HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 1.4.3.22 - diamine oxidase
for references in articles please use BRENDA:EC1.4.3.22
Word Map on EC 1.4.3.22
- 1.4.3.22
-
polyamine
-
oxidases
-
monoamine
- copper
- mucosal
- spermidine
- injury
-
deamination
- aminoguanidine
- seedling
- benzylamine
-
1.4.3.6
- ornithine
-
semicarbazide-sensitive
- bowel
- semicarbazide
-
copper-containing
- cadaverine
- heparin
-
biogenic
- tyramine
-
endotoxin
-
lysyl
- villus
- d-lactate
- methylamine
- n-methyltransferase
- lentil
- pao
- pargyline
- renalase
-
occludin
- demethylase
- tryptamine
- polymorpha
-
postheparin
- hansenula
- beta-phenylethylamine
-
copper-dependent
- deprenyl
- globiformis
- agmatine
- phenylhydrazine
- samdc
-
lysine-specific
-
d-lactic
-
quinoproteins
- clorgyline
-
oxidase-like
- phenylethylamine
- diagnostics
- medicine
- analysis
- biotechnology
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
1.4.3.22
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
diamine oxidase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
histamine + H2O + O2 = (imidazol-4-yl)acetaldehyde + NH3 + H2O2
ping-pong mechanism is suggested
-
histamine + H2O + O2 = (imidazol-4-yl)acetaldehyde + NH3 + H2O2
a mechanistic proposal for O2 reduction is advanced on the basis of thermodynamic considerations together with kinetic studies, the identification of steady-state intermediates, and the analysis of competitive oxygen kinetic isotope effects. The 18O kinetic isotope effect: 1.0136 at pH 7.2 is independent of temperature from 5°C to 47°C and insignificantly changed to 1.0122 upon raising the pH to 9, thus indicating the absence of kinetic complexity
histamine + H2O + O2 = (imidazol-4-yl)acetaldehyde + NH3 + H2O2
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
histamine:oxygen oxidoreductase (deaminating)
A group of enzymes that oxidize diamines, such as histamine, and also some primary monoamines but have little or no activity towards secondary and tertiary amines. They are copper quinoproteins (2,4,5-trihydroxyphenylalanine quinone) and, like EC 1.4.3.21 (primary-amine oxidase) but unlike EC 1.4.3.4 (monoamine oxidase), they are sensitive to inhibition by carbonyl-group reagents, such as semicarbazide.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
in human three functioning genes exist that encode copper-containing amine oxidases
Uniprot
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
-
diamine oxidase is one of the key enzymes for gamma-aminobutyric acid formation
physiological function
-
study of the enzymes of N-alkyltropane biosynthesis: tropinone reductase I (EC 1.1.1.206), tropinone reductase II (EC 1.1.1.236), and tropin:acyl-CoA transferase, pseudotropine:acyl-CoA transferase
physiological function
-
the oxidative deamination is an essential step in both pyridine and tropane alkaloid biosynthesis. MPO is part of a multigene family
physiological function
-
root cultures of Hyoscyamus niger produce nicotine and tropane alkaloids by the same early biosynthetic pathway in which the DAO functions to convert N-methylputrescine to methylpyrrolinium cation. There is no close correlaion between alkaloid production and DAO activity. The biosynthesis of nicotine and tropane alkaloids are not regulated directly by the DAO activities. Specificty for N-methylated diamines enable the Hyoscyamine enzyme to function specifically in tropane alkaloid biosynthesis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
1,5-diamino-3-oxapentane + H2O + O2
?
-
the relative reaction rate with is 13% of that with putrescine
-
-
?
1,8-diamino-3,6-dioxaoctane + H2O + O2
?
-
the relative reaction rate with is 20% of that with putrescine
-
-
?
2-(3,4-dihydroxyphenyl)-ethylamine + H2O + O2
3,4-dihydroxyphenylacetaldehyde + NH3 + H2O2
-
-
?
