Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.4.3.21 - primary-amine oxidase and Organism(s) Homo sapiens and UniProt Accession Q16853

for references in articles please use BRENDA:EC1.4.3.21
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.3 With oxygen as acceptor
                1.4.3.21 primary-amine oxidase
IUBMB Comments
A group of enzymes that oxidize primary monoamines but have little or no activity towards diamines, such as histamine, or towards secondary and tertiary amines. They are copper quinoproteins (2,4,5-trihydroxyphenylalanine quinone) and, unlike EC 1.4.3.4, monoamine oxidase, are sensitive to inhibition by carbonyl-group reagents, such as semicarbazide. In some mammalian tissues the enzyme also functions as a vascular-adhesion protein (VAP-1).
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: Q16853
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
vap-1, vascular adhesion protein-1, copper amine oxidase, benzylamine oxidase, bovine serum amine oxidase, plasma amine oxidase, ssao/vap-1, bovine plasma amine oxidase, copper-containing amine oxidase, primary amine oxidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amine oxidase, copper containing
-
Copper amine oxidase
-
copper-containing monoamine oxidase
-
primary amine oxidase
-
semicarbazide-sensitive amine oxidase
-
vascular adhesion protein-1
-
amine oxidase, copper containing
-
AOC3
-
-
plasma amine oxidase
-
-
primary amine oxidase
-
-
semicarbazide-sensitive amine oxidase
vascular adhesion protein 1
-
-
vascular adhesion protein-1
-
-
additional information
VAP-1 belongs to the semicarbazide-sensitive amine oxidases, SSAOs
SYSTEMATIC NAME
IUBMB Comments
primary-amine:oxygen oxidoreductase (deaminating)
A group of enzymes that oxidize primary monoamines but have little or no activity towards diamines, such as histamine, or towards secondary and tertiary amines. They are copper quinoproteins (2,4,5-trihydroxyphenylalanine quinone) and, unlike EC 1.4.3.4, monoamine oxidase, are sensitive to inhibition by carbonyl-group reagents, such as semicarbazide. In some mammalian tissues the enzyme also functions as a vascular-adhesion protein (VAP-1).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-phenylethylamine + H2O + O2
2-phenylethanal + NH3 + H2O2
show the reaction diagram
-
-
-
?
4-tyramine + H2O + O2
(4-hydroxyphenyl)acetaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
?
aminoacetone + H2O + O2
methylglyoxal + NH3 + H2O2
show the reaction diagram
-
-
-
?
amylamine + H2O + O2
pentanal + NH3 + H2O2
show the reaction diagram
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
butylamine + H2O + O2
butanal + NH3 + H2O2
show the reaction diagram
-
-
-
?
cyclohexanemethylamine + H2O + O2
cyclohexanecarbaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
?
cysteamine + H2O + O2
sulfanylacetaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
?
dopamine + H2O + O2
?
show the reaction diagram
-
-
-
?
ethylamine + H2O + O2
acetaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
?
isoamylamine + H2O + O2
isoamylaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
?
isobutylamine + H2O + O2
isobutyraldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
?
methylamine + H2O + O2
formaldehyde + NH3 + H2O2
show the reaction diagram
phenethylamine + H2O + O2
phenylacetaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
?
propylamine + H2O + O2
propanal + NH3 + H2O2
show the reaction diagram
-
-
-
?
2-phenylethylamine + H2O + O2
beta-phenylethanal + NH3 + H2O2
show the reaction diagram
-
-
-
?
aminoacetone + H2O + O2
methylglyoxal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
hexakis(benzylammonium) decavanadate (V) dihydrate + H2O + O2
?
show the reaction diagram
-
-
-
-
?
methyl 1-(2-methoxyethyl)-3-(trifluoroacetyl)-1H-indole-4-carboxylate + H2O + O2
?
show the reaction diagram
-
-
-
-
?
methylamine + H2O + O2
formaldehyde + NH3 + H2O2
show the reaction diagram
phenylethyl amine + H2O + O2
phenylethanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
tryptamine + H2O + O2
(1H-indol-3-yl)acetaldehyde + NH3 + H2O2
show the reaction diagram
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
?
methylamine + H2O + O2
formaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
?
2-phenylethylamine + H2O + O2
beta-phenylethanal + NH3 + H2O2
show the reaction diagram
-
-
-
?
aminoacetone + H2O + O2
methylglyoxal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
low activity
-
-
?
methylamine + H2O + O2
formaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
phenylethyl amine + H2O + O2
phenylethanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
tryptamine + H2O + O2
(1H-indol-3-yl)acetaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
?
