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Enzyme Nomenclature
Information on EC 1.4.3.21 - primary-amine oxidase
for references in articles please use BRENDA:EC1.4.3.21
Word Map on EC 1.4.3.21
- 1.4.3.21
- endothelial
-
ssaos
- inflammation
- aldehyde
-
deamination
- leukocyte
- lymphocyte
- diamine
- diabetes
-
polyamines
- vessel
- methylamine
-
lysyl
- spermine
- arthrobacter
- putrescine
-
extravasation
-
2,4,5-trihydroxyphenylalanine
- phenylhydrazine
-
klinman
- globiformis
-
biogenic
- pargyline
- cadaverine
- acrolein
-
pyrroloquinoline
-
transmigration
-
half-reaction
- elastin
-
self-processing
- 2-phenylethylamine
- phenelzine
-
copper-binding
- clorgyline
- allylamine
-
quinoproteins
- beta-aminopropionitrile
- histaminase
-
addressins
- deprenyl
- aminoacetone
- medicine
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.4.3.21
-
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RECOMMENDED NAME
GeneOntology No.
primary-amine oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2
-
-
-
-
RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2
proposed mechanism, crystal structure
-
RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2
proposed mechanism, crystal structure; role of copper in enzyme activity
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
primary-amine:oxygen oxidoreductase (deaminating)
A group of enzymes that oxidize primary monoamines but have little or no activity towards diamines, such as histamine, or towards secondary and tertiary amines. They are copper quinoproteins (2,4,5-trihydroxyphenylalanine quinone) and, unlike EC 1.4.3.4, monoamine oxidase, are sensitive to inhibition by carbonyl-group reagents, such as semicarbazide. In some mammalian tissues the enzyme also functions as a vascular-adhesion protein (VAP-1).
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
684285, 685663, 686264, 686502, 687449, 688255, 688488, 688490, 688603, 689200, 701561, 705496, 711430, 711738, 724534
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-
-
-
-
cerebral hemodynamic modifications induce decreases in SSAO activity resulting in cell dedifferentiation and inducing dysregulation of glucose transport
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
enzyme deficiency reduces leukocyte infiltration into adipose tissue and favors fat deposition
physiological function
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
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
-
Cao1 may enable Schizosaccharomyces pombe cells to utilize primary amines as sources of nitrogen
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-aminononane + H2O + O2
nonanal + NH3 + H2O2
-
the aliphatic chain of 1-aminononane induces a shift in the pKa-value of the product Schiff base, the hydrolysis of which appears to be a rate-determining step of the reaction
-
-
?
1-methyl-3-phenylpropylamine + H2O + O2
4-phenylbutan-2-one + NH3 + H2O2
-
-
-
-
?
2-aminoethylpyridine + H2O + O2
pyridine-2-carbaldehyde + NH3 + H2O2
-
-
-
?
2-phenylethylamine + H2O + O2
beta-phenylethanal + NH3 + H2O2
-
-
-
?
3-aminomethylpyridine + H2O + O2
pyridine-3-carbaldehyde + NH3 + H2O2
-
-
-
?
4-aminomethylpyridine + H2O + O2
pyridine-4-carbaldehyde + NH3 + H2O2
-
-
-
?
4-fluorobenzylamine + H2O + O2
4-fluorobenzaldehyde + NH3 + H2O2
-
-
-
-
?
alpha-casein + H2O + O2
?
-
the enzyme oxidizes the lysine residues in alpha-casein protein
-
-
?
beta-phenylethylamine + H2O + O2
beta-phenylethanal + NH3 + H2O2
-
-
-
?
beta-phenylethylamine + O2 + H2O
beta-phenylethanal + NH3 + H2O2
-
-
-
?
cadaverine + H2O + O2
DELTA1-piperideine + NH3 + H2O2
best substrate
-
-
?
cyclohexanemethylamine + H2O + O2
cyclohexanecarbaldehyde + NH3 + H2O2
-
-
-
-
?
methyl 1-(2-methoxyethyl)-3-(trifluoroacetyl)-1H-indole-4-carboxylate + H2O + O2
?
-
-
-
-
?
octopamine + H2O + O2
hydroxy(hydroxyphenyl)acetaldehyde + NH3 + H2O2
-
-
-
-
?
ornithine + H2O + O2
?
ornithine can be transformed in glutamate-5-semialdehyde spontaneously cyclizes yielding DELTA1-pyrroline-5-carboxylic acid
-
-
?
phenylethylamine + H2O + O2
phenylacetaldehyde + NH3 + H2O2
-
main substrate for isoform AO2
-
-
?
pyrrolidine + 2,4,5-trihydroxyphenylalanine quinone + H2O + O2
? + H2O2 + NH3
-
-
-
-
?
serotonin + O2 + H2O
(5-hydroxy-1H-indol-3yl)acetaldehyde + NH3 + H2O2
-
-
-
?
spermidine + H2O + O2
? + NH3 + H2O2
good substrate. The oxidation of spermidine yields to the liberation of ammonia, hydrogen peroxide and the corresponding aldehyde that spontaneously cyclizes yielding first 1-(3-aminopropyl)pyrroliniun and, thereafter, 1,5-diazobicyclononane
-
-
?
tropoelastin + H2O + O2
?