2-aminoethylpyridine + H2O + O2
pyridin-2-ylacetaldehyde + NH3 + H2O2
-
-
-
-
?
4-aminomethylpyridine dihydrochloride + H2O + O2
?
8% substrate activity of 1 mM 4-aminomethylpyridine dihydrochloride as percentage of the activity of the best substrate (putrescine, 1 mM) for various amine oxidases
-
-
?
beta-phenylethylamine + O2 + H2O
beta-phenylethanal + NH3 + H2O2
-
-
-
?
butylamine + H2O + O2
butanal + NH3 + H2O2
-
22% of the activity with histamine
-
-
?
hexylamine + H2O + O2
hexanal + NH3 + H2O2
-
41% of the activity with histamine
-
-
?
histamine + O2 + H2O
(imidazol-4-yl)acetaldehyde + NH3 + H2O2
DAO
-
-
?
N-(2-fluoroethyl)putrescine + H2O + O2
N-(2-fluoroethyl)aminobutanal + NH3 + H2O2
-
same activity as with N-methylputrescine as substrate
-
-
?
N-acetyl-1,4-diaminobutane + H2O + O2
N-acetyl-aminobutanal + acetylamine + H2O2
-
8.6% of activity with putrescine
-
?
N-acetyl-1,5-diaminopentane + H2O + O2
N-acetyl-aminopentanal + acetylamine + H2O2
-
3.8% of activity with putrescine
-
?
N-ethylcadaverine + H2O + O2
5-(ethylamino)pentanal + NH3 + H2O2
-
17% activity compared to activity with N-methylputrescine
-
-
?
N-ethylputrescine + H2O + O2
4-(ethylamino)butanal + NH3 + H2O2
-
same activity as with N-methylputrescine as substrate
-
-
?
N-methylcadaverine + H2O + O2
5-(methylamino)pentanal + NH3 + H2O2
-
16% activity compared to activity with N-methylputrescine
-
-
?
N-n-propylputrescine + H2O + O2
4-propylaminobutanal + NH3 + H2O2
-
50% of the activity compared to N-methylputrescine as substrate
-
-
-
p-dimethylaminomethylbenzylamine + H2O + O2
p-dimethylaminomethylbenzaldehyde + NH3 + H2O2
pentylamine + H2O + O2
pentanal + NH3 + H2O2
-
32% of the activity with histamine
-
-
?
propylamine + H2O + O2
proanal + NH3 + H2O2
-
7% of the activity with histamine
-
-
?
(E,Z)-1,4-diamino-2-butene + H2O + O2
4-aminobut-2-enal + NH3 + H2O2
-
-
-
?
(E,Z)-1,4-diamino-2-butene + H2O + O2
4-aminobut-2-enal + NH3 + H2O2
-
-
-
?
(E,Z)-1,4-diamino-2-butene + H2O + O2
4-aminobut-2-enal + NH3 + H2O2
-
-
-
?
(E,Z)-1,4-diamino-2-butene + H2O + O2
4-aminobut-2-enal + NH3 + H2O2
-
-
-
?
1,10-diaminodecane + H2O + O2
10-aminodecanal + NH3 + H2O2
-
-
-
?
1,3-diaminopropane + H2O + O2
3-aminopropanal + NH3 + H2O2
-
109% of activity with putrescine
-
-
1,3-diaminopropane + H2O + O2
3-aminopropanal + NH3 + H2O2
-
30% activity compared to activity with N-methylputrescine
-
-
-
1,3-diaminopropane + H2O + O2
3-aminopropanal + NH3 + H2O2
-
-
-
?
1,3-diaminopropane + H2O + O2
3-aminopropanal + NH3 + H2O2
-
30% activity compared to activity with putrescine
-
-
-
1,4-diaminobutane + H2O + O2
4-aminobutanal + NH3 + H2O2
-
56% activity compared to activity with N-methylputrescine
-
-
?