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
show the reaction diagram
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4,5-trihydroxyphenylalanine quinone
2,4,5-trihydroxyphenylalaninequinone
-
i.e. TPQ cofactor
trihydroxyphenylalanine quinone
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
dependent on
Zn2+
the zinc content is 0.16 mol per mole of AOC3 monomer
Co2+
dependent on
copper
-
dependent on
sodium bicarbonate
-
activates
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(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
-
1-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-2-(1-methylhydrazino)-ethanol
-
1-(2-(3-chlorophenyl)-2-methoxyethyl)-1-methylhydrazine
-
1-(2-chlorophenyl)-2-(1-methylhydrazino)ethanol
-
1-(2-phenylpropyl)hydrazine
-
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-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-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-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
-
2,2-dimethyl-2-(1-methylhydrazino)-1-phenylethanol
-
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-(4-methoxyphenyl)-1-(1-methylhydrazino)-2-propanol
-
2-hydrazino-1-(3-methoxyphenyl)ethanol
-
2-hydrazino-1-(4-methoxyphenyl)ethanol
-
2-hydrazino-1-phenylethanol
-
hydroxylamine
-
imidazole
-
Phenelzine
-
Semicarbazide
(2E)-3-fluoro-4-phenoxybut-2-en-1-amine
-
-
(2E)-4-phenoxybut-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
-
i.e. LJP 1586. Potent, specific, and orally available inhibitor of SSAO activity is an effective anti-inflammatory compound in vivo
1-(isoquinolin-1-ylcarbonyl)pyrrolidine-2-carboxamide
-
-
2-(4-[2-[2-(acetylamino)-2,3-dihydro-1,3-thiazol-4-yl]ethyl]phenyl)-N-[amino(imino)methyl]acetamide
-
-
2-([[4-(1,1-dimethylpropyl)phenyl]sulfonyl]amino)-N,3-dihydroxybutanamide
-
-
2-Phenylethylamine
substrate inhibition
2-[(biphenyl-4-ylacetyl)amino]pentanedioic acid
-
-
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'-diethylpyridazine-3,5-diamine
-
-
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-propylpyridazin-3-amine
-
44% inhibition at 0.5 mM
4-amino-3-hydroxy-N-(3-phenylpropyl)benzamide
-
-
4-bromo-N-[2-(hydroxyamino)-2-oxoethyl]benzamide
-
-
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
-
-
benzylamine
substrate inhibition
extract from Taiwanofungus camphoratus
-
-
-
hydroxylamine
-
mofegiline
-
-
N,3-dihydroxy-2-[(2-naphthylsulfonyl)amino]butanamide
-
-
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
-
-
Semicarbazide
tryptamine
substrate inhibition
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.94
2-Phenylethylamine
recombinant enzyme expressed in CHO cells
0.066
aminoacetone
at pH 7.4, 37°C
5.71
amylamine
at pH 7.4, 37°C
0.013 - 0.215
benzylamine
2.83
Butylamine
at pH 7.4, 37°C
16.5
cyclohexanemethylamine
at pH 7.4, 37°C
0.031
cysteamine
at pH 7.4, 37°C
0.099
dopamine
at pH 7.4, 37°C
12.8
ethylamine
at pH 7.4, 37°C
4.56
Isoamylamine
at pH 7.4, 37°C
3.42
Isobutylamine
at pH 7.4, 37°C
0.236 - 2.043
methylamine
2.05
phenethylamine
at pH 7.4, 37°C
2.65
Propylamine
at pH 7.4, 37°C
0.077
2-Phenylethylamine
recombinant enzyme expressed in CHO cells
0.167 - 0.287
benzylamine
0.213
hexakis(benzylammonium) decavanadate (V) dihydrate
-
37°C
1.7
methylamine
recombinant enzyme expressed in CHO cells
0.056 - 0.178
tyramine
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.46
aminoacetone
at pH 7.4, 37°C
4.33
amylamine
at pH 7.4, 37°C
3.42
benzylamine
at pH 7.4, 37°C
6.31
Butylamine
at pH 7.4, 37°C
5.36
cyclohexanemethylamine
at pH 7.4, 37°C
1.11
cysteamine
at pH 7.4, 37°C
0.54
dopamine
at pH 7.4, 37°C
6.12
ethylamine
at pH 7.4, 37°C
6.89
Isoamylamine
at pH 7.4, 37°C
7.4
Isobutylamine
at pH 7.4, 37°C
5.6
methylamine
at pH 7.4, 37°C
1.12
phenethylamine
at pH 7.4, 37°C
5.8
Propylamine
at pH 7.4, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
22.3
aminoacetone
at pH 7.4, 37°C
0.757
amylamine
at pH 7.4, 37°C
40.5
benzylamine
at pH 7.4, 37°C
2.23
Butylamine
at pH 7.4, 37°C
0.325
cyclohexanemethylamine
at pH 7.4, 37°C
35.5
cysteamine
at pH 7.4, 37°C
5.44
dopamine
at pH 7.4, 37°C
0.478
ethylamine
at pH 7.4, 37°C
1.51
Isoamylamine
at pH 7.4, 37°C
2.16
Isobutylamine
at pH 7.4, 37°C
8.58
methylamine
at pH 7.4, 37°C
0.545
phenethylamine
at pH 7.4, 37°C
2.19
Propylamine
at pH 7.4, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08
2-Phenylethylamine
recombinant enzyme expressed in CHO cells
0.089
benzylamine
recombinant enzyme expressed in CHO cells
0.032
tryptamine
recombinant enzyme expressed in CHO cells
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
0.02
(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