-
the enzyme oxidizes the lysine residues in tropoelastin protein
-
-
?
tyramine + H2O + O2
4-hydroxyphenylacetaldehyde + NH3 + H2O2
during this reaction, an irreversible inactivation of the enzyme occurs
-
-
?
tyramine + H2O + O2
?
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
-
-
?
1,4-diamino-2-butyne + H2O + O2
?
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
-
-
?
1,4-diamino-2-chloro-2-butene + H2O + O2
?
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
-
-
?
1,5-diamino-2-pentyne + H2O + O2
?
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
-
-
?
1,6-diamino-2,4-hexadiyne + H2O + O2
?
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
-
-
?
2-bromoethylamine + H2O + O2
bromoacetaldehyde + NH3 + H2O2
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
-
-
?
2-phenylethylamine + H2O + O2
2-phenylethanal + NH3 + H2O2
-
-
-
?
2-phenylethylamine + H2O + O2
2-phenylethanal + NH3 + H2O2
-
-
-
-
?
2-phenylethylamine + H2O + O2
phenylacetaldehyde + NH3 + H2O2
-
preferred substrate
-
-
?
2-phenylethylamine + H2O + O2
phenylacetaldehyde + NH3 + H2O2
best substrate
-
-
?
3,3-bis(aminoethyl)-1-hydroxy-2-oxo-1-triazene + H2O + O2
?
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
-
-
?
4-(aminomethyl)-N-[3-(aminomethyl)benzyl]benzamide + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
4-(aminomethyl)-N-[3-(aminomethyl)benzyl]benzamide + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
4-aminomethylpyridine dihydrochloride + H2O + O2
?
45% substrate activity of 1 mM 4-aminomethylpyridine dihydrochloride as percentage of the activity of the best substrate (beta-phenylethylamine, 1 mM) for various amine oxidases
-
-
?
4-aminomethylpyridine dihydrochloride + H2O + O2
?
less than 0.1% substrate activity of 1 mM 4-aminomethylpyridine dihydrochloride as percentage of the activity of the best substrate (putrescine, 1 mM) for various amine oxidases
-
-
?
4-aminomethylpyridine dihydrochloride + H2O + O2
?
-
87% substrate activity of 1 mM 4-aminomethylpyridine dihydrochloride as percentage of the activity of the best substrate (benzylamine, 1 mM) for various amine oxidases
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
very poor substrate
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
low activity
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
best oxidized substrate
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
best oxidized substrate
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
main substrate for isoform AO1
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
main substrate for isoform AO1
-
-
?
dopamine + H2O + O2
(3,4-dihydroxyphenyl)acetaldehyde + NH3 + H2O2
-
-
-
-
?
dopamine + H2O + O2
(3,4-dihydroxyphenyl)acetaldehyde + NH3 + H2O2
-
-
-
-
?
ethylamine + H2O + O2
acetaldehyde + NH3 + H2O2
-
isoforms AO1 and AO2 show 100% activity with ethylamine
-
-
?
histamine + H2O + O2
(imidazol-4-yl)acetaldehyde + NH3 + H2O2
-
-
-
?
histamine + H2O + O2
(imidazol-4-yl)acetaldehyde + NH3 + H2O2
-
-
-
-
?
N6-(4-aminobut-2-ynyl)adenine + H2O + O2
?
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
-
-
?
putrescine + H2O + O2
?
putrescine can be oxidatively deaminated by the enzyme to corresponding aldehyde that spontaneously cyclizes yielding DELTA1-pyrroline
-
-
?
tryptamine + H2O + O2
(1H-indol-3-yl)acetaldehyde + NH3 + H2O2
-
-
-
?
tryptamine + H2O + O2
(1H-indol-3-yl)acetaldehyde + NH3 + H2O2
high activity
-
-
?
tryptamine + H2O + O2
1H-indol-3-ylacetaldehyde + NH3 + H2O2
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
-
-
?
tyramine + H2O + O2
(4-hydroxyphenyl)acetaldehyde + NH3 + H2O2
-
preferred substrate
-
-
?
tyramine + H2O + O2
(4-hydroxyphenyl)acetaldehyde + NH3 + H2O2
-
-
-
?
tyramine + H2O + O2
(4-hydroxyphenyl)acetaldehyde + NH3 + H2O2
-
-
-
?
tyramine + H2O + O2
(4-hydroxyphenyl)acetaldehyde + NH3 + H2O2
-
-
-
-
?