1,4-diaminobutane + H2O + O2
4-aminobutanal + NH3 + H2O2
-
50% activity compared to activity with N-methylputrescine
-
-
?
1,4-diaminobutane + H2O + O2
4-aminobutanal + NH3 + H2O2
-
-
-
-
1,4-diaminobutane + H2O + O2
4-aminobutanal + NH3 + H2O2
-
-
-
?
1,4-diaminobutane + H2O + O2
4-aminobutanal + NH3 + H2O2
-
best substrate
-
-
?
1,4-diaminobutane + H2O + O2
4-aminobutanal + NH3 + H2O2
-
-
-
?
1,5-diaminopentane + H2O + O2
5-aminopentanal + NH3 + H2O2
-
-
-
?
1,5-diaminopentane + H2O + O2
5-aminopentanal + NH3 + H2O2
-
most active
-
-
1,5-diaminopentane + H2O + O2
5-aminopentanal + NH3 + H2O2
-
-
-
?
1,5-diaminopentane + H2O + O2
5-aminopentanal + NH3 + H2O2
-
60% of activity with putrescine
-
?
1,5-diaminopentane + H2O + O2
5-aminopentanal + NH3 + H2O2
-
-
-
?
1,6-diaminohexane + H2O + O2
6-aminohexanal + NH3 + H2O2
-
-
-
-
1,7-diaminoheptane + H2O + O2
7-aminoheptanal + NH3 + H2O2
-
-
-
?
1,7-diaminoheptane + H2O + O2
7-aminoheptanal + NH3 + H2O2
-
-
-
?
1,8-diaminooctane + H2O + O2
8-aminooctanal + NH3 + H2O2
-
-
-
?
1-phenylethylamine + H2O + O2
1-phenylethanal + NH3 + H2O2
-
44% of the activity with histamine
-
-
?
1-phenylethylamine + H2O + O2
1-phenylethanal + NH3 + H2O2
-
44% of the activity with histamine
-
-
?
2-hydroxyputrescine + H2O + O2
2-hydroxy-4-aminobutanal + H2O2 + NH3
-
-
-
?
2-hydroxyputrescine + H2O + O2
2-hydroxy-4-aminobutanal + H2O2 + NH3
-
-
-
?
2-phenylethylamine + H2O + O2
2-phenylethanal + NH3 + H2O2
-
-
-
-
?
2-phenylethylamine + H2O + O2
2-phenylethanal + NH3 + H2O2
-
-
?
3-hydroxycadaverine + H2O + O2
3-hydroxy-4-aminopentanal + H2O2 + NH3
-
-
-
?
3-hydroxycadaverine + H2O + O2
3-hydroxy-4-aminopentanal + H2O2 + NH3
-
-
-
?
4-phenylbutylamine + H2O + O2
4-phenylbutanal + NH3 + H2O2
-
72.6% of the activity with tyramine
-
-
?
4-phenylbutylamine + H2O + O2
4-phenylbutanal + NH3 + H2O2
-
53.6% of the activity with tyramine
-
-
?
4-phenylbutylamine + H2O + O2
4-phenylbutanal + NH3 + H2O2
-
19.3% of the activity with cadaverine
-
-
?
agmatine + H2O + O2
?
-
4% of the activity with histamine
-
-
?
agmatine + H2O + O2
?
-
4% of the activity with histamine
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
88.5% of the activity with tyramine
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
15.3% of the activity with tyramine
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
66.5% of the activity with cadaverine
-
-
?
cadaverine + H2O + O2
5-aminopentanal + NH3 + H2O2
-
15% activity compared to activity with N-methylputrescine
-
-
?
cadaverine + H2O + O2
5-aminopentanal + NH3 + H2O2
-
30% activity compared to activity with N-methylputrescine
-
-
?
cadaverine + H2O + O2
5-aminopentanal + NH3 + H2O2
-
75% activity compared to activity with putrescine
-
-
?
