Literature summary for 1.4.3.22 extracted from

McGrath, A.P.; Hilmer, K.M.; Collyer, C.A.; Shepard, E.M.; Elmore, B.O.; Brown, D.E.; Dooley, D.M.; Guss, J.M.
Structure and inhibition of human diamine oxidase (2009), Biochemistry, 48, 9810-9822.

Cloned(Commentary)

Cloned (Comment)	Organism
cloned and expressed in Drosophila S2 cells	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
the structure of the native enzyme is determined by X-ray crystallography to a resolution of 1.8 A. The homodimeric structure has the archetypal amine oxidase fold. Two active sites, one in each subunit, are characterized by the presence of a copper ion and a topaquinone residue formed. Substrate binding pocket and entry channel of hDAO are distinctly different from other amine oxidases in accord with the different substrate specificities. The structures of two inhibitor complexes of hDAO, berenil and pentamidine, are refined to resolutions of 2.1 and 2.2 A, respectively. They bind noncovalently in the active-site channel. The inhibitor binding suggests that an aspartic acid residue, conserved in all diamine oxidases but absent from other amine oxidases, is responsible for the diamine specificity by interacting with the second amino group of preferred diamine substrates	Homo sapiens

Crystallization (Comment)

Organism

the structure of the native enzyme is determined by X-ray crystallography to a resolution of 1.8 A. The homodimeric structure has the archetypal amine oxidase fold. Two active sites, one in each subunit, are characterized by the presence of a copper ion and a topaquinone residue formed. Substrate binding pocket and entry channel of hDAO are distinctly different from other amine oxidases in accord with the different substrate specificities. The structures of two inhibitor complexes of hDAO, berenil and pentamidine, are refined to resolutions of 2.1 and 2.2 A, respectively. They bind noncovalently in the active-site channel. The inhibitor binding suggests that an aspartic acid residue, conserved in all diamine oxidases but absent from other amine oxidases, is responsible for the diamine specificity by interacting with the second amino group of preferred diamine substrates

Homo sapiens

Inhibitors

Inhibitors	Comment	Organism
4,4'-(pentane-1,5-diylbis(oxy))dibenzimidamide	noncompetitive inhibition	Homo sapiens
Berenil	mixed inhibition	Homo sapiens
cimetidine	mixed inhibition	Homo sapiens
clonidine	mixed inhibition	Homo sapiens
isoniazid	noncompetitive inhibition	Homo sapiens
Pentamidine	mixed inhibition	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	enzmye contains 2 Ca2+-binding sites per subunit	Homo sapiens
copper	enzyme binds Cu	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P19801	in human three functioning genes exist that encode copper-containing amine oxidases	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	putative N-glycosylation sites: Asn110, Asn538, and Asn745	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
putrescine + H2O + O2	-	Homo sapiens	?	-	?

Subunits

Subunits	Comment	Organism
homodimer	crystal structure	Homo sapiens

Synonyms

Synonyms	Comment	Organism
Diamine oxidase	-	Homo sapiens
hDAO	-	Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Homo sapiens

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.2	-	assay at	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
topaquinone	-	Homo sapiens

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism
0.0011	-	4,4'-(pentane-1,5-diylbis(oxy))dibenzimidamide	-	Homo sapiens
0.013	-	Berenil	-	Homo sapiens
0.09	-	cimetidine	-	Homo sapiens
0.1	-	clonidine	-	Homo sapiens
0.29	-	Pentamidine	-	Homo sapiens
0.9	-	isoniazid	-	Homo sapiens