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
-
quantum mechanical hydrogen tunneling can be enhanced by an enzyme protein scaffold including the catalytic base that directly mediates the hydrogen transfer
-
-
?
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
high activity
-
-
?
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
-
-
-
-
?
additional information
?
-
-
MAO-N is a flavoenzyme that catalyses the oxidative deamination of primary amines, substrate specificity, overview
-
-
-
additional information
?
-
-
MAO-N is an FAD-dependent enzyme that catalyses the conversion of terminal amines to their corresponding aldehyde
-
-
-
additional information
?
-
-
Semicarbazide-sensitive amine oxidase acts as a vascular-adhesion protein, mediating the adhesion of lymphocytes to vascular endothelial cells under inflammatory conditions
-
-
-
additional information
?
-
the catalytic reaction proceeds via two half-reactions; the aldehyde product is released at the end of the reductive half-reaction before reduction of molecular oxygen in the oxidative half-reaction. Mechanism of molecular oxygen entry into the buried active site of the copper amine oxidase, the N-terminal domain does not affect oxygen entry, overview. The protein-derived cofactor TPQ and the off-metal O2-binding site are located in the vicinity of a conserved active-site Met699
-
-
-
additional information
?
-
the enzyme oxidizes arginine to ammonia, urea, hydrogen peroxide and glutamate-5-semialdehyde which spontaneously cyclizes yielding DELTA1-pyrroline-5-carboxylic acid
-
-
-
additional information
?
-
-
physiologic role for SSAO in elastin maturation
-
-
-
additional information
?
-
-
SSAO may contribute to the vascular damage associated to Alzheimer’s disease
-
-
-
additional information
?
-
synergistic interaction between semicarbazide-sensitive amine oxidase and angiotensin-converting enzyme in diabetes. Semicarbazide-sensitive amine oxidase is involved in the following biological processes: vision, inflammatory response, biogenic amine metabolism, catecholamine metabolism, amine metabolism, cell adhesion
-
-
-
additional information
?
-
semicarbazide-sensitive amine oxidases constitute a group of copper-dependent enzymes, which oxidatively deaminate primary endo- and exogenous amines
-
-
-
additional information
?
-
semicarbazide-sensitive amine oxidases constitute a group of copper-dependent enzymes, which oxidatively deaminate primary endo- and exogenous amines
-
-
-
additional information
?
-
AOC2 is an enzymatically active cell surface SSAO with distinct substrate specificity, the preferred in vitro substrates of AOC2 are 2-phenylethylamine, tryptamine and p-tyramine, cf. EC 1.4.3.4, instead of methylamine and benzylamine, the favored substrates of AOC3. Substrate docking, molecular modeling and comparison of AOC2 and AOC3, overview. No activity of AOC2 with methylamine, polyamine spermidine, or histamine
-
-
-
additional information
?
-
AOC2 is an enzymatically active cell surface SSAO with distinct substrate specificity, the preferred in vitro substrates of AOC2 are 2-phenylethylamine, tryptamine and p-tyramine, cf. EC 1.4.3.4, instead of methylamine and benzylamine, the favored substrates of AOC3. Substrate docking, molecular modeling and comparison of AOC2 and AOC3, overview. No activity of AOC2 with methylamine, polyamine spermidine, or histamine
-
-
-
additional information
?
-
substrate docking, molecular modeling and comparison of AOC2 and AOC3, overview. No activity of AOC3 with polyamine spermidine or histamine
-
-
-
additional information
?
-
substrate docking, molecular modeling and comparison of AOC2 and AOC3, overview. No activity of AOC3 with polyamine spermidine or histamine
-
-
-
additional information
?
-
-
the catalytic center is deeply buried within the enzyme and is accessible only through a narrow channel with a diameter of about 4.5 A. This channel is gated by the side chain of L469 which, along with the copper-TPQ coordination, controls the catalytic activity of SSAO. While specific interactions with residues lining the surface of the accessing channel are important for substrate specificity, the flexibility of substrates also plays an important role, molecular dynamics and induced docking studies, detailed overview
-
-
-
additional information
?
-
-
VAP-1/SSAOs convert amines into aldehydes. SSAOs are distinct from the mammalian monoamine oxidases, MAOs, but their substrate specificities are partly overlapping
-
-
-
additional information
?
-
-
no activity with dimethylamide substituted indole 3-((4-[5-(aminomethyl)-2-fluorophenyl]piperidin-1-yl)carbonyl)-1-(2-methoxyethyl)-N,N-dimethyl-1H-indole-4-carboxamide
-
-
-
additional information
?
-
-
alkylamines 2-bromoethylamine and 2-chloroethylamine, and the short diamine 1,2-diaminoethane are both poor substrates and irreversible inactivators of LSAO
-
-
-
additional information
?
-
-
T0901317 inhibits SSAO gene expression and its activity in atherogenic apoE-/- mice. The atheroprotective effect of LXR agonist T0901317 is related to the inhibition of SSAO gene expression and its activity
-
-
-
additional information
?