cadaverine + H2O + O2
5-aminopentanal + NH3 + H2O2
-
80% activity compared to activity with putrescine
-
-
?
dopamine + H2O + O2
2-(3,4-dihydroxyphenyl)ethanal + NH3 + H2O2
-
51% of the activity with histamine
-
-
?
dopamine + H2O + O2
2-(3,4-dihydroxyphenyl)ethanal + NH3 + H2O2
-
93.7% of the activity with tyramine
-
-
?
dopamine + H2O + O2
2-(3,4-dihydroxyphenyl)ethanal + NH3 + H2O2
-
62.3% of the activity with tyramine
-
-
?
dopamine + H2O + O2
2-(3,4-dihydroxyphenyl)ethanal + NH3 + H2O2
-
18.4% of the activity with cadaverine
-
-
?
histamine + H2O + O2
(imidazol-4-yl)acetaldehyde + NH3 + H2O2
-
-
-
-
?
histamine + H2O + O2
(imidazol-4-yl)acetaldehyde + NH3 + H2O2
-
-
-
-
?
histamine + H2O + O2
(imidazol-4-yl)acetaldehyde + NH3 + H2O2
-
-
-
?
histamine + H2O + O2
(imidazol-4-yl)acetaldehyde + NH3 + H2O2
-
-
?
histamine + H2O + O2
(imidazol-4-yl)acetaldehyde + NH3 + H2O2
-
28% of activity with putrescine
-
-
histamine + H2O + O2
(imidazol-4-yl)acetaldehyde + NH3 + H2O2
-
-
-
-
?
histamine + H2O + O2
(imidazol-4-yl)acetaldehyde + NH3 + H2O2
-
preferred substrate
-
-
?
histamine + H2O + O2
(imidazol-4-yl)acetaldehyde + NH3 + H2O2
-
-
-
?
histamine + H2O + O2
(imidazol-4-yl)acetaldehyde + NH3 + H2O2
-
60% activity compared to activity with putrescine
-
-
?
N-methyl-1,3-diaminopropane + H2O + O2
N-methyl-3-aminopropanal + NH3 + H2O2
-
40% activity compared to activity with N-methylputrescine
-
-
?
N-methyl-1,3-diaminopropane + H2O + O2
N-methyl-3-aminopropanal + NH3 + H2O2
-
40% activity compared to activity with putrescine
-
-
?
N-methylputrescine + H2O + O2
4-(methylamino)butanal + NH3 + H2O2
-
best substrate
-
-
?
N-methylputrescine + H2O + O2
4-(methylamino)butanal + NH3 + H2O2
-
best substrate. Specificity for N-methylated diamines enable the Hyoscyamine enzyme to function specifically in tropane alkaloid biosynthesis
-
-
?
N-methylputrescine + H2O + O2
4-(methylamino)butanal + NH3 + H2O2
-
-
-
-
?
N-methylputrescine + H2O + O2
4-(methylamino)butanal + NH3 + H2O2
-
50% activity compared to activity with putrescine
-
-
?
N-methylputrescine + H2O + O2
4-(methylamino)butanal + NH3 + H2O2
-
75% activity compared to activity with putrescine
-
-
?
p-dimethylaminomethylbenzylamine + H2O + O2
p-dimethylaminomethylbenzaldehyde + NH3 + H2O2
-
-
-
?
p-dimethylaminomethylbenzylamine + H2O + O2
p-dimethylaminomethylbenzaldehyde + NH3 + H2O2
-
-
-
?
p-dimethylaminomethylbenzylamine + H2O + O2
p-dimethylaminomethylbenzaldehyde + NH3 + H2O2
-
-
-
?
p-dimethylaminomethylbenzylamine + H2O + O2
p-dimethylaminomethylbenzaldehyde + NH3 + H2O2
-
-
-
?
p-dimethylaminomethylbenzylamine + H2O + O2
p-dimethylaminomethylbenzaldehyde + NH3 + H2O2
-
-
-
?
p-dimethylaminomethylbenzylamine + H2O + O2
p-dimethylaminomethylbenzaldehyde + NH3 + H2O2
-
-
-
?
p-dimethylaminomethylbenzylamine + H2O + O2
p-dimethylaminomethylbenzaldehyde + NH3 + H2O2
-
-
-
?
p-dimethylaminomethylbenzylamine + H2O + O2
p-dimethylaminomethylbenzaldehyde + NH3 + H2O2
-
-
-
?
putrescine + H2O + O2
?