0.000027 - 0.000043
(Z)-3-fluoro-2-(4-methoxybenzyl)allylamine hydrochloride
0.000078
1-(isoquinolin-1-ylcarbonyl)pyrrolidine-2-carboxamide
Homo sapiens
-
-
0.0000026
2-(4-[2-[2-(acetylamino)-2,3-dihydro-1,3-thiazol-4-yl]ethyl]phenyl)-N-[amino(imino)methyl]acetamide
Homo sapiens
-
-
0.000004
2-([[4-(1,1-dimethylpropyl)phenyl]sulfonyl]amino)-N,3-dihydroxybutanamide
Homo sapiens
-
-
0.000125
2-[(biphenyl-4-ylacetyl)amino]pentanedioic acid
Homo sapiens
-
-
0.03
4-(aminomethyl)-N,N'-diethylpyridazine-3,5-diamine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000146
4-amino-3-hydroxy-N-(3-phenylpropyl)benzamide
Homo sapiens
-
-
0.0001
4-bromo-N-[2-(hydroxyamino)-2-oxoethyl]benzamide
Homo sapiens
-
-
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
-
-
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
-
-
0.000033
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
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6
assay at
7.4
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
semicarbazide-sensitive amine oxidase is overexpressed in cerebrovascular tissue of patients with Alzheimer’s disease cerebral amyloid angiopathy. The enzyme colocalizes with beta-amyloid deposits
Manually annotated by BRENDA team
-
significantly elevated serum SSAO activity in diabetic patients, overview
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzymatic activity plays a crucial role in leukocyte trafficking
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AOC3_HUMAN
763
1
84622
Swiss-Prot
Secretory Pathway (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
human SSAO is a dimeric membrane protein with a short N-terminal cytoplasmic tail, a membrane-spanning domain, and an extracellular catalytic domain. 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, gated by the side chain of L469 which, along with the copper-TPQ coordination, controls the catalytic activity of SSAO, conformational changes, detailed overview
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.7 M potassium/sodium tartrate, 100 mM imidazole (pH 7.4), and 200 mM NaCl, at room temperature
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L469G
the mutant shows increased affinity for benzylamine and methylamine compared to the wild type enzyme
M211V
the mutant shows increased affinity for benzylamine and methylamine compared to the wild type enzyme
M211V/Y394N/L469G
T212A
the mutant shows increased affinity for benzylamine and reduced affinity for methylamine compared to the wild type enzyme
Y394N
the mutant shows reduced affinity for benzylamine and methylamine compared to the wild type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Sepharose column chromatography, and Sephacryl S-200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
AOC3, cDNA library screening, transient expression of wild-type and mutant enzymes in HEK293, HEK293-EBNA or CHO cells
expressed in Drosophila melanogaster Schneider-2 cells and in 3T3-L1 mouse adipocytes
expressed in Escherichia coli DH5alpha cells
expression in CHO cells
AOC2, cDNA library screening, DNA and amino acid sequence determination and analysis, transient expression of wild-type enzyme in HEK293, HEK293-EBNA or CHO cells
mice overexpressing human semicarbazide-sensitive amine oxidase in smooth muscle cells. No differences in elastin quantity or lung capacity could be observed between transgenic or nontransgenic littermates. Pulse pressure is higher in transgenic mice, and aorta shows elastin fibers parallel with the aorta wall (i. e., straight fibers instead of folded compared with control mice). No difference in the response to adrenaline or sodium chloride is observed between the transgenic and control mice. The control mice have a clear decrease in blood pressure with a longer duration as a response to injection of a nitric oxide donor, sodium nitroprusside, compared with transgenic mice where only a minor response is observed. The SSAO activity in serum of control mice is elevated in response to injection of the NO donor, but not in response to a ganglion blocker
-
overexpression in CHO cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cells are induced to express the enzyme with 0.6 mM CuSO4
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
VAP-1 might be a target for anti-inflammatory drug therapy because of its role in leukocyte adhesion to endothelium
medicine
-
hexakis(benzylammonium) decavanadate (V) dihydrate acts as a prodrug of peroxovanadate insulin mimetics. SSAO oxidizes hexakis(benzylammonium) decavanadate (V) dihydrate to the same extent as it does benzylamine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team