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
-
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
-
analysis
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biotechnology
-
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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KM Value
KM Value on EC 1.4.3.22 - diamine oxidase
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additional information
additional information
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the kinetic properties of the MPO1 enzyme may play an important role in determining the pyridine alkaloid profiles observed in tobacco roots
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0.35
1,3-diaminopropane
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Vmax: 11.3 nkat, pH and temperature not specified in the publication
0.31
1,4-diaminobutane
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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
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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
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Vmax: 11.1 nkat, pH and temperature not specified in the publication
2.85
1,4-diaminobutane
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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
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enzyme from placenta, at 37°C, pH not specified in the publication
2.032
Butylamine
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enzyme from seminal plasma, at 37°C, pH not specified in the publication
0.26
cadaverine
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pH 7.9, 30°C, lowest KM-value compared with N-putrescine or cadaverine as substrates, Vmax: 96.2 pkat
0.3
cadaverine
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pH 7.9, 30°C, higher KM-value compared with N-putrescine or cadaverine as substrates, Vmax: 20.5 pkat
1.79
cadaverine
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Vmax: 5.2 nkat, pH and temperature not specified in the publication
2.84
cadaverine
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immobilized enzyme, apparent value, in 0.1 M phosphate buffer, pH 7.4, at 25°C
6.25
cadaverine
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pH 7.9, 30°C, higher KM-value compared with N-putrescine or cadaverine as substrates, Vmax: 19.6 pkat, specifiity constant 1% of the constant for N-methylputrescine
0.108
histamine
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enzyme from seminal plasma, at 37°C, pH not specified in the publication
0.124
histamine
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enzyme from placenta, at 37°C, pH not specified in the publication
1.05
histamine
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immobilized enzyme, apparent value, in 0.1 M phosphate buffer, pH 7.4, at 25°C
0.075
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enzyme from seminal plasma, at 37°C, pH not specified in the publication
0.158
Methylhistamine
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enzyme from placenta, at 37°C, pH not specified in the publication
0.19
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Vmax: 28.8 nkat, pH and temperature not specified in the publication
0.33
N-methylputrescine
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pH 7.9, 30°C, lowest KM-value compared with putrescine or cadaverine as substrates, Vmax: 90.4 pkat
0.82
N-methylputrescine
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pH 7.9, 30°C, lowest KM-value compared with putrescine or cadaverine as substrates, Vmax: 23.3 pkat
1.22
N-methylputrescine
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pH 7.9, 30°C, highest KM-value compared with putrescine or cadaverine as substrates, Vmax: 93.5 pkat
0.00037
reaction performed with benzylamine. KM value is too low to be measurable. Therefore, it is calculated from KCAT_KM with putrescine
0.84
Phenylethylamine
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immobilized enzyme, apparent value, in 0.1 M phosphate buffer, pH 7.4, at 25°C
0.063
putrescine
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enzyme from seminal plasma, at 37°C, pH not specified in the publication
0.094
putrescine
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enzyme from placenta, at 37°C, pH not specified in the publication
1.58
putrescine
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immobilized enzyme, apparent value, in 0.1 M phosphate buffer, pH 7.4, at 25°C
0.033
spermidine
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enzyme from seminal plasma, at 37°C, pH not specified in the publication
0.057
spermidine
-
enzyme from placenta, at 37°C, pH not specified in the publication
1.77
spermidine
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immobilized enzyme, apparent value, in 0.1 M phosphate buffer, pH 7.4, at 25°C
0.031
spermine
-
enzyme from seminal plasma, at 37°C, pH not specified in the publication
0.055
spermine
-
enzyme from placenta, at 37°C, pH not specified in the publication
1.14
spermine
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immobilized enzyme, apparent value, in 0.1 M phosphate buffer, pH 7.4, at 25°C
0.53
tyramine
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immobilized enzyme, apparent value, in 0.1 M phosphate buffer, pH 7.4, at 25°C