Information on EC 1.4.3.21 - primary-amine oxidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.4.3.21
-
RECOMMENDED NAME
GeneOntology No.
primary-amine oxidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2
show the reaction diagram
-
-
-
-
RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2
show the reaction diagram
proposed mechanism, crystal structure
-
RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2
show the reaction diagram
role of copper in enzyme activity
-
RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2
show the reaction diagram
proposed mechanism, crystal structure; role of copper in enzyme activity
Ogataea angusta 1A2V
-
-
PATHWAY
KEGG Link
MetaCyc Link
beta-Alanine metabolism
-
Biosynthesis of secondary metabolites
-
Glycine, serine and threonine metabolism
-
Isoquinoline alkaloid biosynthesis
-
Metabolic pathways
-
Phenylalanine metabolism
-
phenylethanol biosynthesis
-
phenylethylamine degradation I
-
threonine degradation III (to methylglyoxal)
-
Tropane, piperidine and pyridine alkaloid biosynthesis
-
Tyrosine metabolism
-
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).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AMAO2
A1R2C3
isoform
AMAO2
A1R2C3
isoform
-
AMAO3
A1RDD3
isoform
AMAO3
A1RDD3
isoform
-
amine oxidase 1
P12807
-
amine oxidase, copper containing
O75106, Q16853
-
AO1
-
isoform
AO1
Rhodococcus opacus DSM 43250
-
isoform
-
AO2
-
isoform
AO2
Rhodococcus opacus DSM 43250
-
isoform
-
AOC2
O75106
-
AOC3
-
-
AOC3
-
the major SSAO form expressed in mouse adipocytes is encoded by the AOC3 gene
BAO
Q16853
-
benzylamine oxidase
Q16853
-
bovine plasma amine oxidase
-
-
bovine serum amine oxidase
-
-
BPAO
-
-
BSAO
-
-
CAO
I6NC69
-
CAO
E7R5K2
-
CAO
Schizosaccharomyces pombe FY435
-
-
-
Copper amine oxidase
-
-
Copper amine oxidase
-
-
Copper amine oxidase
-
-
Copper amine oxidase
P46883
-
Copper amine oxidase
Q16853
-
Copper amine oxidase
I6NC69
-
Copper amine oxidase
E7R5K2
-
Copper amine oxidase
P12807
-
Copper amine oxidase
-
-
Copper amine oxidase
-
-
Copper amine oxidase
Schizosaccharomyces pombe FY435
-
-
-
Copper amine oxidase
-
-
copper amine oxidase 1
-
-
copper amine oxidase 1
Schizosaccharomyces pombe FY435
-
-
-
copper-containing amine oxidase
F4IAX1, Q8H1H9, Q8L866
-
copper-containing amine oxidase
-
-
copper-containing amine oxidase
Q42432
-
copper-containing amine oxidase
-
-
copper-containing amine oxidase
Rhodococcus opacus DSM 43250
-
-
-
copper-containing monoamine oxidase
A1R2C3, A1RDD3
-
copper-containing monoamine oxidase
A1R2C3, A1RDD3
-
-
copper-containing monoamine oxidase
Q16853
-
copper-dependent amine oxidase
-
-
copper/quinone containing amine oxidase
Q9SW90
-
Cu/TPQ amine oxidase
Q6A174
-
Cu/TPQ amine oxidase
-
-
Cu/TPQ amine oxidase
Q43077
-
CuAO
F4IAX1, Q8H1H9, Q8L866
-
CuAO
Rhodococcus opacus DSM 43250
-
-
-
CuAO
-
-
CuAO1
Q8H1H9
isoform
CuAO2
F4IAX1
isoform
CuAO3
Q8L866
isoform
EC 1.4.3.6
F4IAX1, Q8H1H9, Q8L866
formerly
EC 1.4.3.6
-
formerly
EC 1.4.3.6
-
formerly
ELAO
Q9SW90
-
GPAO
Q6A174
-
grass pea amine oxidase
Q6A174
-
Hansenula polymorpha amine oxidase
P12807
-
HPAO
P12807
-
hPAO-1
E7R5K2
isoform
hPAO-1
P12807
-
HPAO-2
E7R5K2
isoform
lentil seedling amine oxidase
-
-
PAO
-
-
pea seedling amine oxidase
Q43077
-
plasma amine oxidase
-
-
primary amine oxidase
-
-
primary amine oxidase
Q16853
-
PSAO
Q42432
-
PSAO
Q43077
-
quinone- and copper-containing amine oxidase
-
-
quinone-containing copper amine oxidase
-
-
quinone-dependent amine oxidase
-
-
RAO
O75106
-
sainfoin amine oxidase
-
-
semicarbazide-sensitive amine oxidase
-
-
semicarbazide-sensitive amine oxidase
O75106
-
semicarbazide-sensitive amine oxidase
Q16853
-
semicarbazide-sensitive amine oxidase
-
-
semicarbazide-sensitive amine oxidase
-
-
semicarbazide-sensitive amine oxidase
Mycobacterium sp. JC1
-
-
-
semicarbazide-sensitive amine oxidase
-
-
semicarbazide-sensitive amine oxidase
O08590
-
semicarbazide-sensitive amine oxidase/vascular adhesion protein-1
-
-
semicarbazide-sensitive amine oxidases
-
-
semicarbazide-sensitive amine oxidases
-
-
SSAO
O75106
-
SSAO
Q16853
-
SSAO
Mycobacterium sp. JC1
-
-
-
SSAO
O08590
-
SSAO/VAP-1
-
-
SSAO/VAP-1
-
-
TPQ-containing CuAO
-
-
VAP-1
-
-
vascular adhesion protein 1
-
-
vascular adhesion protein 1
-
-
vascular adhesion protein-1
-
-
vascular adhesion protein-1
Q16853
-
vascular adhesion protein-1
-
-
vascular adhesion protein-1
-
-
additional information
-
VAP-1 belongs to the semicarbazide-sensitive amine oxidases, SSAOs
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
isoform CuAO1
UniProt
Manually annotated by BRENDA team
isoform CuAO2
UniProt
Manually annotated by BRENDA team
isoform CuAO3
UniProt
Manually annotated by BRENDA team
isoform AMAO2
UniProt
Manually annotated by BRENDA team
isoform AMAO3
UniProt
Manually annotated by BRENDA team
isoform AMAO2
UniProt
Manually annotated by BRENDA team
isoform AMAO3
UniProt
Manually annotated by BRENDA team
AOC2
UniProt
Manually annotated by BRENDA team
AOC3
SwissProt
Manually annotated by BRENDA team
recombinant
-
-
Manually annotated by BRENDA team
Chinese club moss
UniProt
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
female and male C57BL/6 mice, gene AOC3
-
-
Manually annotated by BRENDA team
strain JC1 DSM 3803
-
-
Manually annotated by BRENDA team
Mycobacterium sp. JC1
strain JC1 DSM 3803
-
-
Manually annotated by BRENDA team
no activity in Cyprinus carpio
-
-
-
Manually annotated by BRENDA team
no activity in Saccharomyces cerevisiae
-
-
-
Manually annotated by BRENDA team
-
E7R5K2
UniProt
Manually annotated by BRENDA team
expressed in Saccharomyces cerevisiae
-
-
Manually annotated by BRENDA team
Ogataea angusta 1A2V
1A2V
-
-
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
cerebral hemodynamic modifications induce decreases in SSAO activity resulting in cell dedifferentiation and inducing dysregulation of glucose transport
-
-
Manually annotated by BRENDA team
male Wistar rats
-
-
Manually annotated by BRENDA team
nine-week-old male Wistar rats
UniProt
Manually annotated by BRENDA team
Rhodococcus opacus DSM 43250
-
-
-
Manually annotated by BRENDA team
strain FY435, ATCC 87284, gene cao1+
-
-
Manually annotated by BRENDA team
Schizosaccharomyces pombe FY435
strain FY435, ATCC 87284, gene cao1+
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
enzyme deficiency reduces leukocyte infiltration into adipose tissue and favors fat deposition
physiological function
-
SSAO is also known as vascular adhesion protein-1 and acts as one of the adhesion molecules involved in lymphocytes trafficking. Increased serum SSAO/VAP-1 mediates tissue-selective lymphocyte adhesion and thus it may be involved in inflammatory liver cirrhosis and congestive heart failure
physiological function
-
the enzyme is present on the endothelial cell surface where it is involved in leukocyte extravasation
physiological function
-
Cao1 may enable Schizosaccharomyces pombe cells to utilize primary amines as sources of nitrogen
physiological function
-
SSAO is involved in oxidative stress and inflammation in the dental pulp, and is involved in reversible pulpitits
physiological function
-
VAP-1 mediates lymphocyte adhesion to endothelia at sites of inflammation in vitro and in vivo. Inhibition of the SSAO activity of the enzyme by semicarbazid significantly decreases inflammatory cell infiltration in liver allografts, but does not influence the luminal expression of VAP-1 in the liver allografts
physiological function
-
the enzymatic activity plays a crucial role in leukocyte trafficking
physiological function
F4IAX1, Q8H1H9, Q8L866
polyamine catabolism in the Arabidopsis apoplast is mediated predominantly by copper-containing amine oxidases, while in peroxisomes the co-localization of copper-containing amine oxidase-dependent terminal catabolism with FAD-dependent amine oxidases-back-conversion machineries contributes to modulating putrescine-mediated inhibition of the back-conversion; polyamine catabolism in the Arabidopsis apoplast is mediated predominantly by copper-containing amine oxidases, while in peroxisomes the co-localization of copper-containing amine oxidase-dependent terminal catabolism with FAD-dependent amine oxidases-back-conversion machineries contributes to modulating putrescine-mediated inhibition of the back-conversion; polyamine catabolism in the Arabidopsis apoplast is mediated predominantly by copper-containing amine oxidases, while in peroxisomes the co-localization of copper-containing amine oxidase-dependent terminal catabolism with FAD-dependent amine oxidases-back-conversion machineries contributes to modulating putrescine-mediated inhibition of the back-conversion
physiological function
Schizosaccharomyces pombe FY435
-
Cao1 may enable Schizosaccharomyces pombe cells to utilize primary amines as sources of nitrogen
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,4-diamino-2-butyne + H2O + O2
?
show the reaction diagram
-
-
-
-
?
1,4-diamino-2-butyne + H2O + O2
?
show the reaction diagram
Q43077
-
-
-
?
1,4-diamino-2-butyne + H2O + O2
?
show the reaction diagram
Q6A174
-
-
-
?
1,4-diamino-2-butyne + H2O + O2
?
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
1,4-diamino-2-chloro-2-butene + H2O + O2
?
show the reaction diagram
Q43077
-
-
-
?
1,4-diamino-2-chloro-2-butene + H2O + O2
?
show the reaction diagram
Q6A174
-
-
-
?
1,4-diamino-2-chloro-2-butene + H2O + O2
?
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
1,5-diamino-2-pentyne + H2O + O2
?
show the reaction diagram
Q43077
-
-
-
?
1,5-diamino-2-pentyne + H2O + O2
?
show the reaction diagram
Q6A174
-
-
-
?
1,5-diamino-2-pentyne + H2O + O2
?
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
1,6-diamino-2,4-hexadiyne + H2O + O2
?
show the reaction diagram
Q43077
-
-
-
?
1,6-diamino-2,4-hexadiyne + H2O + O2
?
show the reaction diagram
Q6A174
-
-
-
?
1,6-diamino-2,4-hexadiyne + H2O + O2
?
show the reaction diagram
-
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-fluoro-4-methylphenyl)methanamine + H2O + O2
? + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
1-(4-fluorophenyl)methanamine + H2O + O2
? + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
1-aminobutane + H2O + O2
butanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
1-aminoheptane + H2O + O2
heptanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
1-aminohexane + H2O + O2
hexanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
1-aminononane + H2O + O2
nonanal + NH3 + H2O2
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
1-aminopentane + H2O + O2
pentanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
1-methyl-3-phenylpropylamine + H2O + O2
4-phenylbutan-2-one + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
1-methylhistamine + O2 + H2O
?
show the reaction diagram
O08590
-
-
-
?
2-aminoethylpyridine + H2O + O2
pyridine-2-carbaldehyde + NH3 + H2O2
show the reaction diagram
-, I6NC69
-
-
-
?
2-bromoethylamine + H2O + O2
bromoacetaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
2-bromoethylamine + H2O + O2
bromoacetaldehyde + NH3 + H2O2
show the reaction diagram
Q43077
-
-
-
?
2-bromoethylamine + H2O + O2
bromoacetaldehyde + NH3 + H2O2
show the reaction diagram
Q6A174
-
-
-
?
2-bromoethylamine + H2O + O2
bromoacetaldehyde + NH3 + H2O2
show the reaction diagram
-
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-phenylethanamine + H2O + O2
? + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
2-phenylethylamine + H2O + O2
2-phenylethanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
2-phenylethylamine + H2O + O2
2-phenylethanal + NH3 + H2O2
show the reaction diagram
P46881
-
-
-
?
2-phenylethylamine + H2O + O2
2-phenylethanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
2-phenylethylamine + H2O + O2
2-phenylethanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
2-phenylethylamine + H2O + O2
2-phenylethanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
2-phenylethylamine + H2O + O2
beta-phenylethanal + NH3 + H2O2
show the reaction diagram
O75106, Q16853
-
-
-
?