-
-
the catalytic mechanism can be divided into two half-reactions: a reductive half-reaction in which a primary amine substrate is oxidized to its corresponding aldehyde with the concomitant reduction of the organic cofactor 2,4,5-trihydroxyphenylalanine quinone and an oxidative half-reaction in which reduced 2,4,5-trihydroxyphenylalanine quinone is re-oxidized with the reduction of molecular oxygen to hydrogen peroxide
-
-
-
additional information
?
-
-
isoform HPAO-2 shows a clear preference for bulkier aromatic amines and isoform HPAO-1 shows a preference for short aliphatic amines
-
-
-
additional information
?
-
-
docking of substrates to the enzyme, the enzyme shows electrostatic control of the docking process, overview. The active site contains two negatively charged amino acid residues which seem to interact with positively charged groups of the substrate molecules
-
-
-
additional information
?
-
-
isoform AO1 isolated from butylamine-induced cells with a distinct specificity towards benzylamine (relative to phenylethylamine), acts on a broad range of aliphatic monoamines (C1-C5). Isoform AO2 isolated from phenylethylamine-treated cells displays activity towards phenylethylamine as well as tyramine and heterocyclic amines but negligible conversion of benzylamine and short chain aliphatic amines. Neither AO1 nor AO2 exhibit any measurable activity when using diamines (putrescine or cadaverine) as substrate
-
-
-
additional information
?
-
-
isoform AO1 isolated from butylamine-induced cells with a distinct specificity towards benzylamine (relative to phenylethylamine), acts on a broad range of aliphatic monoamines (C1-C5). Isoform AO2 isolated from phenylethylamine-treated cells displays activity towards phenylethylamine as well as tyramine and heterocyclic amines but negligible conversion of benzylamine and short chain aliphatic amines. Neither AO1 nor AO2 exhibit any measurable activity when using diamines (putrescine or cadaverine) as substrate
-
-
-
additional information
?
-
-
three histidine residues within the C-terminal region of Cao1 that are necessary for amine oxidase activity
-
-
-
additional information
?
-
-
three histidine residues within the C-terminal region of Cao1 that are necessary for amine oxidase activity
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-phenylethylamine + H2O + O2
beta-phenylethanal + NH3 + H2O2
O75106, Q16853
-
-
-
?
alpha-casein + H2O + O2
?
-
the enzyme oxidizes the lysine residues in alpha-casein protein
-
-
?
tropoelastin + H2O + O2
?
-
the enzyme oxidizes the lysine residues in tropoelastin protein
-
-
?
tryptamine + H2O + O2
(1H-indol-3-yl)acetaldehyde + NH3 + H2O2
O75106, Q16853
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
O75106, Q16853
low activity
-
-
?
additional information
?
-
-
MAO-N is a flavoenzyme that catalyses the oxidative deamination of primary amines, substrate specificity, overview
-
-
-
additional information
?
-
-
Semicarbazide-sensitive amine oxidase acts as a vascular-adhesion protein, mediating the adhesion of lymphocytes to vascular endothelial cells under inflammatory conditions
-
-
-
additional information
?
-
-
physiologic role for SSAO in elastin maturation
-
-
-
additional information
?
-
-
SSAO may contribute to the vascular damage associated to Alzheimer’s disease
-
-
-
additional information
?
-
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
?
-
O75106
semicarbazide-sensitive amine oxidases constitute a group of copper-dependent enzymes, which oxidatively deaminate primary endo- and exogenous amines
-
-
-
additional information
?
-
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
?
-
-
T0901317 inhibits SSAO gene expression and its activity in atherogenic apoE-/- mice. The atheroprotective effect of LXR agonist T0901317 is related to the inhibition of SSAO gene expression and its activity
-
-
-
additional information
?