-
catalytic activity of xenon-treated LSAO towards putrescine is about 40% of that of the native LSAO
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
enzyme plays a protective role against histamine in diseases such as ischaemic bowel syndrome, mesenteric infarction and ulcerative colitis
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
enzyme plays a protective role against histamine in diseases such as ischaemic bowel syndrome, mesenteric infarction and ulcerative colitis
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
no activity with spermidine
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
no activity with benzylamine
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
no activity with p-dimethylaminomethylbenzylamine
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
no activity with histamine
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
only aliphatic diamines from C4 to C10 and cystamine are oxidized, enzymatic activity decreases sharply with increasing chain length of diamines
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
short-chain aliphatic diamines are deaminated with highest reaction velocity
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
enzyme plays a protective role against histamine in diseases such as ischaemic bowel syndrome, mesenteric infarction and ulcerative colitis
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
very low activity with: 2-phenylethylamine, tryptamine, histamine, N1-naphthylethylenediamine, dopamine, spermine, benzylamine or homoveratrylamine
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
very low activity with: 2-phenylethylamine, tryptamine, histamine, N1-naphthylethylenediamine, dopamine, spermine, benzylamine or homoveratrylamine
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
enzyme plays a protective role against histamine in diseases such as ischaemic bowel syndrome, mesenteric infarction and ulcerative colitis
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
no activity with benzylamine
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
enzyme plays a protective role against histamine in diseases such as ischaemic bowel syndrome, mesenteric infarction and ulcerative colitis
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
treatment of diamine oxidase with reducing agents induces ability to catalyze oxidative deamination of substrates of monoamine oxidase EC 1.4.3.4
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
enzyme plays a protective role against histamine in diseases such as ischaemic bowel syndrome, mesenteric infarction and ulcerative colitis
-
?
tryptamine + H2O + O2
1H-indol-3-ylacetaldehyde + NH3 + H2O2
-
15% of the activity with histamine
-
-
?
tryptamine + H2O + O2
1H-indol-3-ylacetaldehyde + NH3 + H2O2
-
35.2% of the activity with tyramine
-
-
?
tryptamine + H2O + O2
1H-indol-3-ylacetaldehyde + NH3 + H2O2
-
48.4% of the activity with tyramine
-
-
?
tryptamine + H2O + O2
1H-indol-3-ylacetaldehyde + NH3 + H2O2
-
15.7% of the activity with cadaverine
-
-
?
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
-
36% of the activity with histamine
-
-
?
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
-
36% of the activity with histamine
-
-
?
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
-
-
?
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
-
19.1% of the activity with cadaverine
-
-
?
additional information
?
-
-
no activity with putrescine, cadaverine, spermine, and spermidine
-
-
-
additional information
?
-
-
no activity with putrescine, cadaverine, spermine, and spermidine
-
-
-
additional information
?
-
-
relevance of the enzyme as a H2O2-delivering system in wound response, as well as in the protection against fungal invasion
-
-
-
additional information
?
-
-
polyamine degradation via DAO produces DELTA1-pyrroline, DELTA1-pyrroline can be catabolized to gamma-aminobutyric acid, which is converted via transamination and oxidation to succinate and successively introduced in the Krebs cycle.
-
-
-
additional information
?
-
hDAO is unique among CAOs in that it has a distinct substrate preference for diamines
-
-
-
additional information
?