2-phenylethylamine + H2O + O2
?
show the reaction diagram
A1R2C3, A1RDD3
-
-
-
?
2-phenylethylamine + H2O + O2
phenylacetaldehyde + NH3 + H2O2
show the reaction diagram
A1R2C3, A1RDD3
best substrate
-
-
?
2-phenylethylamine + H2O + O2
phenylacetaldehyde + NH3 + H2O2
show the reaction diagram
-
preferred substrate
-
-
?
3,3-bis(aminoethyl)-1-hydroxy-2-oxo-1-triazene + H2O + O2
?
show the reaction diagram
-
-
-
-
?
3,3-bis(aminoethyl)-1-hydroxy-2-oxo-1-triazene + H2O + O2
?
show the reaction diagram
Q43077
-
-
-
?
3,3-bis(aminoethyl)-1-hydroxy-2-oxo-1-triazene + H2O + O2
?
show the reaction diagram
Q6A174
-
-
-
?
3,3-bis(aminoethyl)-1-hydroxy-2-oxo-1-triazene + H2O + O2
?
show the reaction diagram
-
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-aminomethylpyridine + H2O + O2
pyridine-3-carbaldehyde + NH3 + H2O2
show the reaction diagram
-, I6NC69
-
-
-
?
3-phenylpropan-1-amine + H2O + O2
? + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
4-(aminomethyl)-N-[3-(aminomethyl)benzyl]benzamide + H2O + O2
? + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
4-aminomethylpyridine + H2O + O2
pyridine-4-carbaldehyde + NH3 + H2O2
show the reaction diagram
-, I6NC69
-
-
-
?
4-aminomethylpyridine dihydrochloride + H2O + O2
?
show the reaction diagram
P12807
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
?
show the reaction diagram
Q16853
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-aminomethylpyridine dihydrochloride + H2O + O2
?
show the reaction diagram
Q42432
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-fluorobenzylamine + H2O + O2
4-fluorobenzaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
4-N,N-dimethylaminomethyl benzylamine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
4-phenylbutan-1-amine + H2O + O2
? + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
4-tyramine + H2O + O2
(4-hydroxyphenyl)acetaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
allyl [3-(aminomethyl)benzyl]carbamate + H2O + O2
? + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
alpha-casein + H2O + O2
?
show the reaction diagram
-
the enzyme oxidizes the lysine residues in alpha-casein protein
-
-
?
aminoacetone + H2O + O2
methylglyoxal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
amphetamine + H2O + O2
1-phenyl-2-propanoate + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
amylamine + H2O + O2
pentanal + 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
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
-
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
-
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
O75106, Q16853
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
Q16853
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
E7R5K2
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
-, I6NC69
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
-
very poor substrate
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
-
best substrate
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
O75106, Q16853
low activity
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
-
best oxidized substrate
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
-
main substrate for isoform AO1
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
Mycobacterium sp. JC1
-
best oxidized substrate
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
Rhodococcus opacus DSM 43250
-
main substrate for isoform AO1
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
Ogataea angusta 1A2V
-
-
-
-
-
benzylamine + O2 + H2O
benzaldehyde + NH3 + H2O2
show the reaction diagram
O08590
-
-
-
?
beta-phenylethylamine + H2O + O2
beta-phenylethanal + NH3 + H2O2
show the reaction diagram
P12807
-
-
-
?
beta-phenylethylamine + O2 + H2O
beta-phenylethanal + NH3 + H2O2
show the reaction diagram
O08590
-
-
-
?
butylamine + H2O + O2
butanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
butylamine + H2O + O2
butanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
cadaverine + H2O + O2
?
show the reaction diagram
A1R2C3, A1RDD3
-
-
-
?
cadaverine + H2O + O2
?
show the reaction diagram
A1R2C3, A1RDD3
-
-
-
?
cadaverine + H2O + O2
DELTA1-piperideine + NH3 + H2O2
show the reaction diagram
-, I6NC69
best substrate
-
-
?
cyclohexanemethylamine + H2O + O2
cyclohexanecarbaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
cysteamine + H2O + O2
sulfanylacetaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
dopamine + H2O + O2
(3,4-dihydroxyphenyl)acetaldehyde + NH3 + H2O2
show the reaction diagram
Rhodococcus opacus, Rhodococcus opacus DSM 43250
-
-
-
-
?
dopamine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
ethanolamine + H2O + O2
glycolaldehyde + NH3 + H2O2
show the reaction diagram
Rhodococcus opacus, Rhodococcus opacus DSM 43250
-
-
-
-
?
ethylamine + H2O + O2
ethanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
ethylamine + H2O + O2
acetaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
ethylamine + H2O + O2
acetaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
ethylamine + H2O + O2
acetaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
ethylamine + H2O + O2
acetaldehyde + NH3 + H2O2
show the reaction diagram
-
isoforms AO1 and AO2 show 100% activity with ethylamine
-
-
?
ethylamine + H2O + O2
acetaldehyde + NH3 + H2O2
show the reaction diagram
Schizosaccharomyces pombe FY435
-
-
-
-
?
hexakis(benzylammonium) decavanadate (V) dihydrate + H2O + O2
?
show the reaction diagram
-
-
-
-
?
histamine + H2O + O2
4-imidazolylethanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
histamine + H2O + O2
4-imidazolylethanal + NH3 + H2O2
show the reaction diagram
-, I6NC69
-
-
-
?
histamine + H2O + O2
4-imidazolylethanal + NH3 + H2O2
show the reaction diagram
Mycobacterium sp. JC1
-
-
-
-
?
histamine + H2O + O2
1H-imidazol-4-ylacetaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
histamine + H2O + O2
?
show the reaction diagram
A1R2C3, A1RDD3
-
-
-
?
histamine + H2O + O2
?
show the reaction diagram
A1R2C3, A1RDD3
-
-
-
?
isoamylamine + H2O + O2
isoamylaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
isobutylamine + H2O + O2
isobutyraldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
methyl 1-(2-methoxyethyl)-3-(trifluoroacetyl)-1H-indole-4-carboxylate + H2O + O2
?
show the reaction diagram
-
-
-
-
?
methylamine + H2O + O2
methanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
methylamine + H2O + O2
methanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
-
methylamine + H2O + O2
methanal + NH3 + H2O2
show the reaction diagram
-
-
-
?
methylamine + H2O + O2
methanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
methylamine + H2O + O2
methanal + NH3 + H2O2
show the reaction diagram
Ogataea angusta 1A2V
-
-
-
-
-
methylamine + H2O + O2
methanal + NH3 + H2O2
show the reaction diagram
Ogataea angusta 1A2V
-
-
-
?
methylamine + H2O + O2
formaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
methylamine + H2O + O2
formaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
methylamine + H2O + O2
formaldehyde + NH3 + H2O2
show the reaction diagram
O75106, Q16853
-
-
-
?
methylamine + H2O + O2
formaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
methylamine + H2O + O2
formaldehyde + NH3 + H2O2
show the reaction diagram
E7R5K2
-
-
-
?
N-[3-(aminomethyl)benzyl]-4-bromobenzamide + H2O + O2
? + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
N-[3-(aminomethyl)benzyl]acetamide + H2O + O2
? + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
N-[3-(aminomethyl)benzyl]benzamide + H2O + O2
? + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
N-[3-(aminomethyl)benzyl]propanamide + H2O + O2
? + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
N6-(4-aminobut-2-ynyl)adenine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
N6-(4-aminobut-2-ynyl)adenine + H2O + O2
?
show the reaction diagram
Q43077
-
-
-
?
N6-(4-aminobut-2-ynyl)adenine + H2O + O2
?
show the reaction diagram
Q6A174
-
-
-
?
N6-(4-aminobut-2-ynyl)adenine + H2O + O2
?
show the reaction diagram
-
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
-
-
?
octopamine + H2O + O2
hydroxy(hydroxyphenyl)acetaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
ornithine + H2O + O2
?
show the reaction diagram
Q9SW90
ornithine can be transformed in glutamate-5-semialdehyde spontaneously cyclizes yielding DELTA1-pyrroline-5-carboxylic acid
-
-
?
phenethylamine + H2O + O2
phenylacetaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
phenylethyl amine + H2O + O2
phenylethanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
phenylethylamine + H2O + O2
phenylacetaldehyde + NH3 + H2O2
show the reaction diagram
-
main substrate for isoform AO2
-
-
?
propylamine + H2O + O2
propanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
propylamine + H2O + O2
propanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
putrescine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
putrescine + H2O + O2
?
show the reaction diagram
Q42432
-
-
-
?
putrescine + H2O + O2
?
show the reaction diagram
F4IAX1, Q8H1H9, Q8L866
-
-
-
?
putrescine + H2O + O2
?
show the reaction diagram
A1R2C3, A1RDD3
-
-
-
?
putrescine + H2O + O2
?
show the reaction diagram
-, I6NC69
-
-
-
?
putrescine + H2O + O2
?
show the reaction diagram
Q9SW90
putrescine can be oxidatively deaminated by the enzyme to corresponding aldehyde that spontaneously cyclizes yielding DELTA1-pyrroline
-
-
?
putrescine + H2O + O2
?
show the reaction diagram
A1R2C3, A1RDD3
-
-
-
?
pyrrolidine + 2,4,5-trihydroxyphenylalanine quinone + H2O + O2
? + H2O2 + NH3
show the reaction diagram
-
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
show the reaction diagram
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
show the reaction diagram
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
show the reaction diagram
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
show the reaction diagram
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
show the reaction diagram
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
show the reaction diagram
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
show the reaction diagram
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
show the reaction diagram
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
show the reaction diagram
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
show the reaction diagram
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
show the reaction diagram
Ogataea angusta 1A2V
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
show the reaction diagram
Ogataea angusta 1A2V
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
show the reaction diagram
Ogataea angusta 1A2V
-
-
-
?
sec-butylamine + H2O + O2
sec-butanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
serotonin + O2 + H2O
(5-hydroxy-1H-indol-3yl)acetaldehyde + NH3 + H2O2
show the reaction diagram
O08590
-
-
-
?
spermidine + H2O + O2
?
show the reaction diagram
F4IAX1, Q8H1H9, Q8L866
-
-
-
?
spermidine + H2O + O2
?
show the reaction diagram
A1R2C3, A1RDD3
-
-
-
?
spermidine + H2O + O2
?
show the reaction diagram
-, I6NC69
-
-
-
?
spermidine + H2O + O2
?
show the reaction diagram
A1R2C3, A1RDD3
-
-
-
?
spermidine + H2O + O2
? + NH3 + H2O2
show the reaction diagram
Q9SW90
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
show the reaction diagram
Q9SW90
good substrate
-
-
?
tropoelastin + H2O + O2
?
show the reaction diagram
-
the enzyme oxidizes the lysine residues in tropoelastin protein
-
-
?
tryptamine + H2O + O2
1H-indol-3-ylacetaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
tryptamine + H2O + O2
1H-indol-3-ylacetaldehyde + NH3 + H2O2
show the reaction diagram
Q43077
-
-
-
?
tryptamine + H2O + O2
1H-indol-3-ylacetaldehyde + NH3 + H2O2
show the reaction diagram
Q6A174
-
-
-
?
tryptamine + H2O + O2
1H-indol-3-ylacetaldehyde + NH3 + H2O2
show the reaction diagram
-
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-yl)acetaldehyde + NH3 + H2O2
show the reaction diagram
O75106, Q16853
-
-
-
?
tryptamine + H2O + O2
(1H-indol-3-yl)acetaldehyde + NH3 + H2O2
show the reaction diagram
O75106, Q16853
high activity
-
-
?
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
show the reaction diagram
Q43077
-
-
-
?
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
show the reaction diagram
Q6A174
-
-
-
?
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
show the reaction diagram
O75106, Q16853
-
-
-
?
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
show the reaction diagram
O75106, Q16853
high activity
-
-
?
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
show the reaction diagram
-
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
show the reaction diagram
Mycobacterium sp. JC1
-
-
-
-
?
tyramine + H2O + O2
(4-hydroxyphenyl)acetaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
tyramine + H2O + O2
(4-hydroxyphenyl)acetaldehyde + NH3 + H2O2
show the reaction diagram
A1R2C3, A1RDD3
-
-
-
?
tyramine + H2O + O2
(4-hydroxyphenyl)acetaldehyde + NH3 + H2O2
show the reaction diagram
-
preferred substrate
-
-
?
tyramine + H2O + O2
(4-hydroxyphenyl)acetaldehyde + NH3 + H2O2
show the reaction diagram
A1R2C3, A1RDD3
-
-
-
?
tyramine + H2O + O2
(4-hydroxyphenyl)acetaldehyde + NH3 + H2O2
show the reaction diagram
Rhodococcus opacus DSM 43250
-
-
-
-
?
tyramine + H2O + O2
?
show the reaction diagram
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
-
-
?
tyramine + H2O + O2
4-hydroxyphenylacetaldehyde + NH3 + H2O2
show the reaction diagram
Q9SW90
during this reaction, an irreversible inactivation of the enzyme occurs
-
-
?
tyramine + O2 + H2O
4-hydroxyphenylethanal + NH3 + H2O2
show the reaction diagram
O08590
-
-
-
?
vanillylamine + H2O + O2
vanillic aldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
methylbenzylamine + H2O + O2
methylbenzaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
physiologic role for SSAO in elastin maturation
-
-
-
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
?
