Diamine oxidase

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Diamine oxidase
Crystal Structure of Human Diamine Oxidase.png
Ribbon representation of human diamine oxidase[1][2] (rendered with PyMOL)
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

Diamine oxidase, also known as histaminase, is an enzyme (EC 1.4.3.22) involved in the metabolism, oxidation, and inactivation of histamine in animals. Highest content is observed in the digestive tract and placenta. It is also secreted by eosinophils.[3][4] In case of a shortage of diamine oxidase in the human body, it may appear as an allergy or histamine intolerance.

Diamine oxidase should not be confused with D-amino acid oxidase as they are both sometimes referred to as DAO.

References[edit]

  1. ^ PDB: 3HI7
  2. ^ McGrath AP, Hilmer KM, Collyer CA, Shepard EM, Elmore BO, Brown DE, Dooley DM, Guss JM (2009). "Structure and inhibition of human diamine oxidase". Biochemistry. 48 (41): 9810–22. doi:10.1021/bi9014192. PMC 2791411Freely accessible. PMID 19764817. 
  3. ^ Zeiger RS, Colten HR (1977). "Histaminase release from human eosinophils". Journal of Immunology. 118 (2): 540–3. PMID 402420. 
  4. ^ Agúndez JA, Ayuso P, Cornejo-García JA, Blanca M, Torres MJ, Doña I, Salas M, Blanca-López N, Canto G, Rondon C, Campo P, Laguna JJ, Fernández J, Martínez C, García-Martín E (2012). "The diamine oxidase gene is associated with hypersensitivity response to non-steroidal anti-inflammatory drugs". PLoS ONE. 7 (11): e47571. doi:10.1371/journal.pone.0047571. PMC 3495953Freely accessible. PMID 23152756. 

See also[edit]

External links[edit]