1.4.3.22: diamine oxidase
This is an abbreviated version!
For detailed information about diamine oxidase, go to the full flat file.
Word Map on EC 1.4.3.22
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1.4.3.22
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polyamine
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oxidases
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monoamine
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mucosal
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copper
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spermidine
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deamination
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1.4.3.6
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aminoguanidine
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benzylamine
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endotoxin
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ornithine
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semicarbazide-sensitive
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occludin
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d-lactate
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copper-containing
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cadaverine
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bowel
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biogenic
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semicarbazide
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villus
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ileum
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d-lactic
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jejunal
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lysyl
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tyramine
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zonula
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piglets
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pao
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claudin-1
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methylamine
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n-methyltransferase
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pargyline
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agmatine
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tryptamine
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renalase
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hansenula
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occludens-1
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postheparin
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phenylhydrazine
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lentil
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deprenyl
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beta-aminopropionitrile
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oxidase-like
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clorgyline
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beta-phenylethylamine
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phenylethylamine
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quinoproteins
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samdc
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globiformis
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diagnostics
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analysis
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biotechnology
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medicine
- 1.4.3.22
- polyamine
- oxidases
-
monoamine
- mucosal
- copper
- spermidine
-
deamination
-
1.4.3.6
- aminoguanidine
- benzylamine
- endotoxin
- ornithine
-
semicarbazide-sensitive
- occludin
- d-lactate
-
copper-containing
- cadaverine
- bowel
-
biogenic
- semicarbazide
- villus
- ileum
-
d-lactic
- jejunal
-
lysyl
- tyramine
-
zonula
-
piglets
- pao
-
claudin-1
- methylamine
- n-methyltransferase
- pargyline
- agmatine
- tryptamine
- renalase
- hansenula
-
occludens-1
-
postheparin
- phenylhydrazine
- lentil
- deprenyl
- beta-aminopropionitrile
-
oxidase-like
- clorgyline
- beta-phenylethylamine
- phenylethylamine
-
quinoproteins
- samdc
- globiformis
- diagnostics
- analysis
- biotechnology
- medicine
Reaction
Synonyms
ABP1, AGAO, Amiloride-binding protein, Amine oxidase, BSAO, Copper amine oxidase, DAO, DAO-1, Diamine oxidase, EC 1.4.3.6, ELAO, GPAO, hDAO, histaminase, histamine dehydrogenase, histamine oxidase, LCAO, LSAO, methylputrescine oxidase, More, MPO, N-methylputrescine oxidase, pea seedling amine oxidase, PKAO, PPLO, PSAO, pWGH15, rhDAO, vDAO
ECTree
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Inhibitors
Inhibitors on EC 1.4.3.22 - diamine oxidase
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(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
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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
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3-cyclohexylmethylamino-4-aminomethylpyridine dihydrochloride monohydrate
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4,4'-[[4-(aminomethyl)pyridine-3,5-diyl]bis(oxy)]dibutan-1-ol dihydrochloride
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4-(aminomethyl)-N,N'-bis(1-methylethyl)pyridine-3,5-diamine dihydrochloride
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gabexate mesylate
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anti coagulant drug, competitive vs. agmatine and putrescine oxidation
methylglyoxalbis(guanylhydrazone)
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without preincubation competitive inhibitor, non-competitive after 1 h preincubation
N,N-diethyldithiocarbamate
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the inactive enzyme is restored with Cu2+ to 65% of its initial activity
NaCl
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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
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uncompetitive vs. p-dimethylaminomethylbenzylamine, SCN- is equatorially coordinated to a tetragonal Cu(II) center
