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
-
lysyl
-
tyramine
-
zonula
-
piglets
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pao
-
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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Posttranslational Modification
Posttranslational Modification on EC 1.4.3.22 - diamine oxidase
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glycoprotein
glycoprotein
the enzyme has multiple N-glycosylation sites. The N-glycosylation sites Asn168, Asn538, and Asn745 in recombinant human diamine oxidase carry complex-type glycans, whereas Asn110 carries only mammalian-atypical oligomannosidic glycans. Glycans at Asn168 are predominantly sialylated with bi- to tetra-antennary branches, and Asn538 and Asn745 have similar complex-type glycans with some tissue- and cell line-specific variations. Mutations of Asn168, Asn538, and Asn745 reduce secretion of the recombinant enzyme by 13, 71, and 32%, respectively. Asn538/745 double and Asn168/538/745 triple substitutions reduce rhDAO secretion by 85% and 94%. Because of their locations in the diamine oxidase structure, Asn538 and Asn745 glycosylations might be important for efficient DAO dimer formation. Glycosylation seems essential for reaching high enzyme expression levels in the gastrointestinal tract, kidney, and placenta
glycoprotein
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deglycosylation has no effect on the thermal stability of the enzyme