-
-
SSAO may contribute to the vascular damage associated to Alzheimers disease
-
-
-
additional information
?
-
Q16853
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
?
-
-
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
?
-
-
alkylamines 2-bromoethylamine and 2-chloroethylamine, and the short diamine 1,2-diaminoethane are both poor substrates and irreversible inactivators of LSAO
-
-
-
additional information
?
-
-
MAO-N is a flavoenzyme that catalyses the oxidative deamination of primary amines, substrate specificity, overview
-
-
-
additional information
?
-
O75106, Q16853
semicarbazide-sensitive amine oxidases constitute a group of copper-dependent enzymes, which oxidatively deaminate primary endo- and exogenous amines
-
-
-
additional information
?
-
O75106, Q16853
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
?
-
-
MAO-N is an FAD-dependent enzyme that catalyses the conversion of terminal amines to their corresponding aldehyde
-
-
-
additional information
?
-
O75106, Q16853
substrate docking, molecular modeling and comparison of AOC2 and AOC3, overview. No activity of AOC3 with polyamine spermidine or histamine
-
-
-
additional information
?
-
P46883
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
?
-
-
three histidine residues within the C-terminal region of Cao1 that are necessary for amine oxidase activity
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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 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
?
-
E7R5K2
isoform HPAO-2 shows a clear preference for bulkier aromatic amines and isoform HPAO-1 shows a preference for short aliphatic amines
-
-
-
additional information
?
-
Q9SW90
the enzyme oxidizes arginine to ammonia, urea, hydrogen peroxide and glutamate-5-semialdehyde which spontaneously cyclizes yielding DELTA1-pyrroline-5-carboxylic acid
-
-
-
additional information
?
-
Schizosaccharomyces pombe FY435
-
three histidine residues within the C-terminal region of Cao1 that are necessary for amine oxidase activity
-
-
-
additional information
?
-
Rhodococcus opacus DSM 43250
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-phenylethylamine + H2O + O2
beta-phenylethanal + NH3 + H2O2
show the reaction diagram
O75106, Q16853
-
-
-
?
alpha-casein + H2O + O2
?
show the reaction diagram
-
the enzyme oxidizes the lysine residues in alpha-casein protein
-
-
?
aminoacetone + H2O + O2
methylglyoxal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
O75106, Q16853
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
O75106, Q16853
low activity
-
-
?
ethylamine + H2O + O2
acetaldehyde + NH3 + H2O2
show the reaction diagram
Schizosaccharomyces pombe, Schizosaccharomyces pombe FY435
-
-
-
-
?
methylamine + H2O + O2
formaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
phenylethyl amine + H2O + O2
phenylethanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
tropoelastin + H2O + O2
?
show the reaction diagram
-
the enzyme oxidizes the lysine residues in tropoelastin protein
-
-
?
tryptamine + H2O + O2
(1H-indol-3-yl)acetaldehyde + NH3 + H2O2
show the reaction diagram
O75106, Q16853
-
-
-
?
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
show the reaction diagram
O75106, Q16853
-
-
-
?
methylamine + H2O + O2
formaldehyde + NH3 + H2O2
show the reaction diagram
O75106, Q16853
-
-
-
?
additional information
?
-
-
physiologic role for SSAO in elastin maturation
-
-
-
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
?
-
-
SSAO may contribute to the vascular damage associated to Alzheimers disease
-
-
-
additional information
?
-
Q16853
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
?
-
-
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
?
-
-
MAO-N is a flavoenzyme that catalyses the oxidative deamination of primary amines, substrate specificity, overview
-
-
-
additional information
?
-
O75106, Q16853
semicarbazide-sensitive amine oxidases constitute a group of copper-dependent enzymes, which oxidatively deaminate primary endo- and exogenous amines
-
-
-
additional information
?
-
-
the catalytic center is deeply buried within the enzyme and is accessible only through a narrow channel with a diameter of about 4.5 A. This channel is gated by the side chain of L469 which, along with the copper-TPQ coordination, controls the catalytic activity of SSAO. While specific interactions with residues lining the surface of the accessing channel are important for substrate specificity, the flexibility of substrates also plays an important role, molecular dynamics and induced docking studies, detailed overview
-
-
-
additional information
?
-
-
VAP-1/SSAOs convert amines into aldehydes. SSAOs are distinct from the mammalian monoamine oxidases, MAOs, but their substrate specificities are partly overlapping
-
-
-
additional information
?
-
-
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
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,4,5-trihydroxyphenylalanine quinone
-
enzyme contains one per monomer
2,4,5-trihydroxyphenylalanine quinone
-
i.e. TPQ, covalently bound cofactor, one per monomer, generated by posttranslational modification of the first conserved tyrosine residue in the consensus sequence Asn-Tyr-(Glu/Asp)-Tyr
2,4,5-trihydroxyphenylalanine quinone
-
-
2,4,5-trihydroxyphenylalanine quinone
-
-
2,4,5-trihydroxyphenylalanine quinone
-
-
2,4,5-trihydroxyphenylalanine quinone
-, I6NC69
-
2,4,5-trihydroxyphenylalanine quinone
F4IAX1, Q8H1H9, Q8L866
-
2,4,5-trihydroxyphenylalanine quinone
-
-
2,4,5-trihydroxyphenylalanine quinone
-
-
2,4,5-trihydroxyphenylalanine quinone
-
-
2,4,5-trihydroxyphenylalanine quinone
-
-
2,4,5-trihydroxyphenylalanine quinone
-
-
2,4,5-trihydroxyphenylalanine quinone
Q9SW90
-
2,4,5-trihydroxyphenylalanine quinone
A1R2C3, A1RDD3
;
2,4,5-trihydroxyphenylalaninequinone
-
i.e. TPQ cofactor
2,4,5-trihydroxyphenylalaninequinone
-
i.e. TPQ cofactor, the cofactor is spontaneously formed by post-translational modifications of active site amino-acid residues
2,4,5-trihydroxyphenylalaninequinone
-
i.e. TPQ cofactor
FAD
-
dependent on
pyridoxal 5'-phosphate
-
enzyme may contain pyridoxal phosphate
topaquinone
Q6A174
quinone of 2,4,5-trihydroxyphenylalanine, TPQ
topaquinone
-
quinone of 2,4,5-trihydroxyphenylalanine, TPQ
topaquinone
Q43077
quinone of 2,4,5-trihydroxyphenylalanine, TPQ
trihydroxyphenylalanine quinone
-
-
FAD
-
flavoenzyme, a hydrophobic cavity extends from the protein surface to the active site, where a noncovalently bound FAD sits at the base of an aromatic cage, the sides of which are formed by Trp430 and Phe466, binding structure, overview
additional information
-
contains one 'active-carbonyl' cofactor per dimer
-
additional information
-
no evidences of topaquinone cofactor involvement
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
calcium is the normal ligand of these peripheral sites. Enzyme activity is stimulated by 3 mM. Removal of the not solvent exposed calcium ion with EDTA results in a 60-90% reduction in enzyme activity
Co2+
-
can replace Cu2+ in the enzyme
Co2+
-
enzyme reconstituted with Co2+ exhibits 2.2% of the activity of the original Cu2+ -enzyme, KM-values for amine substrate and dioxygen are comparable
Co2+
-
besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently. Although these noncupric metal ions can not initiate topaquinone formation under the atmospheric conditions, slow spectral changes are observed in the enzyme bound with Co2+ or Ni2+ ion under the dioxygen-saturating conditions. X-ray crystallographic analysis reveals structural identity of the active sites of Co- and Ni-activated enzymes with Cu-enzyme. Co2+ and Ni2+ ions are also capable of forming topaquinone, though much less efficiently than Cu2+
Co2+
O75106, Q16853
dependent on; dependent on
Co2+
-
cobalt-substituted enzyme displays nominal catalytic activity
Cobalt
-
the Km-value for O2 of the cobalt-substituted enzyme form is approximately 70fold higher than that of the copper-containing wild-type enzyme
copper
-
3.7 gatom of copper per mol of enzyme; contains cupric copper; copper involved in enzyme activity; copper protein
copper
-
contains 8 Cu2+ per 1200000 Da, Co2+, Zn2+ and Ni2+ can replace Cu2+, no effect of Mn2+; copper protein
copper
-
2 mol of Cu2+ per dimer
copper
-
copper protein
copper
-
study of cupric ions by magnetic-resonance and kinetic methods, native enzyme contains 2 tightly bound Cu2+ ions
copper
-
2 mol copper/mol enzyme dimer
copper
-
copper depleted enzyme can be reconstituted with either Cu2+, Zn2+, Co2+, or Ni2+, 79% of activity is restored with Cu2+, 19% is restored with Co2+, 1.7% with Zn2+ or Ni2+
copper
-
copper protein
copper
-
copper-containing amine oxidase
copper
-
-
copper
-
the purified enzyme contains 2.39 mol of copper per mol of subunit
copper
-
bound by three His ligands of the active-site
copper
-
dependent on
Cu
-
only the copper-containing homodimer is capable of rapid reoxidation and the zinc-copper heterodimers are incapable of rapid turnover at either subunit
Cu2+
-
contains one Cu2+ per monomer
Cu2+
-
copper protein. The native Cu2+ has essential roles such as catalyzing the electron transfer between the aminoresorcinol form of the reduced topaquinone cofactor and dioxygen, in part by providing a binding site for 1e- and 2e- reduced dioxygen species to be efficiently protonated and released and also preventing the back reaction between the product aldehyde and the aminoresorcinol form of the reduced topaquinone cofactor and dioxygen
Cu2+
-
besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently. Although these noncupric metal ions can not initiate topaquinone formation under the atmospheric conditions, slow spectral changes are observed in the enzyme bound with Co2+ or Ni2+ ion under the dioxygen-saturating conditions. X-ray crystallographic analysis reveals structural identity of the active sites of Co- and Ni-activated enzymes with Cu-enzyme. Co2+ and Ni2+ ions are also capable of forming topaquinone, though much less efficiently than Cu2+
Cu2+
Q6A174
-
Cu2+
Q43077
-
Cu2+
-
type-2 copper centre, role in the catalytic mechanism, overview
Cu2+
-
absolutely required for catalytic activity
Cu2+
-
dependent on
Cu2+
-
active site bound, coordinated by three conserved histidine residues
Cu2+
-
required
Cu2+
-
required
Cu2+
-
the wild type enzyme contains 1 mol copper per mol of subunit, copper is the most efficient catalytic metal
Cu2+
-
contains copper
Cu2+
-, I6NC69
required for activity
Cu2+
-
contains a mononuclear copper ion
Cu2+
-
the wild type enzyme contains 1.4 mol copper per monomer
Cu2+
-
contains copper
Cu2+
-
required for activity, the zinc content is 0.4 mol per mole of AOC3 monomer
Cu2+
Q9SW90
the enzyme contains one non-blue copper type 2 ion as an inorganic cofactor
Cu2+
A1R2C3, A1RDD3
required for activity, after overnight incubation with 0.1 mM CuSO4, isoform AMAO3 shows slightly enhanced activity (114% of untreated enzyme activity); required for activity, after overnight incubation with 0.1 mM CuSO4, there is no change in the activity of isoform AMAO2
Mg2+
-
enzyme activity is stimulated by 3 mM
Ni2+
-
can replace Cu2+ in the enzyme
Ni2+
-
enzyme reconstituted with Co2+ exhibits 0.9% of the activity of the original Cu2+ -enzyme, KM-values for amine substrate and dioxygen are comparable
Ni2+
-
besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently. Although these noncupric metal ions can not initiate topaquinone formation under the atmospheric conditions, slow spectral changes are observed in the enzyme bound with Co2+ or Ni2+ ion under the dioxygen-saturating conditions. X-ray crystallographic analysis reveals structural identity of the active sites of Co- and Ni-activated enzymes with Cu-enzyme. Co2+ and Ni2+ ions are also capable of forming topaquinone, though much less efficiently than Cu2+
sodium bicarbonate
-
activates
Sr2+
-
enzyme activity is stimulated by 3 mM
Zn
-
the presence of substantial amount of zinc results in two distinctive enzyme species, designated as the fast and slow enzymes. Both forms are rapidly reduced by substrate methylamine with a rate constant of 199/s but behave differently in their oxidation rates. The fast enzyme is oxidized by dioxygen at a rate of 22.1/s, whereas the slow enzyme reacts at a rate of 0.00018/s. An investigation of the relationship between the copper content and the extent of the fast enzyme shows that only the copper-containing homodimer is capable of rapid reoxidation and the zinc-copper heterodimers are incapable of rapid turnover at either subunit
Zn2+
-
can replace Cu2+ in the enzyme
Zn2+
-
besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently
Zn2+
-
the zinc content is 0.16 mol per mole of AOC3 monomer
Mn2+
-
enzyme activity is stimulated by 3 mM
additional information
-
not activated by Zn2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
-
-
(2-methylprop-2-en-1-yl)hydrazine
-
-
(2-phenylprop-2-en-1-yl)hydrazine
-
-
(2E)-3-chloroprop-2-en-1-amine
-
-
(2Z)-3-chloroprop-2-en-1-amine
-
-
(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
1,2-Diaminoethane
-
-
1,4-diamino-2-butyne
Q6A174
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
Q43077
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
Q6A174
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
Q43077
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
Q6A174
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
Q43077
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
Q6A174
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
Q43077
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-(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 hydrogen fumarate
-
-
-
1-(2-phenylpropyl)hydrazine
-
-
-
1-(3,5-diethoxypyridin-4-yl)methanamine dihydrochloride
-
-
1-(3,5-diethoxypyridin-4-yl)methanamine dihydrochloride
Q42432
-
1-(3,5-diethoxypyridin-4-yl)methanamine dihydrochloride
Q16853
-
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
Q16853
-
1-[3,5-bis(tert-butylsulfanyl)pyridin-4-yl]methanamine dihydrochloride
Q16853
-
1-[3-(benzyloxy)-5-ethoxypyridin-4-yl]methanamine dihydrochloride
Q16853
-
2,2-dimethyl-2-(1'-methylhydrazino)-1-phenylethanol
-
-
-
2-(1'-methylhydrazino)-1-(2,3,4-trimethoxyphenyl)ethanol
-
-
-
2-(1-isobutylhydrazino)-1-phenylethanol
-
-
-
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-Bromoethylamine
Q6A174
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
Q43077
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-chloroethylamine
-
-
2-ethylaminobenzylamine dihydrochloride
-
-
2-ethylaminobenzylamine dihydrochloride
Q42432
-
2-ethylaminobenzylamine dihydrochloride
Q16853
-
2-hydrazino-1-(3-methoxyphenyl)ethanol
-
-
2-hydrazino-1-(4-methoxyphenyl)ethanol
-
-
2-hydrazino-1-phenylethanol
-
-
2-methylaminobenzylamine dihydrochloride
-
-
2-methylaminobenzylamine dihydrochloride
Q42432
-
2-methylaminobenzylamine dihydrochloride
Q16853
-
2-Phenylethylamine
O75106, Q16853
substrate inhibition
2-Phenylethylamine
A1R2C3, A1RDD3
; substrate inhibition
2-[(biphenyl-4-ylacetyl)amino]pentanedioic acid
-
-
3,3'-[[4-(aminomethyl)pyridine-3,5-diyl]bis(oxy)]dipropan-1-ol dihydrochloride
Q16853
-
3,3-bis(aminoethyl)-1-hydroxy-2-oxo-1-triazene
Q6A174
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
Q43077
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
Q16853
-
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
Q16853
-
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-cycloheptylamino-4-aminomethylpyridine dihydrochloride monohydrate
Q42432
-
3-cycloheptylamino-4-aminomethylpyridine dihydrochloride monohydrate
Q16853
-
3-cyclohexylamino-4-aminomethylpyridine dihydrochloride monohydrate
-
-
3-cyclohexylamino-4-aminomethylpyridine dihydrochloride monohydrate
Q16853
-
3-cyclohexylmethylamino-4-aminomethylpyridine dihydrochloride monohydrate
-
-
3-cyclohexylmethylamino-4-aminomethylpyridine dihydrochloride monohydrate
Q42432
-
3-cyclohexylmethylamino-4-aminomethylpyridine dihydrochloride monohydrate
Q16853
-
3-cyclopentylamino-4-aminomethylpyridine dihydrochloride hemihydrate
-
-
3-cyclopentylamino-4-aminomethylpyridine dihydrochloride hemihydrate
Q16853
-
3-cyclopropylamino-4-aminomethylpyridine dihydrochloride sesquihydrate
-
-
3-cyclopropylamino-4-aminomethylpyridine dihydrochloride sesquihydrate
Q16853
-
3-ethylamino-4-aminomethylpyridine dihydrochloride
-
-
3-ethylamino-4-aminomethylpyridine dihydrochloride
Q42432
-
3-ethylamino-4-aminomethylpyridine dihydrochloride
Q16853
-
3-methylamino-4-aminomethylpyridine dihydrochloride
-
-
3-methylamino-4-aminomethylpyridine dihydrochloride
Q42432
-
3-methylamino-4-aminomethylpyridine dihydrochloride
Q16853
-
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-pyrroline
-
-
3-[(1-methylethyl)amino]-4-aminomethylpyridine dihydrochloride
-
-
3-[(1-methylethyl)amino]-4-aminomethylpyridine dihydrochloride
Q16853
-
3-[2-(3-methoxyphenyl)ethyl]-2,5-dihydro-1H-pyrrole
-
-
4,4'-[[4-(aminomethyl)pyridine-3,5-diyl]bis(oxy)]dibutan-1-ol dihydrochloride
Q16853
-
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
Q16853
-
4-(aminomethyl)-N,N'-dibutylpyridine-3,5-diamine dihydrochloride
Q16853
-
4-(aminomethyl)-N,N'-diethylpyridazine-3,5-diamine
-
-
-
4-(aminomethyl)-N,N'-diethylpyridine-3,5-diamine dihydrochloride
-
-
4-(aminomethyl)-N,N'-diethylpyridine-3,5-diamine dihydrochloride
Q42432
-
4-(aminomethyl)-N,N'-diethylpyridine-3,5-diamine dihydrochloride
Q16853
-
4-(aminomethyl)-N,N'-dimethylpyridine-3,5-diamine dihydrochloride
-
-
4-(aminomethyl)-N,N'-dimethylpyridine-3,5-diamine dihydrochloride
Q42432
-
4-(aminomethyl)-N,N'-dimethylpyridine-3,5-diamine dihydrochloride
Q16853
-
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
Q16853
-
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-fluorobenzylamine
-
-
-
4-hydroxybenzylhydrazine
-
-
-
4-phenoxybut-2-yn-1-amine
-
-
5-amino-2-hydroxy-N-(3-phenylpropyl)benzamide
-
-
8-hydroxyquinoline
-
0.0075 mM, 27% inhibition
8-hydroxyquinoline
F4IAX1, Q8H1H9, Q8L866
non-competitive inhibitor; non-competitive inhibitor; non-competitive inhibitor
alkylamino derivatives of 4-aminomethylpyridine, substratelike, reversible inhibitors
-
-
-
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
F4IAX1, Q8H1H9, Q8L866
irreversible competitive inhibitor; irreversible competitive inhibitor; irreversible competitive inhibitor
Aminoguanidine
-
isoform AO1 shows 18% residual activity at 0.1 mM, isoform AO2 shows 17% residual activity at 0.1 mM
benzylamine
O75106, Q16853
substrate inhibition
benzylhydrazine
-
forms adducts with the TPQ cofactor, binding structure, overview
but-3-yn-1-amine
-
-
buta-2,3-dien-1-amine
-
-
Cupricin
-
-
Cuprizone
-
copper chelating, 0.006 mM, 98% inhibition, competitive vs. benzylamine
Cuprizone
-
competitive binding to enzyme copper is suggested
Cuprizone
-
-
Cuprizone
-
isoform AO1 shows 2% residual activity at 0.1 mM, isoform AO2 shows 1% residual activity at 0.1 mM
cyanide
-
0.1 mM, 76% inhibition
cyanide
-
uncompetitive vs. benzylamine, non-competititve vs. O2
cysteamine
-
reversible inhibition
D-galactosamine
-
-
diethyldithiocarbamate
-
3.3 mM, 74% inhibition
diethyldithiocarbamate
-
no inhibition
EDTA
-
treatment with EDTA reduces the activity of wild type enzyme
extract from Taiwanofungus camphoratus
-
-
-
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
A1R2C3, A1RDD3
substrate inhibition; substrate inhibition
Hydrazines
-
-
hydroxylamine
-
3.3 mM, 30% inhibition
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
O75106, Q16853
;
imidazole
-
-
isonazid
-
isoform AO1 shows 14% residual activity at 0.1 mM, isoform AO2 shows 16% residual activity at 0.1 mM
-
Isoniazid
-
0.2 mM, 42% inhibition of dimeric enzyme, 39% inhibition of tetrameric enzyme
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
MDL 72223
-
-
-
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
Q6A174
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
Q43077
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
NaCl
-
100 mM, 88% inhibition of dimeric and tetrameric enzyme
NaN3
-
3.3 mM, 48% inhibition
NaN3
-
uncompetitive inhibition
NaN3
-
azide binds to Cu2+ ions, competitive inhibition vs. O2, uncompetitive vs. benzylamine
Neocuproine
-
0.033 mM, 61% inhibition
nitric oxide
Q9SW90
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
Phenelzine
-
0.001 mM, complete inhibition of enzyme from cultured aortic smooth muscle cells
Phenelzine
-
-
Phenylethylamine
-
-
phenylhydrazine
-
irreversible inactivation most likely due to hydrazone formation
phenylhydrazine
-
-
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
-
Semicarbazide
-
0.01 mM, complete inhibition of enzyme from cultured aortic smooth muscle cells
Semicarbazide
O08590
causes significant decreases in the oxidative deamination activity of four among the five substrates catalyzed by SSAO
Semicarbazide
-
0.2 mM, 49% inhibition of dimeric enzyme, 45% inhibition of tetrameric enzyme
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
O75106, Q16853
;
Semicarbazide
-
isoform AO1 shows 1% residual activity at 0.1 mM, isoform AO2 shows 2% residual activity at 0.1 mM
Sodium thioglycolate
-
slight
tacsimate
-
-
-
Tranylcypromine
-
fully reversible competitive onhibitor
Tranylcypromine
-
forms adducts with the TPQ cofactor, also termed (1R,2S)-rel-2-phenylcyclopropanamine, is a mixture of (1R,2S)-2-phenylcyclopropanamine and (1S,2R)-2-phenylcyclopropanamine, binding structure, overview
tryptamine
Q6A174
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
Q43077
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
O75106, Q16853
substrate inhibition
tyramine
Q6A174
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
Q43077
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
Q9SW90
irreversible inhibitor
tyramine
A1R2C3, A1RDD3
substrate inhibition; substrate inhibition
vanillylamine
-
-
[(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
-
-
mofegiline
-
-
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
O08590
clorgyline and deprenyl do not significantly inhibit the activities
-
additional information
-
no effect: DTT or EDTA at 1 mM, 1,4-diamino-2-butanone, sodium azide or KCN
-
additional information
-
no inhibition by pargyline. SSAO activity remains unchanged during starvation
-
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
-
not inhibited by 2-aminoethanol and 2-(N,N-dimethylamino)ethanethiol
-
additional information
-
not inhibited by pargyline, clorgyline, and neocupine
-
additional information
A1R2C3, A1RDD3
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Atx1-like protein
-
required for the synthesis of fully active Cao1
-
additional information
-
active Cao1 requires Ctr4/5-mediated copper transport and the transcription factor Cuf1
-
additional information
-
SSAO activity remains unchanged during starvation
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1
-
