
Lee, H.I.; Kim, Y.M.; Ro, Y.T.
Purification and characterization of a copper-containing amine oxidase from Mycobacterium sp. strain JC1 DSM 3803 grown on benzylamine
J. Biochem.
144
107-114
2008
Mycobacterium sp., Mycobacterium sp. DSM 3803 / JC1
brenda
Wiwanitkit, V.
Synergistic interaction between semicarbazide-sensitive amine oxidase and angiotensin-converting enzyme in diabetes: functional analysis by gene ontology
J. Diabetes Complicat.
22
413-419
2008
Homo sapiens (Q16853)
brenda
An, Z.; Jing, W.; Liu, Y.; Zhang, W.
Hydrogen peroxide generated by copper amine oxidase is involved in abscisic acid-induced stomatal closure in Vicia faba
J. Exp. Bot.
59
815-825
2008
Vicia faba
brenda
Leonetti, F.; Capaldi, C.; Pisani, L.; Nicolotti, O.; Muncipinto, G.; Stefanachi, A.; Cellamare, S.; Caccia, C.; Carotti, A.
Solid-phase synthesis and insights into structure-activity relationships of safinamide analogues as potent and selective inhibitors of type B monoamine oxidase
J. Med. Chem.
50
4909-4916
2007
Homo sapiens
brenda
Olivieri, A.; Tipton, K.; O'Sullivan, J.
L-lysine as a recognition molecule for the VAP-1 function of SSAO
J. Neural Transm.
114
747-749
2007
Bos taurus
brenda
O'Sullivan, J.; Davey, G.; OSullivan, M.; Tipton, K.F.
Hydrogen peroxide derived from amine oxidation mediates the interaction between aminosugars and semicarbazide-sensitive amine oxidase
J. Neural Transm.
114
751-756
2007
Bos taurus
brenda
Yabanoglu, S.; Ucar, G.; Gokhan, N.; Salgin, U.; Yesilada, A.; Bilgin, A.A.
Interaction of rat lung SSAO with the novel 1-N-substituted thiocarbamoyl-3-substituted phenyl-5-(2-pyrolyl)-2-pyrazoline derivatives
J. Neural Transm.
114
769-773
2007
Rattus norvegicus
brenda
Bour, S.; Prevot, D.; Guigne, C.; Stolen, C.; Jalkanen, S.; Valet, P.; Carpene, C.
Semicarbazide-sensitive amine oxidase substrates fail to induce insulin-like effects in fat cells from AOC3 knockout mice
J. Neural Transm.
114
829-833
2007
Mus musculus
brenda
Nemcsik, J.; Szoekoe, E.; Soltesz, Z.; Fodor, E.; Toth, L.; Egresits, J.; Tabi, T.; Magyar, K.; Kiss, I.
Alteration of serum semicarbazide-sensitive amine oxidase activity in chronic renal failure
J. Neural Transm.
114
841-843
2007
Homo sapiens
brenda
Soltesz, Z.; Tabi, T.; Halasz, A.S.; Palfi, M.; Kocsis, E.; Magyar, K.; Toth, M.; Szoekoe, E.
Studies on the insulinomimetic effects of benzylamine, exogenous substrate of semicarbazide-sensitive amine oxidase enzyme in streptozotocin induced diabetic rats
J. Neural Transm.
114
851-855
2007
Rattus norvegicus
brenda
Unzeta, M.; Sole, M.; Boada, M.; Hernandez, M.
Semicarbazide-sensitive amine oxidase (SSAO) and its possible contribution to vascular damage in Alzheimers disease
J. Neural Transm.
114
857-862
2007
Homo sapiens
brenda
Vidrio, H.; Medina, M.
Hypotensive effect of hydroxylamine, an endogenous nitric oxide donor and SSAO inhibitor
J. Neural Transm.
114
863-865
2007
Rattus norvegicus
brenda
Sibon, I.; Mercier, N.; Darret, D.; Lacolley, P.; Lamaziere, J.M.
Association between semicarbazide-sensitive amine oxidase, a regulator of the glucose transporter, and elastic lamellae thinning during experimental cerebral aneurysm development: laboratory investigation
J. Neurosurg.
108
558-566
2008
Rattus norvegicus
brenda
ORourke, A.M.; Wang, E.Y.; Miller, A.; Podar, E.M.; Scheyhing, K.; Huang, L.; Kessler, C.; Gao, H.; Ton-Nu, H.T.; Macdonald, M.T.; Jones, D.S.; Linnik, M.D.