-
-
the catalytic mechanism can be divided into two half-reactions: a reductive half-reaction in which a primary amine substrate is oxidized to its corresponding aldehyde with the concomitant reduction of the organic cofactor 2,4,5-trihydroxyphenylalanine quinone and an oxidative half-reaction in which reduced 2,4,5-trihydroxyphenylalanine quinone is re-oxidized with the reduction of molecular oxygen to hydrogen peroxide
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,4,5-trihydroxyphenylalanine quinone
-
i.e. TPQ, covalently bound cofactor, one per monomer, generated by posttranslational modification of the first conserved tyrosine residue in the consensus sequence Asn-Tyr-(Glu/Asp)-Tyr
2,4,5-trihydroxyphenylalaninequinone
-
i.e. TPQ cofactor, the cofactor is spontaneously formed by post-translational modifications of active site amino-acid residues
FAD
-
flavoenzyme, a hydrophobic cavity extends from the protein surface to the active site, where a noncovalently bound FAD sits at the base of an aromatic cage, the sides of which are formed by Trp430 and Phe466, binding structure, overview
additional information
-
no evidences of topaquinone cofactor involvement
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
calcium is the normal ligand of these peripheral sites. Enzyme activity is stimulated by 3 mM. Removal of the not solvent exposed calcium ion with EDTA results in a 60-90% reduction in enzyme activity
Co2+
Cobalt
-
the Km-value for O2 of the cobalt-substituted enzyme form is approximately 70fold higher than that of the copper-containing wild-type enzyme
copper
Cu
-
only the copper-containing homodimer is capable of rapid reoxidation and the zinc-copper heterodimers are incapable of rapid turnover at either subunit
Cu2+
Ni2+
Zn
-
the presence of substantial amount of zinc results in two distinctive enzyme species, designated as the fast and slow enzymes. Both forms are rapidly reduced by substrate methylamine with a rate constant of 199/s but behave differently in their oxidation rates. The fast enzyme is oxidized by dioxygen at a rate of 22.1/s, whereas the slow enzyme reacts at a rate of 0.00018/s. An investigation of the relationship between the copper content and the extent of the fast enzyme shows that only the copper-containing homodimer is capable of rapid reoxidation and the zinc-copper heterodimers are incapable of rapid turnover at either subunit
Zn2+
Co2+
-
enzyme reconstituted with Co2+ exhibits 2.2% of the activity of the original Cu2+ -enzyme, KM-values for amine substrate and dioxygen are comparable
Co2+
-
besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently. Although these noncupric metal ions can not initiate topaquinone formation under the atmospheric conditions, slow spectral changes are observed in the enzyme bound with Co2+ or Ni2+ ion under the dioxygen-saturating conditions. X-ray crystallographic analysis reveals structural identity of the active sites of Co- and Ni-activated enzymes with Cu-enzyme. Co2+ and Ni2+ ions are also capable of forming topaquinone, though much less efficiently than Cu2+
copper
-
3.7 gatom of copper per mol of enzyme; contains cupric copper; copper involved in enzyme activity; copper protein
copper
-
the purified enzyme contains 2.39 mol of copper per mol of subunit
copper
-
copper depleted enzyme can be reconstituted with either Cu2+, Zn2+, Co2+, or Ni2+, 79% of activity is restored with Cu2+, 19% is restored with Co2+, 1.7% with Zn2+ or Ni2+
copper
-
contains 8 Cu2+ per 1200000 Da, Co2+, Zn2+ and Ni2+ can replace Cu2+, no effect of Mn2+; copper protein
copper
-
study of cupric ions by magnetic-resonance and kinetic methods, native enzyme contains 2 tightly bound Cu2+ ions
Cu2+
-
copper protein. The native Cu2+ has essential roles such as catalyzing the electron transfer between the aminoresorcinol form of the reduced topaquinone cofactor and dioxygen, in part by providing a binding site for 1e- and 2e- reduced dioxygen species to be efficiently protonated and released and also preventing the back reaction between the product aldehyde and the aminoresorcinol form of the reduced topaquinone cofactor and dioxygen
Cu2+
-
besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently. Although these noncupric metal ions can not initiate topaquinone formation under the atmospheric conditions, slow spectral changes are observed in the enzyme bound with Co2+ or Ni2+ ion under the dioxygen-saturating conditions. X-ray crystallographic analysis reveals structural identity of the active sites of Co- and Ni-activated enzymes with Cu-enzyme. Co2+ and Ni2+ ions are also capable of forming topaquinone, though much less efficiently than Cu2+
Cu2+
-
the wild type enzyme contains 1 mol copper per mol of subunit, copper is the most efficient catalytic metal
Cu2+
the enzyme contains one non-blue copper type 2 ion as an inorganic cofactor
Cu2+
-
required for activity, the zinc content is 0.4 mol per mole of AOC3 monomer
Cu2+
required for activity, after overnight incubation with 0.1 mM CuSO4, isoform AMAO3 shows slightly enhanced activity (114% of untreated enzyme activity); required for activity, after overnight incubation with 0.1 mM CuSO4, there is no change in the activity of isoform AMAO2
Ni2+
-
enzyme reconstituted with Co2+ exhibits 0.9% of the activity of the original Cu2+ -enzyme, KM-values for amine substrate and dioxygen are comparable
Ni2+
-
besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently. Although these noncupric metal ions can not initiate topaquinone formation under the atmospheric conditions, slow spectral changes are observed in the enzyme bound with Co2+ or Ni2+ ion under the dioxygen-saturating conditions. X-ray crystallographic analysis reveals structural identity of the active sites of Co- and Ni-activated enzymes with Cu-enzyme. Co2+ and Ni2+ ions are also capable of forming topaquinone, though much less efficiently than Cu2+
Zn2+
-
besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(4-[[(2E)-4-amino-2-fluorobut-2-en-1-yl]oxy]phenyl)(pyrrolidin-1-yl)methanone
-
-
2-(4-[2-[2-(acetylamino)-2,3-dihydro-1,3-thiazol-4-yl]ethyl]phenyl)-N-[amino(imino)methyl]acetamide
-
-
3,3'-[[4-(aminomethyl)pyridine-3,5-diyl]bis(oxy)]dipropan-1-ol dihydrochloride
-
-
3-(4-methoxy-3-nitrophenyl)-3-pyrroline
-
0.015 mM, inactivation of BPAO by 3-aryl-3-pyrrolines
3-(4-methoxyphenyl)-2,5-dihydro-1H-pyrrole hydrochloride
-
0.4 mM, inactivation of BPAO by 3-aryl-3-pyrrolines
3-(4-methoxyphenyl)-N-methyl-5-(1H-pyrrol-2-yl)-4,5-dihydro-1H-pyrazole-1-carbothioamide
-
-
3-biphenyl-4-yl-2,5-dihydro-1H-pyrrole hydrochloride
-
0.1 mM, inactivation of BPAO by 3-aryl-3-pyrrolines
3-naphthalen-1-yl-2,5-dihydro-1H-pyrrole hydrochloride
-
0.4 mM, inactivation of BPAO by 3-aryl-3-pyrrolines
4-(2,5-dihydro-1H-pyrrol-3-yl)-N,N-dimethylaniline hydrochloride
-
0.4 mM, inactivation of BPAO by 3-aryl-3-pyrrolines
4-(aminomethyl)-2-benzyl-5-(ethylamino)pyridazin-3(2H)-one
-
below 10% inhibition at 0.5 mM
4-(aminomethyl)-2-methyl-5-(morpholin-4-yl)pyridazin-3(2H)-one
-
93% inhibition at 0.5 mM
4-(aminomethyl)-2-methyl-5-(pyrrolidin-1-yl)pyridazin-3(2H)-one
-
below 10% inhibition at 0.5 mM
4-(aminomethyl)-5-(ethylamino)-2-methylpyridazin-3(2H)-one
-
13% inhibition at 0.5 mM
4-(aminomethyl)-N,N-diethylpyridazine-3,5-diamine
-
over 99% inhibition at 0.5 mM
geraniin
-
competitive inhibition. Inhibitory activities of 10.87%, 37.24%, 77.67%, and 95.77%, respectively, for 0.00066, 0.00164, 0.00328, and 0.00656 mM of geraniin
histamine
substrate inhibition; substrate inhibition
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
L-Lys
-
the presence of L-lysine during the oxidation of benzylamine results in time- and dose-dependent inhibition of SSAO activity, in a process that is dependent on the H2O2 formed during benzylamine oxidation
N-allyl-3-(4-methoxyphenyl)-5-(1H-pyrrol-2-yl)-4,5-dihydro-1H-pyrazole-1-carbothioamide
-
-
N-ethyl-3-(4-methoxyphenyl)-5-(1H-pyrrol-2-yl)-4,5-dihydro-1H-pyrazole-1-carbothioamide
-
-
N-[4-(2-[4-[(2-amino-1H-imidazol-5-yl)methyl]phenyl]ethyl)-1,3-thiazol-2-yl]acetamide
-
-
N-[4-[2-(4-carbamimidamidophenyl)ethyl]-5-(4-sulfamoylbenzyl)-1,3-thiazol-2-yl]acetamide
-
-
N-[4-[2-(4-[[amino(imino)methyl]amino]phenyl)ethyl]-1,3-thiazol-2-yl]acetamide
-
-
o-phenylenediamine
-
0.2 mM, 33% inhibition of dimeric enzyme, 26% inhibition of tetrameric enzyme
p-Chloromercuriphenylsulfonate
-
0.1 mM, complete inhibition of enzyme from cultured aortic smooth muscle cells
ruthenium(II) molecular wires
-
the enzyme is reversibly inhibited by molecular wires comprising a Ru(II) complex head group and an aromatic tail group joined by an alkane linker
-
(Z)-3-fluoro-2-(4-methoxybenzyl)allylamine hydrochloride
-
i.e. LJP 1586. Potent, specific, and orally available inhibitor of SSAO activity is an effective anti-inflammatory compound in vivo
(Z)-3-fluoro-2-(4-methoxybenzyl)allylamine hydrochloride
-
i.e. LJP 1586. Potent, specific, and orally available inhibitor of SSAO activity is an effective anti-inflammatory compound in vivo
(Z)-3-fluoro-2-(4-methoxybenzyl)allylamine hydrochloride
-
i.e. LJP 1586. Potent, specific, and orally available inhibitor of SSAO activity is an effective anti-inflammatory compound in vivo
1,4-diamino-2-butyne
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
1,4-diamino-2-butyne
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
1,4-diamino-2-butyne
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
1,4-diamino-2-butyne
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
1,4-diamino-2-chloro-2-butene
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
1,4-diamino-2-chloro-2-butene
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
1,4-diamino-2-chloro-2-butene
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
1,4-diamino-2-chloro-2-butene
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
1,5-diamino-2-pentyne
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
1,5-diamino-2-pentyne
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
1,5-diamino-2-pentyne
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
1,5-diamino-2-pentyne
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
1,6-diamino-2,4-hexadiyne
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
1,6-diamino-2,4-hexadiyne
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
1,6-diamino-2,4-hexadiyne
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
1,6-diamino-2,4-hexadiyne
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
2-Bromoethylamine
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
2-Bromoethylamine
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
2-Bromoethylamine
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
2-Bromoethylamine
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
3,3-bis(aminoethyl)-1-hydroxy-2-oxo-1-triazene
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
3,3-bis(aminoethyl)-1-hydroxy-2-oxo-1-triazene