-
active site of hDAO: contacts made by cofactor trihydroxyphenylalanine quinone to the active-site Cu2+, and Thr685 and to a glycerol molecule within the active-site channel
-
-
-
additional information
?
-
-
involvement of the enzyme in the supply of H2O2 to peroxidase-catalysed reactions in the chalazal cells during grain filling
-
-
-
additional information
?
-
-
low activity with histamine, n-butylamine, and 1,6-diaminohexane
-
-
-
additional information
?
-
-
low or no activity with 1,3-diaminopropane, N-methyl-1,3-diaminopropane, n-butylamine, 1,6-diaminohexane, and histamine
-
-
-
additional information
?
-
-
low activity with n-butylamine or 1,6-diaminohexane as substrate
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
histamine + H2O + O2
(imidazol-4-yl)acetaldehyde + NH3 + H2O2
-
preferred substrate
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
enzyme plays a protective role against histamine in diseases such as ischaemic bowel syndrome, mesenteric infarction and ulcerative colitis
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
enzyme plays a protective role against histamine in diseases such as ischaemic bowel syndrome, mesenteric infarction and ulcerative colitis
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
enzyme plays a protective role against histamine in diseases such as ischaemic bowel syndrome, mesenteric infarction and ulcerative colitis
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
enzyme plays a protective role against histamine in diseases such as ischaemic bowel syndrome, mesenteric infarction and ulcerative colitis
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
enzyme plays a protective role against histamine in diseases such as ischaemic bowel syndrome, mesenteric infarction and ulcerative colitis
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
-
enzyme plays a protective role against histamine in diseases such as ischaemic bowel syndrome, mesenteric infarction and ulcerative colitis
-
?
additional information
?
-
-
relevance of the enzyme as a H2O2-delivering system in wound response, as well as in the protection against fungal invasion
-
-
-
additional information
?
-
-
polyamine degradation via DAO produces DELTA1-pyrroline, DELTA1-pyrroline can be catabolized to gamma-aminobutyric acid, which is converted via transamination and oxidation to succinate and successively introduced in the Krebs cycle.
-
-
-
additional information
?
-
P19801
hDAO is unique among CAOs in that it has a distinct substrate preference for diamines
-
-
-
additional information
?
-
-
involvement of the enzyme in the supply of H2O2 to peroxidase-catalysed reactions in the chalazal cells during grain filling
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,4,5-trihydroxyphenylalanine quinone
-
irreversible inactivation with p-nitrophenylhydrazine gives rise to a coloured enzyme p-nitrophenylhydrazone indicating dopaquinone as cofactor
2,4,5-trihydroxyphenylalanine quinone
-
i.e. iminoquinone, content of 2,4,5-trihydroxyphenylalanine quinone per dimer is 1.4
2,4,5-trihydroxyphenylalanine quinone
-
i.e. iminoquinone, content of 2,4,5-trihydroxyphenylalanine quinone per dimer is 1.4
2,4,5-trihydroxyphenylalanine quinone
-
i.e. iminoquinone, content of 2,4,5-trihydroxyphenylalanine quinone per dimer is 1.6
2,4,5-trihydroxyphenylalanine quinone
-
i.e. iminoquinone, content of 2,4,5-trihydroxyphenylalanine quinone per dimer is 1.8
2,4,5-trihydroxyphenylalanine quinone
it is shown that PSAO exists predominantly in the Cu(I), topaquinone semiquinone state
pyrroloquinoline quinone
-
enzyme may contain pyrroloquinoline-quinione as prosthetic group
pyrroloquinoline quinone
-