Anti-inflammatory effects of LJP 1586 [Z-3-fluoro-2-(4-methoxybenzyl)allylamine hydrochloride], an amine-based inhibitor of semicarbazide-sensitive amine oxidase activity
J. Pharmacol. Exp. Ther.
324
867-875
2008
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Takahashi, K.; Kakuta, I.; Sugimoto, H.; Obata, T.; Oreland, L.; Kinemuchi, H.
Absence of tissue-bound semicarbazide-sensitive amine oxidase activity in carp tissues
Life Sci.
80
1094-1099
2007
no activity in Cyprinus carpio
brenda
Jiang, Z.J.; Richardson, J.S.; Yu, P.H.
The contribution of cerebral vascular semicarbazide-sensitive amine oxidase to cerebral amyloid angiopathy in Alzheimers disease
Neuropathol. Appl. Neurobiol.
34
194-204
2008
Homo sapiens
brenda
Carpene, C.; Iffiu-Soltesz, Z.; Bour, S.; Prevot, D.; Valet, P.
Reduction of fat deposition by combined inhibition of monoamine oxidases and semicarbazide-sensitive amine oxidases in obese Zucker rats
Pharmacol. Res.
56
522-530
2007
Rattus norvegicus
brenda
Prevot, D.; Soltesz, Z.; Abello, V.; Wanecq, E.; Valet, P.; Unzeta, M.; Carpene, C.
Prolonged treatment with aminoguanidine strongly inhibits adipocyte semicarbazide-sensitive amine oxidase and slightly reduces fat deposition in obese Zucker rats
Pharmacol. Res.
56
70-79
2007
Rattus norvegicus
brenda
Carpene, C.; Abello, V.; Iffiu-Soltesz, Z.; Mercier, N.; Feve, B.; Valet, P.
Limitation of adipose tissue enlargement in rats chronically treated with semicarbazide-sensitive amine oxidase and monoamine oxidase inhibitors
Pharmacol. Res.
57
426-434
2008
Rattus norvegicus
brenda
Pirrat, P.; Smith, M.A.; Pearson, A.R.; McPherson, M.J.; Phillips, S.E.
Structure of a xenon derivative of Escherichia coli copper amine oxidase: confirmation of the proposed oxygen-entry pathway
Acta Crystallogr. Sect. F
64
1105-1109
2008
Escherichia coli (P46883), Escherichia coli
brenda
Atkin, K.E.; Reiss, R.; Turner, N.J.; Brzozowski, A.M.; Grogan, G.
Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of variants of monoamine oxidase from Aspergillus niger
Acta Crystallogr. Sect. F
64
182-185
2008
Aspergillus niger
brenda
Langley, D.B.; Trambaiolo, D.M.; Duff, A.P.; Dooley, D.M.; Freeman, H.C.; Guss, J.M.
Complexes of the copper-containing amine oxidase from Arthrobacter globiformis with the inhibitors benzylhydrazine and tranylcypromine
Acta Crystallogr. Sect. F
64
577-583
2008
Arthrobacter globiformis (P46881), Arthrobacter globiformis
brenda
Nunes, S.F.; Figueiredo, I.V.; Soares, P.J.; Costa, N.E.; Lopes, M.C.; Caramona, M.M.
Semicarbazide-sensitive amine oxidase activity and total nitrite and nitrate concentrations in serum: novel biochemical markers for type 2 diabetes?
Acta Diabetol.
46
135-140
2009
Homo sapiens
brenda
Bour, S.; Caspar-Bauguil, S.; Iffiu-Soltesz, Z.; Nibbelink, M.; Cousin, B.; Miiluniemi, M.; Salmi, M.; Stolen, C.; Jalkanen, S.; Casteilla, L.; Penicaud, L.; Valet, P.; Carpene, C.
Semicarbazide-sensitive amine oxidase/vascular adhesion protein-1 deficiency reduces leukocyte infiltration into adipose tissue and favors fat deposition
Am. J. Pathol.
174
1075-1083
2009
Mus musculus
brenda
Kaitaniemi, S.; Elovaara, H.; Groen, K.; Kidron, H.; Liukkonen, J.; Salminen, T.; Salmi, M.; Jalkanen, S.; Elima, K.
The unique substrate specificity of human AOC2, a semicarbazide-sensitive amine oxidase
Cell. Mol. Life Sci.
66
2743-2757
2009
Homo sapiens (O75106), Homo sapiens (Q16853)
brenda
Peter, C.; Laliberte, J.; Beaudoin, J.; Labbe, S.