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
3,3-bis(aminoethyl)-1-hydroxy-2-oxo-1-triazene
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
3,3-bis(aminoethyl)-1-hydroxy-2-oxo-1-triazene
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
3-cyclohexylmethylamino-4-aminomethylpyridine dihydrochloride monohydrate
-
-
3-cyclohexylmethylamino-4-aminomethylpyridine dihydrochloride monohydrate
-
8-hydroxyquinoline
non-competitive inhibitor; non-competitive inhibitor; non-competitive inhibitor
aminoguanidine
irreversible competitive inhibitor; irreversible competitive inhibitor; irreversible competitive inhibitor
aminoguanidine
-
strongly inhibits adipocyte semicarbazide-sensitive amine oxidase and slightly reduces fat deposition in obese Zucker rats. Aminoguanidine may be useful for treating obesity via its SSAO blocking properties
aminoguanidine
-
isoform AO1 shows 18% residual activity at 0.1 mM, isoform AO2 shows 17% residual activity at 0.1 mM
benzylhydrazine
-
forms adducts with the TPQ cofactor, binding structure, overview
Cuprizone
-
copper chelating, 0.006 mM, 98% inhibition, competitive vs. benzylamine
Cuprizone
-
isoform AO1 shows 2% residual activity at 0.1 mM, isoform AO2 shows 1% residual activity at 0.1 mM
hydroxylamine
-
elicits hypotension in the rat. This effect is due in part to its conversion to nitric oxide and in part to a hydralazine-like action involving SSAO inhibition
N6-(4-aminobut-2-ynyl)adenine
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
N6-(4-aminobut-2-ynyl)adenine
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
N6-(4-aminobut-2-ynyl)adenine
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
N6-(4-aminobut-2-ynyl)adenine
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
NaN3
-
azide binds to Cu2+ ions, competitive inhibition vs. O2, uncompetitive vs. benzylamine
Phenelzine
-
0.001 mM, complete inhibition of enzyme from cultured aortic smooth muscle cells
phenylhydrazine
-
irreversible inactivation most likely due to hydrazone formation
Semicarbazide
-
0.2 mM, 49% inhibition of dimeric enzyme, 45% inhibition of tetrameric enzyme
Semicarbazide
causes significant decreases in the oxidative deamination activity of four among the five substrates catalyzed by SSAO
Semicarbazide
-
irreversible inhibitor. Pargyline + semicarbazide-induced reduction of fat deposition results from decreased food intake and from impaired MAO (EC 1.4.3.4) and SSAO-dependent lipogenic and antilipolytic actions of endogenous or alimentary amines
Semicarbazide
-
isoform AO1 shows 1% residual activity at 0.1 mM, isoform AO2 shows 2% residual activity at 0.1 mM
Semicarbazide
-
0.01 mM, complete inhibition of enzyme from cultured aortic smooth muscle cells
Tranylcypromine
-
forms adducts with the TPQ cofactor, also termed (1R,2S)-rel-2-phenylcyclopropanamine, is a mixture of (1R,2S)-2-phenylcyclopropanamine and (1S,2R)-2-phenylcyclopropanamine, binding structure, overview
tryptamine
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
tryptamine
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
tryptamine
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
tryptamine
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
tyramine
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
tyramine
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
tyramine
-
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
tyramine
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
additional information
-
3-pyrrolines are mechanism-based inactivators of the quinone-dependent amine oxidases but only substrates of the flavin-dependent amine oxidases
-
additional information
-
not inhibited by 2-aminoethanol and 2-(N,N-dimethylamino)ethanethiol
-
additional information
-
synthesis and in vitro activities of a series of VAP-1 selective inhibitors, molecular dynamics simulations and docking studies, pIC50 values, overview. Movements of Met211, Ser496, and especially Leu469 can enlarge the ligand-binding pocket, allowing larger ligands than those seen in the crystal structures to bind. Three-dimensional quantitative structure-activity relationship models for VAP-1 in comparison to MAOs, overview
-
additional information
-
no effect: DTT or EDTA at 1 mM, 1,4-diamino-2-butanone, sodium azide or KCN
-
additional information
the enzyme activity is not significantly affected in the presence of 5 mM EDTA; the enzyme activity is not significantly affected in the presence of 5 mM EDTA
-
additional information
the enzyme activity is not significantly affected in the presence of 5 mM EDTA; the enzyme activity is not significantly affected in the presence of 5 mM EDTA
-
additional information
clorgyline and deprenyl do not significantly inhibit the activities
-
additional information
-
no inhibition by pargyline. SSAO activity remains unchanged during starvation
-
additional information
-
not inhibited by pargyline, clorgyline, and neocupine
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Atx1-like protein
-
required for the synthesis of fully active Cao1
-
additional information
-
SSAO activity remains unchanged during starvation
-
additional information
-
active Cao1 requires Ctr4/5-mediated copper transport and the transcription factor Cuf1
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.13
4-fluorobenzylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
2.05
ethanolamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