0.1 mM, 28% inhibition; 0.1 mM, 28% inhibition
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10 mM with 2 mM N-methylputrescine as substrate, 32% relative inhibition
1,3-diaminopropane
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10 mM with 2 mM N-methylputrescine as substrate, 70% relative inhibition
1,3-diaminopropane
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10 mM with 2 mM N-methylputrescine as substrate, 93% relative inhibition
aminoguanidine
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0.00001 mM, 50% inhibition, putrescine or histamine as substrates
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noncompetitive with respect to oxidative half-reaction, noncompetitive with respect to reductive half-reaction
azide
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partially competitive with respect to oxidative half-reaction, competitive with respect to reductive half-reaction
azide
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mode of inhibition is dependent of azide concentration with respect to oxidative half-reaction, noncompetitive with respect to reductive half-reaction
azide
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competitive with respect to oxidative half-reaction, noncompetitive with respect to reductive half-reaction
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0.0033 mM, with 0.01 mM tyramine, 89.4% inhibition
beta-hydroxyethylhydrazine
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0.0033 mM, with 0.01 mM tyramine, 89.5% inhibition
beta-hydroxyethylhydrazine
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0.0033 mM, with 0.01 mM cadaverine, 85.5% inhibition
clonidine
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antihypertensive drug, competitive vs. agmatine and putrescine oxidation
diethyldithiocarbamate
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0.0033 mM, with 0.01 mM tyramine, 90.4% inhibition
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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
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1 mM, inhibits activity completely, is used to stop the enzyme reaction
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10 mM with 2 mM N-methylputrescine as substrate, 19% relative inhibition
n-butylamine
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10 mM with 2 mM N-methylputrescine as substrate, 66% relative inhibition
n-butylamine
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10 mM with 2 mM N-methylputrescine as substrate, 60% relative inhibition
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10 mM with 2 mM N-methylputrescine as substrate, 34% relative inhibition
N-methyl-1,3-diamonopropane
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10 mM with 2 mM N-methylputrescine as substrate, 55% relative inhibition
N-methyl-1,3-diamonopropane
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10 mM with 2 mM N-methylputrescine as substrate, 61% relative inhibition
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10 mM with 2 mM N-methylputrescine as substrate, 70% relative inhibition
N-methylbutylamine
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10 mM with 2 mM N-methylputrescine as substrate, 23% relative inhibition
N-methylbutylamine
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10 mM with 2 mM N-methylputrescine as substrate, 19% relative inhibition
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10 mM with 2 mM N-methylputrescine as substrate, 75% relative inhibition
N-methylpropylamine
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10 mM with 2 mM N-methylputrescine as substrate, 13% relative inhibition
N-methylpropylamine
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10 mM with 2 mM N-methylputrescine as substrate, 22% relative inhibition
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10 mM with 2 mM N-methylputrescine as substrate, 28% relative inhibition
n-Propylamine
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10 mM with 2 mM N-methylputrescine as substrate, 23% relative inhibition
n-Propylamine
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10 mM with 2 mM N-methylputrescine as substrate, 48% relative inhibition
NaN3
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uncompetitive vs. p-dimethylaminomethylbenzylamine, N3- is equatorially coordinated to a tetragonal Cu(II) center
phenylhydrazine
1 mM, complete inhibition; 1 mM, complete inhibition
additional information
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the recombinant enzyme is not inhibited by ethanol, acetaldehyde, disulfiram, diethyldithiocarbamate or cyanamide
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additional information
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inhibition 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 inhibitors of the Hyoscyamus enzyme than of the others DAOs
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additional information
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primary amines inhibit pea and pig kidney DAO activities more strongly than the Hyoscyamus niger. N-methylated amines are stronger inhibitors of the Hyoscyamus enzyme than of the others DAOs
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additional information
clorgyline and deprenyl do not decrease DAO activity
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additional information
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no substrate inhibition with monoamines; substrate inhibition with diamines
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additional information
alkylamino derivatives of 4-aminomethylpyridine, substrate-like, reversible inhibitors
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additional information
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primary amines inhibit pea and pig kidney DAO activities more strongly than the Hyoscyamus niger. N-methylated amines are stronger inhibitors of the Hyoscyamus enzyme than of the others DAOs
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