1,4-diamino-2-butyne
Q43077
-
1.7
-
2-aminoethylpyridine
-, I6NC69
in 50 mM Tris-HCl buffer, pH 8.0, at 25C
0.0012
-
2-Phenylethylamine
-
wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 25C
0.0019
-
2-Phenylethylamine
-
pH 6.8, 30C, Co2+-substituted enzyme
0.0021
-
2-Phenylethylamine
-
pH 6.8, 30C, mutant enzyme D298A
0.0025
-
2-Phenylethylamine
-
pH 6.8, 30C, native copper protein
0.0025
-
2-Phenylethylamine
-
pH 6.8, 30C, Co-activated enzyme; pH 6.8, 30C, Cu-activated enzyme
0.0025
-
2-Phenylethylamine
-
pH 6.8, 30C, wild-type enzyme
0.0025
-
2-Phenylethylamine
-
in 50mM HEPES buffer, pH 6.8, at 15C
0.0034
-
2-Phenylethylamine
-
pH 6.8, 30C, Ni-activated enzyme
0.0038
-
2-Phenylethylamine
-
pH 6.8, 30C, Ni2+-substituted enzyme
0.0055
-
2-Phenylethylamine
A1R2C3, A1RDD3
isoform AMAO3, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
0.012
-
2-Phenylethylamine
A1R2C3, A1RDD3
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
0.077
-
2-Phenylethylamine
O75106, Q16853
recombinant enzyme expressed in CHO cells
1.94
-
2-Phenylethylamine
O75106, Q16853
recombinant enzyme expressed in CHO cells
1.2
-
3-aminomethylpyridine
-, I6NC69
in 50 mM Tris-HCl buffer, pH 8.0, at 25C
1.9
-
4-aminomethylpyridine
-, I6NC69
in 50 mM Tris-HCl buffer, pH 8.0, at 25C
0.016
-
4-aminomethylpyridine dihydrochloride
Q16853
-
0.13
-
4-fluorobenzylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
-
0.066
-
aminoacetone
-
at pH 7.4, 37C
0.11
-
amylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
0.16
-
amylamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30C
5.71
-
amylamine
-
at pH 7.4, 37C
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
-
37C
0.013
-
benzylamine
-
mutant enzyme L469G, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37C
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 37C
0.025
-
benzylamine
-
mutant enzyme M211V, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37C
0.04
-
benzylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
0.061
-
benzylamine
-
37C
0.075
0.095
benzylamine
-
-
0.084
-
benzylamine
-
mutant enzyme T212A, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37C
0.0845
-
benzylamine
-
at pH 7.4, 37C
0.1
-
benzylamine
-
in 50mM HEPES buffer, pH 6.8, at 15C
0.124
-
benzylamine
Q16853
-
0.167
-
benzylamine
O75106, Q16853
recombinant enzyme expressed in CHO cells
0.184
-
benzylamine
-
wild type enzyme, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37C
0.215
-
benzylamine
-
mutant enzyme Y394N, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37C
0.287
-
benzylamine
-
37C
0.5
-
benzylamine
-, I6NC69
in 50 mM Tris-HCl buffer, pH 8.0, at 25C
0.682
-
benzylamine
-
recombinant enzyme
1.49
-
benzylamine
-
-
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 6.5, wild-type enzyme; pH 7.5, wild-type enzyme
0.0018
-
beta-phenylethylamine
-
pH 6.0, wild-type enzyme
0.0023
-
beta-phenylethylamine
-
pH 5.75, wild-type enzyme; pH 8.0, 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 30C; isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30C
2.83
-
Butylamine
-
at pH 7.4, 37C
0.3
-
cadaverine
-, I6NC69
in 50 mM Tris-HCl buffer, pH 8.0, at 25C
12.7
-
cadaverine
A1R2C3, A1RDD3
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
16.5
-
cyclohexanemethylamine
-
at pH 7.4, 37C
-
0.031
-
cysteamine
-
at pH 7.4, 37C
0.099
-
dopamine
-
at pH 7.4, 37C
0.1
-
dopamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30C
2.05
-
ethanolamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
0.86
-
ethylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
12.8
-
ethylamine
-
at pH 7.4, 37C
0.014
-
hexakis(benzylammonium) decavanadate (V) dihydrate
-
37C
0.0865
-
hexakis(benzylammonium) decavanadate (V) dihydrate
-
37C
0.213
-
hexakis(benzylammonium) decavanadate (V) dihydrate
-
37C
0.28
-
histamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30C
0.41
-
histamine
A1R2C3, A1RDD3
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
0.7
-
histamine
-, I6NC69
in 50 mM Tris-HCl buffer, pH 8.0, at 25C
0.88
-
histamine
A1R2C3, A1RDD3
isoform AMAO3, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
4.56
-
Isoamylamine
-
at pH 7.4, 37C
3.42
-
Isobutylamine
-
at pH 7.4, 37C
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 30C
0.236
-
Methylamine
-
mutant enzyme L469G, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37C
0.28
-
Methylamine
-
mutant enzyme M211V, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37C
0.331
-
Methylamine
-
wild type enzyme, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37C
0.502
-
Methylamine
-
mutant enzyme T212A, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37C
0.652
-
Methylamine
-
at pH 7.4, 37C
0.67
-
Methylamine
O75106, Q16853
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 37C
1.7
-
Methylamine
O75106, Q16853
recombinant enzyme expressed in CHO cells
0.0163
-
O2
-
pH 6.8, 30C, Co2+-substituted enzyme
0.0183
-
O2
-
pH 6.8, 30C, Ni2+-substituted enzyme
0.0208
-
O2
-
pH 6.8, 30C, native copper protein
0.021
-
O2
-
copper-reconstituted wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37C
0.026
-
O2
-
wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37C
1
-
O2
-
cobalt-substituted wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37C
0.03
-
Octopamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30C
2.05
-
phenethylamine
-
at pH 7.4, 37C
0.02
-
Phenylethylamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30C
0.49
-
Propylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
2.65
-
Propylamine
-
at pH 7.4, 37C
0.29
-
putrescine
-
copper-reconstituted wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.2, 37C
-
0.57
-
putrescine
-
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.2, 37C
-
1.2
-
putrescine
-, I6NC69
in 50 mM Tris-HCl buffer, pH 8.0, at 25C
-
0.8
-
spermidine
-, I6NC69
in 50 mM Tris-HCl buffer, pH 8.0, at 25C
7.04
-
spermidine
A1R2C3, A1RDD3
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
0.5
-
tryptamine
-
-
0.0104
-
tyramine
-
in 50mM HEPES buffer, pH 6.8, at 15C
0.02
-
tyramine
A1R2C3, A1RDD3
isoform AMAO3, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
0.03
-
tyramine
A1R2C3, A1RDD3
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
0.05
-
tyramine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30C
0.056
-
tyramine
O75106, Q16853
recombinant enzyme expressed in CHO cells
0.178
-
tyramine
O75106, Q16853
recombinant enzyme expressed in CHO cells
0.71
-
tyramine
-
-
0.02
-
vanillylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
2.043
-
Methylamine
-
mutant enzyme M211V/Y394N/L469G, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37C
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
O75106, Q16853
comparison of steady-state kinetics of enzyme expressed in CHO and HEK-293 EBNA cells, overview; 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
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.9
-
2-aminoethylpyridine
-, I6NC69
in 50 mM Tris-HCl buffer, pH 8.0, at 25C
0.00021
-
2-Phenylethylamine
-
pH 6.8, 30C, mutant enzyme D298A
0.63
-
2-Phenylethylamine
-
pH 6.8, 30C, Ni-activated enzyme
0.92
-
2-Phenylethylamine
-
pH 6.8, 30C, Co-activated enzyme
1.3
-
2-Phenylethylamine
-
pH 6.8, 30C, Ni2+-substituted enzyme
1.51
-
2-Phenylethylamine
-
pH 6.8, 30C, Co2+-substituted enzyme
1.72
-
2-Phenylethylamine
A1R2C3, A1RDD3
isoform AMAO3, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
5.12
-
2-Phenylethylamine
A1R2C3, A1RDD3
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
12.4
-
2-Phenylethylamine
-
wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 25C
44
-
2-Phenylethylamine
-
in 50mM HEPES buffer, pH 6.8, at 15C
75.7
-
2-Phenylethylamine
-
pH 6.8, 30C, native copper protein
75.7
-
2-Phenylethylamine
-
pH 6.8, 30C, Cu-activated enzyme
76
-
2-Phenylethylamine
-
pH 6.8, 30C, wild-type enzyme
1.9
-
3-aminomethylpyridine
-, I6NC69
in 50 mM Tris-HCl buffer, pH 8.0, at 25C
3.1
-
4-aminomethylpyridine
-, I6NC69
in 50 mM Tris-HCl buffer, pH 8.0, at 25C
17.3
-
4-fluorobenzylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
-
1.46
-
aminoacetone
-
at pH 7.4, 37C
4.33
-
amylamine
-
at pH 7.4, 37C
5.9
-
amylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
12.7
-
amylamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30C
0.066
-
benzylamine
E7R5K2
isoform HPAO-1, at 25C, in 100 mM potassium phosphate, pH 7.2
0.066
-
benzylamine
-
in 100 mM potassium phosphate, pH 7.2, temperature not specified in the publication
0.24
-
benzylamine
-
in 50mM HEPES buffer, pH 6.8, at 15C
1.4
-
benzylamine
-, I6NC69
in 50 mM Tris-HCl buffer, pH 8.0, at 25C
3.42
-
benzylamine
-
at pH 7.4, 37C
8.1
-
benzylamine
E7R5K2
isoform HPAO-2, at 25C, in 100 mM potassium phosphate, pH 7.2
12.1
-
benzylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
188
198
benzylamine
-
-
0.00612
-
beta-phenylethylamine
-
pH 8.0, mutant enzyme D383E
0.00937
-
beta-phenylethylamine
-
pH 7.0, mutant enzyme D383E
0.01163
-
beta-phenylethylamine
-
pH 5.5, mutant enzyme D383E
0.012
-
beta-phenylethylamine
-
pH 6.0, mutant enzyme D383E
9.6
-
beta-phenylethylamine
-
pH 5.5, wild-type enzyme
11.45
-
beta-phenylethylamine
-
pH 5.75, wild-type enzyme
13.32
-
beta-phenylethylamine
-
pH 7.5, wild-type enzyme
13.68
-
beta-phenylethylamine
-
pH 8.0, wild-type enzyme
14.98
-
beta-phenylethylamine
-
pH 7.0, wild-type enzyme
20.7
-
beta-phenylethylamine
-
pH 6.0, wild-type enzyme
20.77
-
beta-phenylethylamine
-
pH 6.5, wild-type enzyme
4.3
-
Butylamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30C
6.31
-
Butylamine
-
at pH 7.4, 37C
15.3
-
Butylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
0.0619
-
cadaverine
A1R2C3, A1RDD3
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
1
-
cadaverine
-, I6NC69
in 50 mM Tris-HCl buffer, pH 8.0, at 25C
5.36
-
cyclohexanemethylamine
-
at pH 7.4, 37C
-
1.11
-
cysteamine
-
at pH 7.4, 37C
0.54
-
dopamine
-
at pH 7.4, 37C
1.9
-
dopamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30C
3.3
-
ethanolamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
0.16
-
ethylamine
-
pH 7, 37C, mutant enzyme Y305F
6.12
-
ethylamine
-
at pH 7.4, 37C
7.2
-
ethylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
7.5
-
ethylamine
-
pH 7, 37C, mutant enzyme Y305A
20
-
ethylamine
-
pH 7, 37C, wild-type enzyme
20
-
ethylamine
-
in 100 mM potassium phosphate, pH 7.2, temperature not specified in the publication
0.46
-
histamine
A1R2C3, A1RDD3
isoform AMAO3, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
1.8
-
histamine
-, I6NC69
in 50 mM Tris-HCl buffer, pH 8.0, at 25C
5.91
-
histamine
A1R2C3, A1RDD3
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
13.2
-
histamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30C
6.89
-
Isoamylamine
-
at pH 7.4, 37C
7.4
-
Isobutylamine
-
at pH 7.4, 37C
0.4
-
Methylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
2.08
-
Methylamine
-
Co2+ reconstituted enzyme
2.12
-
Methylamine
-
native enzyme
2.18
-
Methylamine
E7R5K2
isoform HPAO-2, at 25C, in 100 mM potassium phosphate, pH 7.2
5.6
-
Methylamine
-
at pH 7.4, 37C
6.2
-
Methylamine
E7R5K2
isoform HPAO-1, at 25C, in 100 mM potassium phosphate, pH 7.2
1.13
-
O2
-
pH 6.8, 30C, Ni2+-substituted enzyme
1.24
-
O2
-
pH 6.8, 30C, Co2+-substituted enzyme
2.1
-
O2
-
Co-substituted enzyme
7.1
-
O2
-
cobalt-substituted wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37C
7.8
-
O2
-
wild-type enzyme
99
-
O2
-
copper-reconstituted wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37C