0.03
octopamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
0.02
Phenylethylamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
0.02
vanillylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
0.0012
2-Phenylethylamine
-
wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 25°C
0.0025
2-Phenylethylamine
-
pH 6.8, 30°C, Co-activated enzyme; pH 6.8, 30°C, Cu-activated enzyme
0.0055
2-Phenylethylamine
isoform AMAO3, in 100 mM potassium phosphate buffer (pH 7.0), at 37°C
0.012
2-Phenylethylamine
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37°C
0.077
2-Phenylethylamine
recombinant enzyme expressed in CHO cells
0.11
amylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
0.16
amylamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
0.0051
benzylamine
-
enzyme from cultured aortic smooth muscle cells, Km decreases with increasing pH
0.013
benzylamine
-
mutant enzyme L469G, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C
0.018
benzylamine
-
mutant enzyme M211V/Y394N/L469G, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C
0.025
benzylamine
-
mutant enzyme M211V, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C
0.04
benzylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
0.084
benzylamine
-
mutant enzyme T212A, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C
0.184
benzylamine
-
wild type enzyme, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C
0.215
benzylamine
-
mutant enzyme Y394N, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C
0.0017
beta-phenylethylamine
-
pH 6.5, wild-type enzyme; pH 7.5, wild-type enzyme
0.0023
beta-phenylethylamine
-
pH 5.75, wild-type enzyme; pH 8.0, wild-type enzyme
0.32
Butylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C; isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
12.7
cadaverine
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37°C
0.1
dopamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
0.86
ethylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
0.28
histamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
0.41
histamine
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37°C
0.88
histamine
isoform AMAO3, in 100 mM potassium phosphate buffer (pH 7.0), at 37°C
0.18
methylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
0.236
methylamine
-
mutant enzyme L469G, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C
0.28
methylamine
-
mutant enzyme M211V, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C
0.331
methylamine
-
wild type enzyme, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C
0.502
methylamine
-
mutant enzyme T212A, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C
1.26
methylamine
-
mutant enzyme Y394N, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C
2.043
methylamine
-
mutant enzyme M211V/Y394N/L469G, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C
0.021
O2
-
copper-reconstituted wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
0.026
O2
-
wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
1
O2
-
cobalt-substituted wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
0.49
Propylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
0.29
putrescine
-
copper-reconstituted wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
0.57
putrescine
-
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
7.04
spermidine
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37°C
0.02
tyramine
isoform AMAO3, in 100 mM potassium phosphate buffer (pH 7.0), at 37°C
0.03
tyramine
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37°C
0.05
tyramine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
additional information
additional information
-
the Km-value for O2 of the cobalt-substituted enzyme form is approximately 70fold higher than that of the copper-containing wild-type enzyme
-
additional information
additional information
comparison of steady-state kinetics of enzyme expressed in CHO and HEK-293 EBNA cells, overview; comparison of steady-state kinetics of enzyme expressed in CHO and HEK-293 EBNA cells, overview
-
additional information
additional information
comparison of steady-state kinetics of enzyme expressed in CHO and HEK-293 EBNA cells, overview; comparison of steady-state kinetics of enzyme expressed in CHO and HEK-293 EBNA cells, overview
-
additional information
additional information
-
kinetic analysis at different ionic strength and pH, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17.3
4-fluorobenzylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
3.3
ethanolamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
3.5
octopamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
20.9
Phenylethylamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
1
vanillylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
1.72
2-Phenylethylamine
isoform AMAO3, in 100 mM potassium phosphate buffer (pH 7.0), at 37°C
5.12
2-Phenylethylamine
isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37°C
12.4
2-Phenylethylamine
-
wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 25°C
5.9
amylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
12.7
amylamine
-
isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30°C
0.066
benzylamine
-
isoform HPAO-1, at 25°C, 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
8.1
benzylamine
-
isoform HPAO-2, at 25°C, in 100 mM potassium phosphate, pH 7.2
12.1
benzylamine
-
isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C