Copper distributed by Atx1 is available to copper amine oxidase 1 in Schizosaccharomyces pombe
Eukaryot. Cell
7
1781-1794
2008
no activity in Saccharomyces cerevisiae, Schizosaccharomyces pombe, Schizosaccharomyces pombe FY435 / ATCC 87284
brenda
Atkin, K.E.; Reiss, R.; Koehler, V.; Bailey, K.R.; Hart, S.; Turkenburg, J.P.; Turner, N.J.; Brzozowski, A.M.; Grogan, G.
The structure of monoamine oxidase from Aspergillus niger provides a molecular context for improvements in activity obtained by directed evolution
J. Mol. Biol.
384
1218-1231
2008
Aspergillus niger
brenda
Iffiu-Soltesz, Z.; Prevot, D.; Carpene, C.
Influence of prolonged fasting on monoamine oxidase and semicarbazide-sensitive amine oxidase activities in rat white adipose tissue
J. Physiol. Biochem.
65
11-23
2009
Rattus norvegicus
brenda
Vavilova, T.; Ostrovskaya, I.; Axenova, L.; Buneeva, O.; Medvedev, A.
Monoamine oxidase and semicarbazide sensitive amine oxidase activities in normal and inflamed human dental pulp
Med. Sci. Monit.
15
BR289-BR292
2009
Homo sapiens
brenda
Stevanato, R.; Cardillo, S.; Braga, M.; De Iuliis, A.; Battaglia, V.; Toninello, A.; Agostinelli, E.; Vianello, F.
Preliminary kinetic characterization of a copper amine oxidase from rat liver mitochondria matrix
Amino Acids
40
713-720
2011
Rattus norvegicus
brenda
Liang, G.; Choi-Sledeski, Y.M.; Poli, G.; Chen, X.; Shum, P.; Minnich, A.; Wang, Q.; Tsay, J.; Sides, K.; Cairns, J.; Stoklosa, G.; Nieduzak, T.; Zhao, Z.; Wang, J.; Vaz, R.J.
A conformationally constrained inhibitor with an enhanced potency for beta-tryptase and stability against semicarbazide-sensitive amine oxidase (SSAO)
Bioorg. Med. Chem. Lett.
20
6721-6724
2010
Homo sapiens
brenda
Haider, N.; Hochholdinger, I.; Matyus, P.; Wobus, A.
Synthesis of ortho-functionalized 4-aminomethylpyridazines as substrate-like semicarbazide-sensitive amine oxidase inhibitors
Chem. Pharm. Bull.
58
964-970
2010
Homo sapiens
brenda
Martelius, T.; Salmi, M.; Krogerus, L.; Loginov, R.; Schoultz, M.; Karikoski, M.; Miiluniemi, M.; Soots, A.; Hoeckerstedt, K.; Jalkanen, S.; Lautenschlager, I.
Inhibition of semicarbazide-sensitive amine oxidases decreases lymphocyte infiltration in the early phases of rat liver allograft rejection
Int. J. Immunopathol. Pharmacol.
21
911-920
2009
Rattus norvegicus
brenda
Nurminen, E.M.; Pihlavisto, M.; Lazar, L.; Szakonyi, Z.; Pentikaeinen, U.; Fueloep, F.; Pentikaeinen, O.T.
Synthesis, in vitro activity, and three-dimensional quantitative structure-activity relationship of novel hydrazine inhibitors of human vascular adhesion protein-1
J. Med. Chem.
53
6301-6315
2010
Homo sapiens (Q16853), Homo sapiens
brenda
Jeon, H.B.; Jang, Y.
Reversible inactivation of bovine plasma amine oxidase by cysteamine and related analogs
Biochem. Biophys. Res. Commun.
403
442-446
2010
Bos taurus
brenda
Smith, M.A.; Pirrat, P.; Pearson, A.R.; Kurtis, C.R.; Trinh, C.H.; Gaule, T.G.; Knowles, P.F.; Phillips, S.E.; McPherson, M.J.
Exploring the roles of the metal ions in Escherichia coli copper amine oxidase
Biochemistry
49
1268-1280
2010
Escherichia coli (P46883), Escherichia coli
brenda
Chang, C.M.; Klema, V.J.; Johnson, B.J.; Mure, M.; Klinman, J.P.; Wilmot, C.M.
Kinetic and structural analysis of substrate specificity in two copper amine oxidases from Hansenula polymorpha
Biochemistry
49
2540-2550
2010
Ogataea angusta (P12807), Ogataea angusta
brenda
Elovaara, H.; Kidron, H.; Parkash, V.; Nymalm, Y.; Bligt, E.; Ollikka, P.; Smith, D.; Pihlavisto, M.; Salmi, M.; Jalkanen, S.; Salminen, T.