110
-
O2
-
pH 6.8, 30C, native copper protein
152
-
O2
-
wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37C
3.5
-
Octopamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30C
1.12
-
phenethylamine
-
at pH 7.4, 37C
20.9
-
Phenylethylamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30C
5.8
-
Propylamine
-
at pH 7.4, 37C
18.9
-
Propylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
1.9
-
putrescine
-, I6NC69
in 50 mM Tris-HCl buffer, pH 8.0, at 25C
-
82
-
putrescine
-
copper-reconstituted wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.2, 37C
-
160
-
putrescine
-
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.2, 37C
-
0.0429
-
spermidine
A1R2C3, A1RDD3
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
2.3
-
spermidine
-, I6NC69
in 50 mM Tris-HCl buffer, pH 8.0, at 25C
2.7
-
tryptamine
-
-
1.6
-
tyramine
A1R2C3, A1RDD3
isoform AMAO3, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
3.95
-
tyramine
A1R2C3, A1RDD3
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
12.8
-
tyramine
-
-
16.1
-
tyramine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30C
35
-
tyramine
-
in 50mM HEPES buffer, pH 6.8, at 15C
1
-
vanillylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.7
-
2-aminoethylpyridine
-, I6NC69
in 50 mM Tris-HCl buffer, pH 8.0, at 25C
263443
314
-
2-Phenylethylamine
A1R2C3, A1RDD3
isoform AMAO3, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
18951
429
-
2-Phenylethylamine
A1R2C3, A1RDD3
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
18951
10330
-
2-Phenylethylamine
-
wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 25C
18951
1.6
-
3-aminomethylpyridine
-, I6NC69
in 50 mM Tris-HCl buffer, pH 8.0, at 25C
82641
1.6
-
4-aminomethylpyridine
-, I6NC69
in 50 mM Tris-HCl buffer, pH 8.0, at 25C
263442
133
-
4-fluorobenzylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
0
22.3
-
aminoacetone
-
at pH 7.4, 37C
6945
0.757
-
amylamine
-
at pH 7.4, 37C
20002
54
-
amylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
20002
79
-
amylamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30C
20002
0.09
-
benzylamine
E7R5K2
isoform HPAO-1, at 25C, in 100 mM potassium phosphate, pH 7.2
7478
0.09
-
benzylamine
-
in 100 mM potassium phosphate, pH 7.2, temperature not specified in the publication
7478
2.8
-
benzylamine
-, I6NC69
in 50 mM Tris-HCl buffer, pH 8.0, at 25C
7478
40.5
-
benzylamine
-
at pH 7.4, 37C
7478
303
-
benzylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
7478
900
-
benzylamine
E7R5K2
isoform HPAO-2, at 25C, in 100 mM potassium phosphate, pH 7.2
7478
2.23
-
Butylamine
-
at pH 7.4, 37C
8143
13
-
Butylamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30C
8143
48
-
Butylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
8143
3.3
-
cadaverine
-, I6NC69
in 50 mM Tris-HCl buffer, pH 8.0, at 25C
8177
0.325
-
cyclohexanemethylamine
-
at pH 7.4, 37C
0
35.5
-
cysteamine
-
at pH 7.4, 37C
8936
5.44
-
dopamine
-
at pH 7.4, 37C
10197
19
-
dopamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30C
10197
2
-
ethanolamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
10368
0.478
-
ethylamine
-
at pH 7.4, 37C
10412
8
-
ethylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
10412
52
-
ethylamine
-
in 100 mM potassium phosphate, pH 7.2, temperature not specified in the publication
10412
0.52
-
histamine
A1R2C3, A1RDD3
isoform AMAO3, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
11436
2.6
-
histamine
-, I6NC69
in 50 mM Tris-HCl buffer, pH 8.0, at 25C
11436
14.6
-
histamine
A1R2C3, A1RDD3
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
11436
47
-
histamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30C
11436
1.51
-
Isoamylamine
-
at pH 7.4, 37C
11757
2.16
-
Isobutylamine
-
at pH 7.4, 37C
11769
1.2
-
Methylamine
E7R5K2
isoform HPAO-2, at 25C, in 100 mM potassium phosphate, pH 7.2
13100
2
-
Methylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
13100
8.58
-
Methylamine
-
at pH 7.4, 37C
13100
30
-
Methylamine
E7R5K2
isoform HPAO-1, at 25C, in 100 mM potassium phosphate, pH 7.2
13100
7.1
-
O2
-
cobalt-substituted wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37C
14738
81
-
O2
E7R5K2
isoform HPAO-1, using benzylamine as cosubstrate, at 25C, in 100 mM potassium phosphate, pH 7.2
14738
160
-
O2
E7R5K2
isoform HPAO-2, using methylamine as cosubstrate, at 25C, in 100 mM potassium phosphate, pH 7.2
14738
400
-
O2
E7R5K2
isoform HPAO-1, using methylamine as cosubstrate, at 25C, in 100 mM potassium phosphate, pH 7.2
14738
470
-
O2
E7R5K2
isoform HPAO-2, using benzylamine as cosubstrate, at 25C, in 100 mM potassium phosphate, pH 7.2
14738
3320
-
O2
-
wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37C
14738
4640
-
O2
-
copper-reconstituted wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37C
14738
116
-
Octopamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30C
14774
0.545
-
phenethylamine
-
at pH 7.4, 37C
22750
1045
-
Phenylethylamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30C
15445
2.19
-
Propylamine
-
at pH 7.4, 37C
15859
39
-
Propylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
15859
0.15
-
putrescine
A1R2C3, A1RDD3
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
0
1.6
-
putrescine
-, I6NC69
in 50 mM Tris-HCl buffer, pH 8.0, at 25C
0
270
-
putrescine
-
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.2, 37C
0
280
-
putrescine
-
copper-reconstituted wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.2, 37C
0
2.9
-
spermidine
-, I6NC69
in 50 mM Tris-HCl buffer, pH 8.0, at 25C
16687
82.3
-
tyramine
A1R2C3, A1RDD3
isoform AMAO3, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
17592
133
-
tyramine
A1R2C3, A1RDD3
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
17592
322
-
tyramine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30C
17592
50
-
vanillylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
213877
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.32
-
1,4-diamino-2-butyne
Q43077
-
0.01
-
1,5-diamino-2-pentyne
-
-
0.05
-
1,5-diamino-2-pentyne
Q6A174
-
0.054
-
2-Bromoethylamine
-
-
0.08
-
2-Phenylethylamine
O75106, Q16853
recombinant enzyme expressed in CHO cells
0.84
-
2-Phenylethylamine
A1R2C3, A1RDD3
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
1.41
-
2-Phenylethylamine
A1R2C3, A1RDD3
isoform AMAO3, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
0.28
-
3,3-bis(aminoethyl)-1-hydroxy-2-oxo-1-triazene
-
-
0.042
-
3-(4-methoxyphenyl)-N-methyl-5-(1H-pyrrol-2-yl)-4,5-dihydro-1H-pyrazole-1-carbothioamide
-
60 min preincubation
0.07011
-
3-(4-methoxyphenyl)-N-methyl-5-(1H-pyrrol-2-yl)-4,5-dihydro-1H-pyrazole-1-carbothioamide
-
no preincubation
0.8
-
4-fluorobenzylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
-
3.1
-
amylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
40
-
azide
-
vs. benzylamine
84
-
azide
-
vs. O2
0.089
-
benzylamine
O75106, Q16853
recombinant enzyme expressed in CHO cells
4.1
-
benzylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
9.9
-
Butylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
0.014
-
Cuprizone
-
-
0.76
-
cyanide
-
vs. O2, deduced from slope
2.17
-
cyanide
-
vs. benzylamine
2.9
-
cyanide
-
vs. O2, deduced from intercept
1.4
-
dopamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30C
0.0007
-
geraniin
-
pH 7.4, 37C
3.51
-
histamine
A1R2C3, A1RDD3
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
0.0374
-
L-Lys
-
pH 7.2, 37C
0.225
-
N-allyl-3-(4-methoxyphenyl)-5-(1H-pyrrol-2-yl)-4,5-dihydro-1H-pyrazole-1-carbothioamide
-
60 min preincubation
0.28
-
N-allyl-3-(4-methoxyphenyl)-5-(1H-pyrrol-2-yl)-4,5-dihydro-1H-pyrazole-1-carbothioamide
-
no preincubation
0.17
-
N-ethyl-3-(4-methoxyphenyl)-5-(1H-pyrrol-2-yl)-4,5-dihydro-1H-pyrazole-1-carbothioamide
-
60 min preincubation
0.23
-
N-ethyl-3-(4-methoxyphenyl)-5-(1H-pyrrol-2-yl)-4,5-dihydro-1H-pyrazole-1-carbothioamide
-
no preincubation
40
-
N3-
-
approx. value
0.6
-
Octopamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30C
0.6
-
Phenylethylamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30C
0.0054
-
Semicarbazide
-
37C, 60 min preincubation
0.0128
-
Semicarbazide
-
37C, no preincubation
0.032
-
tryptamine
O75106, Q16853
recombinant enzyme expressed in CHO cells
0.4
-
tyramine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30C
1.08
-
tyramine
A1R2C3, A1RDD3
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
2.93
-
tyramine
A1R2C3, A1RDD3
isoform AMAO3, in 100 mM potassium phosphate buffer (pH 7.0), at 37C
2.9
-
vanillylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30C
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5.5e-05
-
(2-methylprop-2-en-1-yl)hydrazine
-
-
2e-06
-
(2-phenylprop-2-en-1-yl)hydrazine
-
-
3.5e-05
-
(2-phenylprop-2-en-1-yl)hydrazine
-
-
0.002
-
(2E)-3-chloroprop-2-en-1-amine
-
-
0.011
-
(2Z)-3-chloroprop-2-en-1-amine
-
-
4e-06
-
(Z)-3-fluoro-2-(4-methoxybenzyl)allylamine hydrochloride
-
-
9e-06
-
(Z)-3-fluoro-2-(4-methoxybenzyl)allylamine hydrochloride
-
-
2.7e-05
-
(Z)-3-fluoro-2-(4-methoxybenzyl)allylamine hydrochloride
-
enzyme from umbilical cord
4.3e-05
-
(Z)-3-fluoro-2-(4-methoxybenzyl)allylamine hydrochloride
-
lysates of human SSAO-expressing CHO cells
0.00086
-
1-(2,5-dihydro-1H-pyrrol-3-yl)isoquinoline
-
-
0.00017
-
1-(3,5-diethoxypyridin-4-yl)methanamine dihydrochloride
Q16853
-
0.33
-
1-(3,5-diethoxypyridin-4-yl)methanamine dihydrochloride
Q42432
-
7.8e-05
-
1-(isoquinolin-1-ylcarbonyl)pyrrolidine-2-carboxamide
-
-
0.00023
-
1-ethyl-2-[2-(4-fluorophenyl)prop-2-en-1-yl]hydrazine
-
-
1.7e-06
-
1-[2-(4-fluorophenyl)prop-2-en-1-yl]-2-methylhydrazine
-
-
0.00013
-
1-[3,5-bis(ethylsulfanyl)pyridin-4-yl]methanamine dihydrochloride
Q16853
-
0.0016
-
1-[3,5-bis(tert-butylsulfanyl)pyridin-4-yl]methanamine dihydrochloride
Q16853
-
0.005
-
1-[3-(benzyloxy)-5-ethoxypyridin-4-yl]methanamine dihydrochloride
Q16853
-
0.00075
-
2-(2,5-dihydro-1H-pyrrol-3-yl)pyridine
-
-
2.6e-06
-
2-(4-[2-[2-(acetylamino)-2,3-dihydro-1,3-thiazol-4-yl]ethyl]phenyl)-N-[amino(imino)methyl]acetamide
-
-
9e-05
-
2-(aminooxy)-1-(3,4-dimethoxyphenyl)ethanol
-
-
5e-05
-
2-(aminooxy)-1-phenylethanol
-
-
5
-
2-(methylamino)ethanethiol
-
in 100 mM potassium phosphate buffer, pH 7.2, at 30C
-
1.3
-
2-(methylthio)ethylamine
-
in 100 mM potassium phosphate buffer, pH 7.2, at 30C
4e-06
-
2-([[4-(1,1-dimethylpropyl)phenyl]sulfonyl]amino)-N,3-dihydroxybutanamide
-
-
1.5e-05
-
2-amino-N-[2-fluoro-3-(trifluoromethyl)benzyl]acetamide
-
-
1e-05
-
2-amino-N-[2-fluoro-5-(trifluoromethyl)benzyl]acetamide
-
-
3.3e-05
-
2-amino-N-[3-fluoro-5-(trifluoromethyl)benzyl]acetamide
-
-
0.00018
-
2-amino-N-[4-fluoro-3-(trifluoromethyl)benzyl]acetamide
-
-
1.5
-
2-ethylaminobenzylamine dihydrochloride
-
-
0.75
-
2-methylaminobenzylamine dihydrochloride
-
-
0.000125
-
2-[(biphenyl-4-ylacetyl)amino]pentanedioic acid
-
-
0.0032
-
3,3'-[[4-(aminomethyl)pyridine-3,5-diyl]bis(oxy)]dipropan-1-ol dihydrochloride
Q16853
-
0.1
-
3-(1-piperidinyl)-4-aminomethylpyridine dihydrochloride hemihydrate
Q16853
-
0.0015
-
3-(2,5-dihydro-1H-pyrrol-3-yl)pyridine
-
-
0.042
-
3-(4-methoxyphenyl)-N-methyl-5-(1H-pyrrol-2-yl)-4,5-dihydro-1H-pyrazole-1-carbothioamide
-
-
0.016
-
3-amino-4-aminomethylpyridine dihydrochloride
Q16853
-
0.3
-
3-aminopropanethiol
-
in 100 mM potassium phosphate buffer, pH 7.2, at 30C
-
0.01
-
3-bromoprop-2-yn-1-amine
-
-
0.079
-
3-cycloheptylamino-4-aminomethylpyridine dihydrochloride monohydrate
Q16853
-
1
-