enzyme may contain pyrroloquinoline-quinione as prosthetic group
additional information
-
presence of one carbonyl group per enzyme dimer
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
copper
Cu
Cu2+
Manganese
Zn2+
copper
enzyme binds Cu. It is shown that PSAO exists predominantly in the Cu(I), topaquinone semiquinone state
Cu2+
-
a part of the apoenzyme is reconstituted in presence of Cu2+
Cu2+
-
Cu2+ ions stimulate the activation/maturation of the enzyme. The highest activity is observed at more than 5fold molar ratio between Cu2+ and the enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(E)-1,4-diamino-2-butene
-
0.1 mM, 72% and 87% inhibition; 0.1 mM, 72% and 87% inhibition
(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
2,4-Dinitrophenylhydrazine
-
1 mM, complete inhibition; 1 mM, complete inhibition
3,3'-[[4-(aminomethyl)pyridine-3,5-diyl]bis(oxy)]dipropan-1-ol dihydrochloride
-
3-cyclohexylmethylamino-4-aminomethylpyridine dihydrochloride monohydrate
-
4,4'-(pentane-1,5-diylbis(oxy))dibenzimidamide
noncompetitive inhibition
4,4'-[[4-(aminomethyl)pyridine-3,5-diyl]bis(oxy)]dibutan-1-ol dihydrochloride
-
4-(aminomethyl)-N,N'-bis(1-methylethyl)pyridine-3,5-diamine dihydrochloride
-
gabexate mesylate
-
anti coagulant drug, competitive vs. agmatine and putrescine oxidation
methylglyoxalbis(guanylhydrazone)
-
without preincubation competitive inhibitor, non-competitive after 1 h preincubation
N,N-diethyldithiocarbamate
-
the inactive enzyme is restored with Cu2+ to 65% of its initial activity
NaCl
-
200 mM, approx. 50% inhibition, almost complete inhibition of the purified enzyme with 1 M NaCl
p-Nitrophenylhydrazine
-
1 mM, complete inhibition; 1 mM, complete inhibition
Thiocyanate
-
uncompetitive vs. p-dimethylaminomethylbenzylamine, SCN- is equatorially coordinated to a tetragonal Cu(II) center
1,3-Diaminopropane
-
10 mM with 2 mM N-methylputrescine as substrate, 32% relative inhibition
1,3-Diaminopropane
-
10 mM with 2 mM N-methylputrescine as substrate, 70% relative inhibition
1,3-Diaminopropane
-
10 mM with 2 mM N-methylputrescine as substrate, 93% relative inhibition
aminoguanidine
-
0.00001 mM, 50% inhibition, putrescine or histamine as substrates
azide
-
noncompetitive with respect to oxidative half-reaction, noncompetitive with respect to reductive half-reaction
azide
-
partially competitive with respect to oxidative half-reaction, competitive with respect to reductive half-reaction
azide
-
mode of inhibition is dependent of azide concentration with respect to oxidative half-reaction, noncompetitive with respect to reductive half-reaction
azide
-
competitive with respect to oxidative half-reaction, noncompetitive with respect to reductive half-reaction
beta-hydroxyethylhydrazine
-
0.0033 mM, with 0.01 mM tyramine, 89.4% inhibition
beta-hydroxyethylhydrazine
-
0.0033 mM, with 0.01 mM tyramine, 89.5% inhibition
beta-hydroxyethylhydrazine
-
0.0033 mM, with 0.01 mM cadaverine, 85.5% inhibition
clonidine
-
antihypertensive drug, competitive vs. agmatine and putrescine oxidation
diethyldithiocarbamate
-
0.0033 mM, with 0.01 mM tyramine, 90.4% inhibition
H2O2
-
inactivation by turnover products is a slow reaction of the reduced protein with H2O2 subsequent to turnover and occurs in a similar way for all amines
KCN
-
1 mM, inhibits activity completely, is used to stop the enzyme reaction
n-butylamine
-
10 mM with 2 mM N-methylputrescine as substrate, 19% relative inhibition
n-butylamine
-
10 mM with 2 mM N-methylputrescine as substrate, 66% relative inhibition
n-butylamine
-
10 mM with 2 mM N-methylputrescine as substrate, 60% relative inhibition
N-methyl-1,3-diamonopropane
-
10 mM with 2 mM N-methylputrescine as substrate, 34% relative inhibition
