Diamine oxidase

Diamine oxidase (DAO), also known "amine oxidase, copper-containing, 1" (AOC1), formerly called histaminase,[5] is an enzyme (EC 1.4.3.22) involved in the metabolism, oxidation, and inactivation of histamine and other polyamines such as putrescine or spermidine in animals. It belongs to the amine oxidase (copper-containing) (AOC) family of amine oxidase enzymes. In humans, DAO it is encoded by AOC1 gene.

Diamine oxidase
Diamine oxidase dimer, Human
Identifiers
EC number	1.4.3.22
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

AOC1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3HI7, 3HIG, 3HII, 3K5T, 3MPH
Identifiers
Aliases	AOC1, ABP, ABP1, DAO, DAO1, KAO, amine oxidase, copper containing 1, amine oxidase copper containing 1
External IDs	OMIM: 104610 MGI: 1923757 HomoloGene: 68159 GeneCards: AOC1
Gene location (Human) Chr. Chromosome 7 (human)[1] Band 7q36.1 Start 150,824,627 bp[1] End 150,861,504 bp[1]
Gene location (Mouse) Chr. Chromosome 6 (mouse)[2] Band 6 B2.3|6 23.78 cM Start 48,872,896 bp[2] End 48,909,188 bp[2]
Gene ontology Molecular function • primary amine oxidase activity • calcium ion binding • heparin binding • propane-1,3-diamine oxidase activity • protein homodimerization activity • quinone binding • GO:0032403 macromolecular complex binding • histamine oxidase activity • zinc ion binding • methylputrescine oxidase activity • metal ion binding • drug binding • diamine oxidase activity • oxidoreductase activity • copper ion binding Cellular component • bicellular tight junction • cell membrane • peroxisome • extracellular exosome • extracellular region • extracellular • specific granule lumen Biological process • response to antibiotic • cellular response to azide • cellular response to copper ion starvation • amine metabolic process • cellular response to copper ion • xenobiotic metabolic process • cellular response to heparin • oxidation-reduction process • response to drug • cellular response to histamine • neutrophil degranulation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	26	76507
Ensembl	ENSG00000002726	ENSMUSG00000029811
UniProt	P19801	Q8JZQ5
RefSeq (mRNA)	NM_001091 NM_001272072	NM_001161621 NM_001161622 NM_029638
RefSeq (protein)	NP_001082 NP_001259001	n/a
Location (UCSC)	Chr 7: 150.82 – 150.86 Mb	Chr 6: 48.87 – 48.91 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

The highest levels of DAO expression are observed in the digestive tract and the placenta. In humans, a certain subtype of cells of the placenta, namely the extravillous trophoblasts, express the enzyme and secrete it into the blood stream of a pregnant woman. Lowered diamine oxidase values in maternal blood in early pregnancy might be an indication for trophoblast-related pregnancy disorders like early-onset preeclampsia.[6] Normally the enzyme is not or only very scarce present in the blood circulation of humans, but it increases vastly in pregnant women suggesting a protective mechanism against adverse histamine.[6] It is also secreted by eosinophils.[7][8] In case of a shortage of diamine oxidase in the human body, it may appear as an allergy or histamine intolerance.[9][10]

References

1. GRCh38: Ensembl release 89: ENSG00000002726 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000029811 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Wolvekamp MC, de Bruin RW (1994). "Diamine oxidase: an overview of historical, biochemical and functional aspects". Digestive Diseases. 12 (1): 2–14. doi:10.1159/000171432. PMID 8200121.
6. Velicky P, Windsperger K, Petroczi K, Pils S, Reiter B, Weiss T, et al. (April 2018). "Pregnancy-associated diamine oxidase originates from extravillous trophoblasts and is decreased in early-onset preeclampsia". Scientific Reports. 8 (1): 6342. Bibcode:2018NatSR...8.6342V. doi:10.1038/s41598-018-24652-0. PMC 5910386. PMID 29679053.
7. Zeiger RS, Colten HR (February 1977). "Histaminase release from human eosinophils". Journal of Immunology. 118 (2): 540–3. PMID 402420.
8. Agúndez JA, Ayuso P, Cornejo-García JA, Blanca M, Torres MJ, Doña I, et al. (2012). "The diamine oxidase gene is associated with hypersensitivity response to non-steroidal anti-inflammatory drugs". PLOS ONE. 7 (11): e47571. Bibcode:2012PLoSO...747571A. doi:10.1371/journal.pone.0047571. PMC 3495953. PMID 23152756.
9. Manzotti G, Breda D, Di Gioacchino M, Burastero SE (March 2016). "Serum diamine oxidase activity in patients with histamine intolerance". International Journal of Immunopathology and Pharmacology. 29 (1): 105–11. doi:10.1177/0394632015617170. PMC 5806734. PMID 26574488.
10. Music E, Silar M, Korosec P, Kosnik M, Rijavec M (2011). "Serum diamine oxidase (DAO) activity as a diagnostic test for histamine intolerance". Clinical and Translational Allergy. 1 (Suppl 1): P115. doi:10.1186/2045-7022-1-S1-P115. PMC 3354134.

External links

• Amine+Oxidase+(Copper-Containing) at the US National Library of Medicine Medical Subject Headings (MeSH)