Literature summary for 1.4.3.22 extracted from

McGrath, A.P.; Hilmer, K.M.; Collyer, C.A.; Dooley, D.M.; Guss, J.M.
A new crystal form of human diamine oxidase (2010), Acta Crystallogr. Sect. F, 66, 137-142.

Cloned(Commentary)

Cloned (Comment)	Organism
gene AOC1, expression of hDAO as a secreted enzyme in Drosophila S2 cells	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant wild-type hDAO, hanging drop vapour diffusion, 200 nl protein solution, containing 10 mg/ml protein in 100 mM HEPES, pH 7.2, and 150 mM KCl, and 200 nl crystallant solution, containing 0.1 M MES, pH 6.5, and 12% w/v PEG 20000, are equilibrated over 0.075 ml reservoir solution at room temperature, eight weeks, method optimization using manually dispensed hanging-drop crystallization experiments containing 0.002 ml each of protein and crystallant equilibrated over 0.5 ml reservoir solution, best diffracting crystals grow using 0.1 M MES pH 6.1 and 12% w/v PEG at room temperature over a period of two months, X-ray diffraction structure determination and analysis at 2.1 A resolution	Homo sapiens

Crystallization (Comment)

Organism

purified recombinant wild-type hDAO, hanging drop vapour diffusion, 200 nl protein solution, containing 10 mg/ml protein in 100 mM HEPES, pH 7.2, and 150 mM KCl, and 200 nl crystallant solution, containing 0.1 M MES, pH 6.5, and 12% w/v PEG 20000, are equilibrated over 0.075 ml reservoir solution at room temperature, eight weeks, method optimization using manually dispensed hanging-drop crystallization experiments containing 0.002 ml each of protein and crystallant equilibrated over 0.5 ml reservoir solution, best diffracting crystals grow using 0.1 M MES pH 6.1 and 12% w/v PEG at room temperature over a period of two months, X-ray diffraction structure determination and analysis at 2.1 A resolution

Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Cu2+	required, binding structure at the active site, overview	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Homo sapiens	hDAO is unique among CAOs in that it has a distinct substrate preference for diamines	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P19801	gene AOC1	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant secreted hDAO from Drosophila S2 cells	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	hDAO is unique among CAOs in that it has a distinct substrate preference for diamines	Homo sapiens	?	-	?
additional information	active site of hDAO: contacts made by cofactor trihydroxyphenylalanine quinone to the active-site Cu2+, and Thr685 and to a glycerol molecule within the active-site channel	Homo sapiens	?	-	?

Subunits

Subunits	Comment	Organism
More	hDAO has the archetypal CAO fold with each subunit of hDAO being comprised of domains D2, residues 27-135, D3, residues 144-258, and D4, residues 310-751. The domains are linked by loop regions consisting of residues 136-143 between D2 and D3 and residues 259-309 linking D3 to D4, structure and modelling, overview	Homo sapiens

Synonyms

Synonyms	Comment	Organism
DAO	-	Homo sapiens
More	the enzyme is a member of the copper-containing amine oxidase, CAO, family of enzymes	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
trihydroxyphenylalanine quinone	-	Homo sapiens

General Information

General Information	Comment	Organism
metabolism	hDAO is the frontline enzyme for histamine metabolism	Homo sapiens