N-methyl-1,3-diamonopropane
-
10 mM with 2 mM N-methylputrescine as substrate, 55% relative inhibition
N-methyl-1,3-diamonopropane
-
10 mM with 2 mM N-methylputrescine as substrate, 61% relative inhibition
N-methylbutylamine
-
10 mM with 2 mM N-methylputrescine as substrate, 70% relative inhibition
N-methylbutylamine
-
10 mM with 2 mM N-methylputrescine as substrate, 23% relative inhibition
N-methylbutylamine
-
10 mM with 2 mM N-methylputrescine as substrate, 19% relative inhibition
N-methylpropylamine
-
10 mM with 2 mM N-methylputrescine as substrate, 75% relative inhibition
N-methylpropylamine
-
10 mM with 2 mM N-methylputrescine as substrate, 13% relative inhibition
N-methylpropylamine
-
10 mM with 2 mM N-methylputrescine as substrate, 22% relative inhibition
n-Propylamine
-
10 mM with 2 mM N-methylputrescine as substrate, 28% relative inhibition
n-Propylamine
-
10 mM with 2 mM N-methylputrescine as substrate, 23% relative inhibition
n-Propylamine
-
10 mM with 2 mM N-methylputrescine as substrate, 48% relative inhibition
NaN3
-
uncompetitive vs. p-dimethylaminomethylbenzylamine, N3- is equatorially coordinated to a tetragonal Cu(II) center
additional information
-
inhibtion by the copper ligand diethyldithiocarbamate and the carbonyl reagents suggests that copper and pyrrroloquinoline are present at the active site of this enzyme; primary amines inhibit pea and pig kidney DAO activities more strongly than the Hyoscyamus niger. N-methylated amines are stronger inhibtors of the Hyoscyamus enzyme than of the others DAOs
-
additional information
-
primary amines inhibit pea and pig kidney DAO activities more strongly than the Hyoscyamus niger. N-methylated amines are stronger inhibtors of the Hyoscyamus enzyme than of the others DAOs
-
additional information
clorgyline and deprenyl do not decrease DAO activity
-
additional information
-
no substrate inhibition with monoamines; substrate inhibition with diamines
-
additional information
alkylamino derivatives of 4-aminomethylpyridine, substrate-like, reversible inhibitors
-
additional information
-
primary amines inhibit pea and pig kidney DAO activities more strongly than the Hyoscyamus niger. N-methylated amines are stronger inhibtors of the Hyoscyamus enzyme than of the others DAOs
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaCl
-
in comparison to cultivar Jinchun no. 2, cultivar Changchun mici shows an increase in diamine oxidase activity as well as free spermidine and spermine, soluble conjugated and insoluble bound putrescine, spermidine and spermine contents in the roots during exposure to salinity (50 mM NaCl).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
the kinetic properties of the MPO1 enzyme may play an important role in determining the pyridine alkaloid profiles observed in tobacco roots
-
0.35
1,3-Diaminopropane
-
Vmax: 11.3 nkat, pH and temperature not specified in the publication
0.31
1,4-diaminobutane
-
pH 7.9, 30°C, higher KM-value compared with N-methylputrescine or cadaverine as substrates, Vmax: 21.9 pkat
0.32
1,4-diaminobutane
-
pH 7.9, 30°C, lower KM-value compared with N-methylputrescine and higher compared to cadaverine as substrates, Vmax: 97.3 pkat
0.76
1,4-diaminobutane
-
Vmax: 11.1 nkat, pH and temperature not specified in the publication
2.85
1,4-diaminobutane
-
pH 7.9, 30°C, higher KM-value compared with N-methylputrescine or cadaverine as substrates, Vmax: 82.7 pkat, specifiity constant 11% of the constant for N-methylputrescine
0.877
Butylamine
-
enzyme from placenta, at 37°C, pH not specified in the publication
2.032
Butylamine
-
enzyme from seminal plasma, at 37°C, pH not specified in the publication
0.13
cadaverine