Identification of two imidazole binding sites and key residues for substrate specificity in human primary amine oxidase AOC3
Biochemistry
50
5507-5520
2011
Homo sapiens (Q16853), Homo sapiens
brenda
McGrath, A.P.; Mithieux, S.M.; Collyer, C.A.; Bakhuis, J.G.; van den Berg, M.; Sein, A.; Heinz, A.; Schmelzer, C.; Weiss, A.S.; Guss, J.M.
Structure and activity of Aspergillus nidulans copper amine oxidase
Biochemistry
50
5718-5730
2011
Aspergillus nidulans
brenda
Klema, V.J.; Solheid, C.J.; Klinman, J.P.; Wilmot, C.M.
Structural analysis of aliphatic versus aromatic substrate specificity in a copper amine oxidase from Hansenula polymorpha
Biochemistry
52
2291-2301
2013
Ogataea angusta (P12807), Ogataea angusta
brenda
Foot, J.S.; Deodhar, M.; Turner, C.I.; Yin, P.; van Dam, E.M.; Silva, D.G.; Olivieri, A.; Holt, A.; McDonald, I.A.
The discovery and development of selective 3-fluoro-4-aryloxyallylamine inhibitors of the amine oxidase activity of semicarbazide-sensitive amine oxidase/vascular adhesion protein-1 (SSAO/VAP-1)
Bioorg. Med. Chem. Lett.
22
3935-3940
2012
Homo sapiens
brenda
Sun, J.; Morita, H.; Chen, G.; Noguchi, H.; Abe, I.
Molecular cloning and characterization of copper amine oxidase from Huperzia serrata
Bioorg. Med. Chem. Lett.
22
5784-5790
2012
Huperzia serrata (I6NC69), Huperzia serrata
brenda
Planas-Portell, J.; Gallart, M.; Tiburcio, A.; Altabella, T.
Copper-containing amine oxidases contribute to terminal polyamine oxidation in peroxisomes and apoplast of Arabidopsis thaliana
BMC Plant Biol.
13
109
2013
Arabidopsis thaliana (F4IAX1), Arabidopsis thaliana (Q8H1H9), Arabidopsis thaliana (Q8L866)
brenda
Murakawa, T.; Hayashi, H.; Taki, M.; Yamamoto, Y.; Kawano, Y.; Tanizawa, K.; Okajima, T.
Structural insights into the substrate specificity of bacterial copper amine oxidase obtained by using irreversible inhibitors
J. Biochem.
151
167-178
2012
Arthrobacter globiformis
brenda
Johnson, B.J.; Yukl, E.T.; Klema, V.J.; Klinman, J.P.; Wilmot, C.M.
Structural snapshots from the oxidative half-reaction of a copper amine oxidase: implications for O2 activation
J. Biol. Chem.
288
28409-28417
2013
Ogataea angusta (P12807)
brenda
Mills, S.A.; Brown, D.E.; Dang, K.; Sommer, D.; Bitsimis, A.; Nguyen, J.; Dooley, D.M.
Cobalt substitution supports an inner-sphere electron transfer mechanism for oxygen reduction in pea seedling amine oxidase
J. Biol. Inorg. Chem.
17
507-515
2012
Pisum sativum
brenda
Foster, A.; Barnes, N.; Speight, R.; Keane, M.
Identification, functional expression and kinetic analysis of two primary amine oxidases from Rhodococcus opacus
J. Mol. Catal. B
74
73-82
2012
Rhodococcus opacus, Rhodococcus opacus DSM 43250
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brenda
Shen, S.H.; Wertz, D.L.; Klinman, J.P.
Implication for functions of the ectopic adipocyte copper amine oxidase (AOC3) from purified enzyme and cell-based kinetic studies
PLoS ONE
7
e29270
2012
Homo sapiens (Q16853), Homo sapiens
brenda
Pintus, F.; Spano, D.; Floris, G.; Medda, R.
Euphorbia characias latex amine oxidase and peroxidase: interacting enzymes?
Protein J.
32
435-441
2013
Euphorbia characias (Q9SW90), Euphorbia characias
brenda
Lee, J.I.; Kim, Y.W.
Characterization of amine oxidases from Arthrobacter aurescens and application for determination of biogenic amines
World J. Microbiol. Biotechnol.
29
673-682
2013
Paenarthrobacter aurescens (A1R2C3), Paenarthrobacter aurescens (A1RDD3), Paenarthrobacter aurescens, Paenarthrobacter aurescens TC1 (A1R2C3), Paenarthrobacter aurescens TC1 (A1RDD3)
brenda
Dainese, E.; Sabatucci, A.; Pintus, F.; Medda, R.; Angelucci, C.B.; Floris, G.; Maccarrone, M.
