Diamine oxidase [copper-containing]

Function

Catalyzes the oxidative deamination of primary amines to the corresponding aldehydes with the concomitant production of hydrogen peroxide and ammonia. Its preferred substrates are the diamines histamine and 1-methylhistamine and it could therefore play a role in allergic and immune responses. Has a broad specificity for diamines and can also act on cadaverine and putrescine, two products of amino acid catabolism. It could also act on polyamines, like spermidine and spermine though less efficiently, and regulate various biological processes.

Classification

Family (Pfam)

PF01179 Cu_amine_oxid, PF02727 Cu_amine_oxidN2, PF02728 Cu_amine_oxidN3

InterPro

Cu_Am_Ox_Cu-bd, Cu_Am_ox_TPQ-bd, Cu_amine_oxidase, Cu_amine_oxidase_C, Cu_amine_oxidase_C_sf, Cu_amine_oxidase_N-reg, Cu_amine_oxidase_N2, Cu_amine_oxidase_N3

Functional cluster

Membrane Channels & Lipid-Anchored Proteins

Experimental structures · PDB · 5

• 3HI7 X-ray 1.80A
• 3HIG X-ray 2.09A
• 3HII X-ray 2.15A
• 3K5T X-ray 2.11A
• 3MPH X-ray 2.05A

A predicted model is available from AlphaFold.

Gene Ontology · 17

• GO:0005923 bicellular tight junction
• GO:0070062 extracellular exosome
• GO:0005576 extracellular region
• GO:0005615 extracellular space
• GO:0005777 peroxisome
• GO:0005886 plasma membrane
• GO:0035580 specific granule lumen
• GO:0005509 calcium ion binding
• GO:0005507 copper ion binding
• GO:0052597 diamine oxidase activity
• GO:0008201 heparin binding
• GO:0052598 histamine oxidase activity
• GO:0008131 primary methylamine oxidase activity
• GO:0042803 protein homodimerization activity
• GO:0050232 putrescine oxidase activity
• GO:0048038 quinone binding
• GO:0009445 putrescine metabolic process

Drugs targeting this protein · 1

• PROXIBARBAL activator

Related proteins · sequence + function similarity

• Diamine oxidase [copper-containing] 0.99
• Diamine oxidase [copper-containing] 0.98
• Diamine oxidase [copper-containing] 0.97
• Amine oxidase [copper-containing] 3 0.96
• Amine oxidase [copper-containing] 3 0.96
• Amine oxidase [copper-containing] 2 0.95
• Amine oxidase [copper-containing] 2 0.95
• Amine oxidase [copper-containing] 3 0.95
• Amine oxidase [copper-containing] 3 0.95
• Primary amine oxidase, lung isozyme 0.94
• Amine oxidase [copper-containing] 3 0.94
• Primary amine oxidase, liver isozyme 0.93

Co-cited proteins · studied together in the literature

• Diamine oxidase [copper-containing] 1 shared papers

Literature · 9 cited papers

• Structure and inhibition of human diamine oxidase. Biochemistry · 2009
• The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. · 2004
• The DNA sequence of human chromosome 7. Nature · 2003
• Human kidney diamine oxidase: heterologous expression, purification, and characterization. J. Biol. Inorg. Chem. · 2002
• cDNA sequences of variant forms of human placenta diamine oxidase. Biochem. Genet. · 1995
• The human gene for diamine oxidase, an amiloride binding protein. Molecular cloning, sequencing, and characterization of the promoter. J. Biol. Chem. · 1994
• Diamine oxidase is the amiloride-binding protein and is inhibited by amiloride analogues. J. Biol. Chem. · 1994
• Human kidney amiloride-binding protein: cDNA structure and functional expression. Proc. Natl. Acad. Sci. U.S.A. · 1990
• Oxidation of polymines by diamine oxidase from human seminal plasma. Biochem. J. · 1975