3-cycloheptylamino-4-aminomethylpyridine dihydrochloride monohydrate
Q42432
-
0.0056
-
3-cyclohexylamino-4-aminomethylpyridine dihydrochloride monohydrate
Q16853
-
0.0056
-
3-cyclohexylmethylamino-4-aminomethylpyridine dihydrochloride monohydrate
Q16853
-
0.54
-
3-cyclohexylmethylamino-4-aminomethylpyridine dihydrochloride monohydrate
-
-
0.89
-
3-cyclohexylmethylamino-4-aminomethylpyridine dihydrochloride monohydrate
Q42432
-
0.016
-
3-cyclopentylamino-4-aminomethylpyridine dihydrochloride hemihydrate
Q16853
-
0.7
-
3-cyclopentylamino-4-aminomethylpyridine dihydrochloride hemihydrate
-
-
0.002
-
3-ethylamino-4-aminomethylpyridine dihydrochloride
Q16853
-
0.0093
-
3-ethylamino-4-aminomethylpyridine dihydrochloride
Q42432
-
0.087
-
3-ethylamino-4-aminomethylpyridine dihydrochloride
-
-
0.00071
-
3-methylamino-4-aminomethylpyridine dihydrochloride
Q42432
-
0.008
-
3-methylamino-4-aminomethylpyridine dihydrochloride
Q16853
-
0.053
-
3-methylamino-4-aminomethylpyridine dihydrochloride
-
-
0.1
-
3-[(1-methylethyl)amino]-4-aminomethylpyridine dihydrochloride
Q16853
-
0.0005
-
3-[2-(3-methoxyphenyl)ethyl]-2,5-dihydro-1H-pyrrole
-
-
0.00015
-
4,4'-[[4-(aminomethyl)pyridine-3,5-diyl]bis(oxy)]dibutan-1-ol dihydrochloride
Q16853
-
0.025
-
4-(2-naphthyloxy)but-2-yn-1-amine
-
-
0.02
-
4-(4-methoxyphenoxy)but-2-yn-1-amine
-
-
0.022
-
4-(4-methylphenoxy)but-2-yn-1-amine
-
-
0.02
-
4-(4-nitrophenoxy)but-2-yn-1-amine
-
-
0.35
-
4-(aminomethyl)-N,N'-dibutylpyridine-3,5-diamine dihydrochloride
Q16853
-
0.03
-
4-(aminomethyl)-N,N'-diethylpyridazine-3,5-diamine
-
pH not specified in the publication, temperature not specified in the publication
-
2e-05
-
4-(aminomethyl)-N,N'-diethylpyridine-3,5-diamine dihydrochloride
Q16853
-
0.055
-
4-(aminomethyl)-N,N'-diethylpyridine-3,5-diamine dihydrochloride
Q42432
-
0.35
-
4-(aminomethyl)-N,N'-diethylpyridine-3,5-diamine dihydrochloride
-
-
0.00044
-
4-(aminomethyl)-N,N'-dimethylpyridine-3,5-diamine dihydrochloride
Q16853
-
0.017
-
4-(aminomethyl)-N,N'-dimethylpyridine-3,5-diamine dihydrochloride
Q42432
-
0.1
-
4-(aminomethyl)-N,N'-dimethylpyridine-3,5-diamine dihydrochloride
-
-
0.0017
-
4-(aminomethyl)-N-methylpyridine-3,5-diamine dihydrochloride
Q16853
-
0.000146
-
4-amino-3-hydroxy-N-(3-phenylpropyl)benzamide
-
-
0.013
-
4-aminobut-2-ynenitrile
-
-
0.0001
-
4-bromo-N-[2-(hydroxyamino)-2-oxoethyl]benzamide
-
-
0.2
-
4-phenoxybut-2-yn-1-amine
-
-
0.000575
-
5-amino-2-hydroxy-N-(3-phenylpropyl)benzamide
-
-
0.0029
-
but-3-yn-1-amine
-
-
0.00125
-
buta-2,3-dien-1-amine
-
-
0.0125
-
cysteamine
-
in 100 mM potassium phosphate buffer, pH 7.2, at 30C
0.00658
-
geraniin
-
pH 7.4, 37C
5.4e-05
-
N,3-dihydroxy-2-[(2-naphthylsulfonyl)amino]butanamide
-
-
0.225
-
N-allyl-3-(4-methoxyphenyl)-5-(1H-pyrrol-2-yl)-4,5-dihydro-1H-pyrazole-1-carbothioamide
-
-
0.17
-
N-ethyl-3-(4-methoxyphenyl)-5-(1H-pyrrol-2-yl)-4,5-dihydro-1H-pyrazole-1-carbothioamide
-
-
3.3e-05
-
N-[2-(hydroxyamino)-2-oxoethyl]-2-(2-methyl-1H-indol-3-yl)acetamide
-
-
5.3e-06
-
N-[4-(2-[4-[(2-amino-1H-imidazol-5-yl)methyl]phenyl]ethyl)-1,3-thiazol-2-yl]acetamide
-
-
4.5e-06
-
N-[4-[2-(4-carbamimidamidophenyl)ethyl]-5-(4-sulfamoylbenzyl)-1,3-thiazol-2-yl]acetamide
-
-
0.00015
-
N-[4-[2-(4-[[amino(imino)methyl]amino]phenyl)ethyl]-1,3-thiazol-2-yl]acetamide
-
-
5e-06
-
[(2E)-3-fluoro-2-phenylprop-2-en-1-yl]hydrazine
-
-
4e-06
-
[2-(2-methylphenyl)prop-2-en-1-yl]hydrazine
-
-
3e-06
-
[2-(4-chlorophenyl)prop-2-en-1-yl]hydrazine
-
-
6e-06
-
[2-(4-fluorophenyl)prop-2-en-1-yl]hydrazine
-
-
2e-05
-
mofegiline
-
pH and temperature not specified in the publication
additional information
-
additional information
-
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
Q42432
above 0.1 mM for 2-methylaminobenzylamine dihydrochloride and 2-ethylaminobenzylamine dihydrochloride
-
additional information
-
additional information
Q16853
above 0.1 for 2-methylaminobenzylamine dihydrochloride, 3-cyclopropylamino-4-aminomethylpyridine dihydrochloride sesquihydrate, and 2-ethylaminobenzylamine dihydrochloride, above 0.0001 for 3d
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00015
-
O08590
substrate benzylamine, at low substrate concentration
0.00023
-
O08590
substrate beta-phenylethylamine, at low substrate concentration
0.00025
-
O08590
substrate tyramine, at low substrate concentration
0.00078
-
O08590
substrate 1-methylhistamine, at low substrate concentration
0.00108
-
O08590
substrate tyramine, at high substrate concentration
0.00136
-
O08590
substrate beta-phenylethylamine, at high substrate concentration
0.00165
-
O08590
substrate 1-methylhistamine, at high substrate concentration
0.00193
-
O08590
substrate benzylamine, at high substrate concentration
0.0038
-
-
mutant enzyme D383E
0.00388
-
O08590
substrate serotonin, at high substrate concentration
0.00555
-
-
-
0.016
-
-
copper-depleted wild type enzyme, with 4-N,N-dimethylaminomethyl benzylamine as substrate, in 100 mM potassium phosphate buffer, pH 7.2, 37C
0.0193
-
-
copper depleted, reconstituted with Zn2+
0.0195
-
-
copper depleted, reconstituted with Ni2+
0.039
-
-
isoform AO1, crude extract, in 200 mM potassium phosphate buffer pH 7.6, at 30C
0.0571
-
-
copper depleted enzyme
0.105
-
-
-
0.144
-
-
isoform AO2, crude extract, in 200 mM potassium phosphate buffer pH 7.6, at 30C
0.213
-
-
copper depleted, reconstituted with Co2+
0.38
-
-
cobalt-substituted wild type enzyme, with 4-N,N-dimethylaminomethyl benzylamine as substrate, in 100 mM potassium phosphate buffer, pH 7.2, 37C
0.894
-
-
copper depleted, reconstituted with Cu2+
1.13
-
-
native enzyme
2.08
-
-
enzyme from cultured aortic smooth muscle cells
3.1
-
-
tetrameric enzyme
5.6
-
-
recombinant enzyme, methylamine oxidation
6.302
-
-
isoform AO1, after 161.5fold purification, in 200 mM potassium phosphate buffer pH 7.6, at 30C
6.7
-
-
dimeric enzyme
7
-
-
copper-reconstituted wild type enzyme, with 4-N,N-dimethylaminomethyl benzylamine as substrate, in 100 mM potassium phosphate buffer, pH 7.2, 37C
11
-
-
wild-type enzyme
13.14
-
-
isoform AO2, after 91.3fold purification, in 200 mM potassium phosphate buffer pH 7.6, at 30C
13.6
-
-
wild type enzyme, with 4-N,N-dimethylaminomethyl benzylamine as substrate, in 100 mM potassium phosphate buffer, pH 7.2, 37C
additional information
-
-
1100.0-1200.0 units/mg, 1 unit is defined as the amount of enzyme catalyzing a change of 0.001 absorbance per minute at 25C
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
A1R2C3, A1RDD3
isoform AMAO2
7
-
-
specific activities of dimeric and tetrameric enzyme form in Tris buffer at pH 7.0 is about 6fold lower than those in phosphate buffer at same pH
7
-
A1R2C3, A1RDD3
isoform AMAO3
7.4
-
-
assay at
7.4
-
-
assay at
7.6
-
-
assay at
8
-
-, I6NC69
pH optimum for the piperideine-forming activity oft he enzyme
9
-
-
50 mM glycine, 1 mM EDTA
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.6
10.2
-
assay range
6
10
-
-
6.8
8.5
-, I6NC69
piperideine-forming activity
additional information
-
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35
-
A1R2C3, A1RDD3
isoform AMAO3
37
-
-
assay at
37
-
-
assay at
40
-
-
-
55
-
A1R2C3, A1RDD3
isoform AMAO2
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
40
-
relative activity at 20C: 22.8, at 40C: 31.2
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.6
-
-
isoform AO1, calculated from amino acid sequence
4.9
-
-
isoform AO2, calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
most of the SSAO found in adipose tissue originates from mature adipocytes
Manually annotated by BRENDA team
-
major SSAO form expressed in mouse adipocytes is encoded by the AOC3 gene; the major SSAO form expressed in mouse adipocytes is encoded by the AOC3 gene
Manually annotated by BRENDA team
-
SSAO inhibition is not sufficient to impair fat deposition. However, combined monoamine oxidase (EC 1.4.3.4) inhibition and SSAO inhibition limits adiposity in non-obese as well as in obese rats
Manually annotated by BRENDA team
-
SSAO activity regulates NO availability in white adipose tissue
Manually annotated by BRENDA team
-
most of the SSAO found in adipose tissue originates from mature adipocytes
Manually annotated by BRENDA team
-
SSAO activity is present in white adipose tissues of wild type but is absent in AOC3KO mice
Manually annotated by BRENDA team
-
semicarbazide-sensitive amine oxidase overexpression in cerebrovascular tissue of patients with Alzheimers disease cerebral amyloid angiopathy correlates with high SSAO activity in plasma of severe Alzheimers disease patients
Manually annotated by BRENDA team
-
decreased SSAO serum activity in schizophrenic patients treated with second generation antipsychotics known to disturb glucose metabolism
Manually annotated by BRENDA team
-
reduced enzyme activity is found in haemodialysed uremic patients before and after dialysis treatment, compared to controls. The activity is slightly lower in peritoneally dialysed, and normal in not dialysed patients. In haemodialysed patients SSAO activity is elevated compared to controls
Manually annotated by BRENDA team
-
treatment with benzylamine + vanadate reduces the elevated serum SSAO activity, decreases the accumulation of advanced-glycation end products and increases the bioavailability of nitric oxide in diabetic animals, similarly to insulin
Manually annotated by BRENDA team
-
cerebral vascular SSAO-catalysed deamination contributes to cerebral amyloid angiopathy in Alzheimers disease brains
Manually annotated by BRENDA team
O75106, Q16853
-
Manually annotated by BRENDA team
O75106, Q16853
-
Manually annotated by BRENDA team
-
semicarbazide-sensitive amine oxidase is overexpressed in cerebrovascular tissue of patients with Alzheimers disease cerebral amyloid angiopathy. The enzyme colocalizes with beta-amyloid deposits
Manually annotated by BRENDA team
Mycobacterium sp. JC1
-
-
-
Manually annotated by BRENDA team
F4IAX1, Q8H1H9, Q8L866
-
Manually annotated by BRENDA team
-
CuAO in Vicia faba guard cells is an essential enzymatic source for H2O2 production in absicic acid-induced stomatal closure via the degradation of putrescine
Manually annotated by BRENDA team
F4IAX1, Q8H1H9, Q8L866
-
Manually annotated by BRENDA team
-
luminal expression, immunohistochemic analysis, overview
Manually annotated by BRENDA team
O75106, Q16853
-
Manually annotated by BRENDA team
O75106, Q16853
;
Manually annotated by BRENDA team
-
significantly elevated serum SSAO activity in diabetic patients, overview
Manually annotated by BRENDA team
O75106, Q16853
-
Manually annotated by BRENDA team
F4IAX1, Q8H1H9, Q8L866
-
Manually annotated by BRENDA team
O75106, Q16853
-
Manually annotated by BRENDA team
O75106, Q16853
;
Manually annotated by BRENDA team
additional information
O75106, Q16853
tissue expression pattern of AOC2, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
F4IAX1, Q8H1H9, Q8L866
isoform CuAO1
-
Manually annotated by BRENDA team
O75106, Q16853
;
Manually annotated by BRENDA team
F4IAX1, Q8H1H9, Q8L866
isoform CuAO2; isoform CuAO3
Manually annotated by BRENDA team
Ogataea angusta 1A2V
-
;
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
140000
-
-
gel filtration
150000
-
-
dimer, gel filtration
162000
-
-, I6NC69
gel filtration
184000
-
-
non-denaturing PAGE
186000
-
-
sedimentation-equilibrium
196000
-
-
gradient PAGE
300000
-
-
tetramer, gel filtration
1200000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 130000, SDS-PAGE
?
E7R5K2
x * 72000, SDS-PAGE
?