Domain mobility as probed by small-angle X-ray scattering may account for substrate access to the active site of two copper-dependent amine oxidases
Acta Crystallogr. Sect. D
70
2101-2110
2014
Lens culinaris (P49252), Euphorbia characias (Q9SW90)
brenda
Lucchesini, F.; Pocci, M.; Alfei, S.; Bertini, V.; Buffoni, F.
Synthesis of 2,6-disubstituted benzylamine derivatives as reversible selective inhibitors of copper amine oxidases
Bioorg. Med. Chem.
22
1558-1567
2014
Sus scrofa
brenda
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
brenda
Huang, A.; Wang, Y.; She, X.; Mu, J.; Zhao, J.
Copper amine oxidase-catalysed hydrogen peroxide involves production of nitric oxide in darkness-induced stomatal closure in broad bean
Funct. Plant Biol.
42
1057-1067
2015
Vicia faba
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brenda
Murakawa, T.; Hamaguchi, A.; Nakanishi, S.; Kataoka, M.; Nakai, T.; Kawano, Y.; Yamaguchi, H.; Hayashi, H.; Tanizawa, K.; Okajima, T.
probing the catalytic mechanism of copper amine oxidase from Arthrobacter globiformis with halide ions
J. Biol. Chem.
290
23094-23109
2015
Arthrobacter globiformis (P46881), Arthrobacter globiformis
brenda
Sugawara, A.; Matsui, D.; Yamada, M.; Asano, Y.; Isobe, K.
Characterization of two amine oxidases from Aspergillus carbonarius AIU 205
J. Biosci. Bioeng.
119
629-635
2015
Aspergillus carbonarius, Aspergillus carbonarius AIU 205
brenda
Gross, F.; Rudolf, E.E.; Thiele, B.; Durner, J.; Astier, J.
Copper amine oxidase 8 regulates arginine-dependent nitric oxide production in Arabidopsis thaliana
J. Exp. Bot.
68
2149-2162
2017
Arabidopsis thaliana (F4IAX0), Arabidopsis thaliana
brenda
Zhang, Y.; Li, G.; Zhong, R.; Ma, Y.; Gong, P.; Zhang, F.
Characterization of the copper-containing amine oxidase from Trifolium pratense seedlings
Nucl. Sci. Tech.
27
69
2016
Trifolium pratense
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brenda
Zarei, A.; Trobacher, C.P.; Cooke, A.R.; Meyers, A.J.; Hall, J.C.; Shelp, B.J.
Apple fruit copper amine oxidase isoforms peroxisomal MdAO1 prefers diamines as substrates, whereas extracellular MdAO2 exclusively utilizes monoamines
Plant Cell Physiol.
56
137-147
2015
Malus domestica
brenda
Cona, A.; Tisi, A.; Ghuge, S.A.; Franchi, S.; De Lorenzo, G.; Angelini, R.
Wound healing response and xylem differentiation in tobacco plants over-expressing a fungal endopolygalacturonase is mediated by copper amine oxidase activity
Plant Physiol. Biochem.
82
54-65
2014
Nicotiana tabacum
brenda
Elovaara, H.; Huusko, T.; Maksimow, M.; Elima, K.; Yegutkin, G.G.; Skurnik, M.; Dobrindt, U.; Siitonen, A.; McPherson, M.J.; Salmi, M.; Jalkanen, S.
Primary amine oxidase of Escherichia coli is a metabolic enzyme that can use a human leukocyte molecule as a substrate
PLoS ONE
10
e0142367
2015
Escherichia coli
brenda
Song, X.; She, X.; Yue, M.; Liu, Y.; Wang, Y.; Zhu, X.; Huang, A.
Involvement of copper amine oxidase (CuAO)-dependent hydrogen peroxide synthesis in ethylene-induced stomatal closure in Vicia faba
Russ. J. Plant Physiol.
61
390-396
2014
Vicia faba
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brenda
Murakawa, T.; Baba, S.; Kawano, Y.; Hayashi, H.; Yano, T.; Kumasaka, T.; Yamamoto, M.; Tanizawa, K.; Okajima, T.
In crystallo thermodynamic analysis of conformational change of the topaquinone cofactor in bacterial copper amine oxidase
Proc. Natl. Acad. Sci. USA
116
135-140
2019
Arthrobacter globiformis (P46881), Arthrobacter globiformis
brenda
Amani, M.; Barzegar, A.; Mazani, M.
Osmolytic effect of sucrose on thermal denaturation of pea seedling copper amine oxidase
Protein J.
36
147-153
2017
Pisum sativum (Q43077), Pisum sativum
brenda