-
x * 30000, SDS-PAGE
dimer
-
2 * 95000, SDS-PAGE
dimer
-
2 * 97000, SDS-PAGE
dimer
-
2 * 75000, SDS-PAGE
dimer
-
2 * 93000, SDS-PAGE after treatment with 2-mercaptoethanol
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
dimer
Mycobacterium sp. JC1
-
2 * 75000, SDS-PAGE
-
dimer
Schizosaccharomyces pombe FY435
-
-
-
homodimer
-
x-ray crystallography
homodimer
-, I6NC69
2 * 77676, calculated from amino acid sequence; 2 * 78000, SDS-PAGE
homodimer
-
2 * 70000, isoform AO1 or AO2, SDS-PAGE; 2 * 71695, isoform AO1, calculated from amino acid sequence; 2 * 72051, isoform AO2, calculated from amino acid sequence
homodimer
Q9SW90
2 * 74000, calculated from amino acid sequence
homodimer
Rhodococcus opacus DSM 43250
-
2 * 70000, isoform AO1 or AO2, SDS-PAGE; 2 * 71695, isoform AO1, calculated from amino acid sequence; 2 * 72051, isoform AO2, calculated from amino acid sequence
-
octamer
-
8 * 146000
tetramer
-
4 * 75000, SDS-PAGE
tetramer
-
-
tetramer
Mycobacterium sp. JC1
-
4 * 75000, SDS-PAGE
-
homotetramer
-
MAO-N exists as a homotetramer with a large channel at its centre
additional information
-
Escherichia coli copper amine oxidase possesses an extra N-terminal domain that lies close to one entrance to the beta-sandwich in the structurally conserved beta-sandwich structure
additional information
O75106, Q16853
AOC2 structure homology modelling, comparison with AOC3; AOC3 structure homology modelling, comparison with AOC2
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
heterogenity of pig plasma amine oxidase may be due to variable carbohydrate content
flavoprotein
-
-
additional information
Q6A174
topaquinone is derived by post-translational modification of a conserved tyrosine residue in the protein chain
additional information
-
topaquinone is derived by post-translational modification of a conserved tyrosine residue in the protein chain
additional information
Q43077
topaquinone is derived by post-translational modification of a conserved tyrosine residue in the protein chain
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
complexed with benzylhydrazine, 4-hydroxybenzylhydrazine and phenylhydrazine, micro dialysis method, using 1.05 M potassium sodium tartrate in 25mM HEPES buffer, pH 6.8, at 16C
-
hanging-drop vapor diffusion method. Crystal structures of a series of Ru(II)-wire-enzyme complexes differing with respect to the length of the alkane linker
-
holenzyme, in which topaquinone is generated by incubation with Co2+ or Ni2+ and apoenzyme are crystallized by microdialysis method
-
purified recombinant C-terminal StrepII-tagged enzyme in complex with inhibitors benzylhydrazine or tranylcypromine, vapour diffusion in hanging drop method, mixing of protein solution containing about 10 mg/ml protein in 50 mM HEPES, pH 7.0, with well solution containing 1.6 M ammonium sulfate and 150 mM sodium citrate pH 7.0. CuSO4, in a twofold molar excess, 2 weeks. The crystals are then transferred to a sitting drop well solution containing 30% v/v glycerol and 2 mM benzylhydrazine dihydrochloride or 0.4 mM tranylcypromine for 30 min, X-ray diffraction structure determination and analysis at 1.65-1.86 A resolution
-
the X-ray crystal structure of D298K at 1.7 A resolution
-
X-ray crystal structures of the Co2+ and Ni2+-enzyme are solved at 2.0-1.8 A resolution
-
purified recombinant genetic variants MAO-N-3 and MAO-N-5, from 10% w/v PEG 3350, 0.2 M proline, 0.1 M HEPES, pH 7.5, or 10% w/v PEG 5000 MME, 5% v/v tacsimate, 0.1 M HEPES, pH 7.0, with no difference in diffraction quality between the crystals from the two conditions, X-ray diffraction structure determination and analysis at 2.45 A and 1.85 A resolution, respectively
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purified recombinant mutants MAO-N-D3 and MAO-N-D5, and truncated selenomethionine-labeled mutant MAO-N-D5, X-ray diffraction structure determination and analysis, multiple-wavelength anomalous diffraction and molecular replacement
-
hanging drop vapor diffusion method, using 0.2M (NH4)2SO4 and 0.1 M sodium acetate (pH 4.4) with 25% (w/v) PEG 2000 MME
-
purified enzyme with xenon is used as a molecular oxygen binding-site probe, 8 mg/ml protein in 100 mM HEPES pH 7 and 1.2 M sodium citrate, vappour diffusion method, 18C, 2 weeks, X-ray diffraction structure determination and analysis at 2.5 A resolution, modelling
-
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
-
hanging drop vapor diffusion method, using 8.0-9.5% (w/v) PEG 8000, 0.28-0.3 M phosphate at pH 6.0
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in complex with ethylamine and benzylamine, hanging drop vapor diffusion method, using 8-9% (w/v) polyethylene glycol 8000 in 0.22-0.25 M potassium phosphate (pH 6.0)
-
isoform HPAO-2, sitting drop vapor diffusion method, using 0.5-0.75 M potassium sodium tartrate tetrahydrate in 0.10 M phosphate, pH 6.0-7.5, at 20C
E7R5K2
sitting drop, orthorhombic crystals, X-ray structure, 2.4 A
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
nickel affinity column chromatography; nickel affinity column chromatography
A1R2C3, A1RDD3
recombinant enzyme expressed in Escherichia coli
-
recombinant His-tagged wild-type and mutants enzymes from Escherichia coli strain Rosetta2(DE3), removal of the His tag
-
recombinant selenomethionine-labeled truncated mutant MAO-N-D5 from Escherichia coli strain B834(DE3) by nickel affinity chromatography
-
Q sepharose column chromatography
-
Q-Sepharose column chromatography, and gel filtration
-
ammonium sulfate precipitation, Sepharose column chromatography, and Sephacryl S-200 gel filtration
-
Ni-chelating affinity column chromatography
-, I6NC69
native and recombinant enzyme
-
Q sepharose column chromatography
E7R5K2
ammonium sulfate precipitation, Hi-Prep 16 10 Q column chromatography, Mono Q column chromatography, and Superose 12 gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Nicotiana benthamiana; expressed in Nicotiana benthamiana; expressed in Nicotiana benthamiana
F4IAX1, Q8H1H9, Q8L866
expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
A1R2C3, A1RDD3
expressed in Escherichia coli CD03 cells
-
expression of wild-type and mutant enzymes, expression of selenomethionine-labeled truncated mutant MAO-N-D5 in Escherichia coli strain B834(DE3)
-
overexpression of His-tagged wild-type and mutants enzymes in Escherichia coli strain Rosetta2(DE3)
-
expressed in Escherichia coli JM109 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; AOC3, cDNA library screening, transient expression of wild-type and mutant enzymes in HEK293, HEK293-EBNA or CHO cells
O75106, Q16853
expressed in Drosophila melanogaster Schneider-2 cells and in 3T3-L1 mouse adipocytes
-
expressed in Escherichia coli DH5alpha cells
-
expression in 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
-
expressed in Escherichia coli BL21(DE3)pLysS cells
-, I6NC69
expressed in Saccharomyces cerevisiae
-
expressed in Saccharomyces cerevisiae INVSC-1 cells
E7R5K2
expression Saccharomyces cerevisiae
-
expressed in COS-1 cells
O08590
genes cao1+ and cao2+, cDNA library screening, DNA and amino acid determination and analysis, both genes are expressed in wild-type cells, but only the expression of cao1+,not of cao2+, results in production of an active enzyme. Expression of cao1+ and cao2+ is copper-independent and is not regulated by Cuf1. Recombinant expression of GFP-tagged Cao1 in the cytosol, expression of wild-type and mutant enzymes in Saccharomyces cerevisiae
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
at 24 h, the transcript levels of the gene of isoform CuAO3 decrease in plants exposed to abscisic acid or salicylic acid
F4IAX1, Q8H1H9, Q8L866
isoform CuAO1 expression is not significantly affected by wounding and 1-aminocyclopropane-1-carboxylic acid treatment; isoform CuAO2 transcript levels, which are abundant in stems but low in other organs, are not observed to increase during the developmental stages and is not affected by treatments with abscisic acid, salicylic acid, and flagellin; isoform CuAO3 expression is not significantly affected by wounding and 1-aminocyclopropane-1-carboxylic acid treatment
F4IAX1, Q8H1H9, Q8L866
isoform CuAO2 expression is clearly induced (about 12fold) in wounded and methyl jasmonate-treated plants at 8 h; isoform CuAO3 transcript levels increase during plant development, reaching a peak in flowers of adult plants, followed by leaves and stems. Isoform CuAO3 transcript accumulation is induced by abscisic acid, salicylic acid, flagellin and methyl jasmonate, at 8 h post-treatment. At 24 h the transcript levels of this gene increases in methyl jasmonate-treated plants; the expression of isoform CuAO1 increases about 3fold in 28-day-old seedlings when compared with 4-day-old. The highest expression of isoform CuAO1 is observed after 24 h in salicylic acid-treated plants (about 7.5-fold higher than basal level). The isoform expression is also up-regulated in response to methyl jasmonate, flagellin and abcisic acid, although at lower degree (about 3.5fold)
F4IAX1, Q8H1H9, Q8L866
cells are induced to express the enzyme with 0.6 mM CuSO4
-
AOC3 knockout mice show white adipose tissue with lower CD45 mRNA levels and fewer CD45+ leukocytes and diminished infiltration by T cells, macrophages, natural killer, and natural killer T cells
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enzyme expression is induced by limiting the nitrogen source to butylamine (isoform AO1) and phenylethylamine (isoform AO2)
-
enzyme expression is induced by limiting the nitrogen source to butylamine (isoform AO1) and phenylethylamine (isoform AO2)
Rhodococcus opacus DSM 43250
-
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D298A
-
Km-value for 2-phenylethylamine is 85% of the wild-type enzyme, kcat for 2-phenylethylamine is 360000fold lower than wild-type enzyme
D298K
-
in contrast to M602K and wild-type enzyme, the quinone in D298K does not react with any of the hydrazines. D298K shows no activity toward oxidative deamination of 2-phenylethylamine. The quinone formed in D298K is trapped in a conformation that can not react with amines. D298K contains a quinone other than topaquinone
N336S/M348K/I246M
-
genetic variant MOA-N-3 exhibits improved activity towards a range of amine substrates compared to the wild-type enzyme, including chiral secondary amines
N336S/M348K/I246M
-
gain-of-function mutant MAO-N-D3, structure analysis, overview. Of the mutations that confer the ability to catalyse the oxidation of secondary amines in MAO-N-D3, Asn336Ser reduces steric bulk behind Trp430 of the aromatic cage and Ile246Met confers greater flexibility within the substrate binding site
N336S/M348K/I246M/T384N/D385S
-
genetic variant MOA-N-5 shows improved activity and enantioselectivity towards a broad range of tertiary amines compared to the wild-type enzyme
N336S/M348K/I246M/T384N/D385S
-
gain-of-function mutant MAO-N-D5 is able to oxidise tertiary amines, structure analysis, overview. Of the mutations that confer the ability to catalyse the oxidation of secondary amines in MAO-N-D3, Asn336Ser reduces steric bulk behind Trp430 of the aromatic cage and Ile246Met confers greater flexibility within the substrate binding site. The two additional mutations, Thr384Asn and Asp385Ser, appear to influence the active-site environment remotely through changes in tertiary structure that perturb the side chain of Phe382, again altering the steric and electronic character of the active site near FAD
D383E
-
turnover-number of mutant enzyme is reduced up to 2000fold, depending on pH-value
D383N
-
catalytically inactive mutant enzyme
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
O75106, Q16853
AOC3 mutant
M211V/Y394N/L469G
-
the mutant of AOC3 changes substrate preferences toward those of copper-containing monoamine oxidase AOC2 with high activity towards 2-phenylethylamine
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
F190Y
-, I6NC69
the mutant loses the activity within the range of pH 6.8-8.5
F384G
-, I6NC69
the mutant loses the activity within the range of pH 6.8-8.5
I160F
-, I6NC69
the mutant loses the activity within the range of pH 6.8-8.5
S406T
-, I6NC69
the mutant loses the activity within the range of pH 6.8-8.5
Y320F
-, I6NC69
the mutant loses the activity within the range of pH 6.8-8.5
Y305A
-
mutation has moderate effects on the kinetics of catalysis (2.7fold and 8fold decrease in kcat using ethylamine and benzylamine as substrates), the same mutation slows cofactor formation by about 45-fold relative to that of the wild-type enzyme. The Y305A mutant forms at least two species: primarily topaquinone at lower pH and a species with a blue-shifted absorbance at high pH
Y305F
-
the rate of topaquinone formation is reduced 3fold relative to that of wild-type enzyme, 125fold decrease in kcat using ethylamine as substrate
H456A
-
site-directed mutagenesis, the active site residue mutant shows reduced activity compared to the wild-type enzyme
H458A
-
site-directed mutagenesis, the active site residue mutant shows reduced activity compared to the wild-type enzyme
H460A
-
site-directed mutagenesis, the active site residue mutant shows reduced activity compared to the wild-type enzyme
H621A
-
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
H627A
-
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
H456A
Schizosaccharomyces pombe FY435
-
site-directed mutagenesis, the active site residue mutant shows reduced activity compared to the wild-type enzyme
-
H458A
Schizosaccharomyces pombe FY435
-
site-directed mutagenesis, the active site residue mutant shows reduced activity compared to the wild-type enzyme
-
H460A
Schizosaccharomyces pombe FY435
-
site-directed mutagenesis, the active site residue mutant shows reduced activity compared to the wild-type enzyme
-
H621A
Schizosaccharomyces pombe FY435
-
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
-
H627A
Schizosaccharomyces pombe FY435
-
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
-
M602K
-
the mutant enzyme shows 20% activity toward 2-phenylethylamine in comparison to wild-type enzyme
additional information
-
genetic variants of MAO-N produced by directed evolution possess altered substrate specificity, e.g. MAO-N-3 and MAO-N-5
Y326F
-, I6NC69
the mutant loses the activity within the range of pH 6.8-8.5
additional information
-
construction of AOC3-KO mice which show white adipose tissue with lower CD45 mRNA levels and fewer CD45+ leukocytes and diminished infiltration by T cells, macrophages, natural killer, and natural killer T cells, the phenotype is not rescued by human SSAO/VAP-1 expression on adipocytes under the control of aP2, overview
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
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