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Literature summary 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.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.4.3.22 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

EC Number Inhibitors Comment Organism Structure
1.4.3.22 4,4'-(pentane-1,5-diylbis(oxy))dibenzimidamide noncompetitive inhibition Homo sapiens
1.4.3.22 Berenil mixed inhibition Homo sapiens
1.4.3.22 cimetidine mixed inhibition Homo sapiens
1.4.3.22 clonidine mixed inhibition Homo sapiens
1.4.3.22 isoniazid noncompetitive inhibition Homo sapiens
1.4.3.22 Pentamidine mixed inhibition Homo sapiens

Metals/Ions

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

Organism

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

Posttranslational Modification

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

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
1.4.3.22 homodimer crystal structure Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.4.3.22 Diamine oxidase
-
Homo sapiens
1.4.3.22 hDAO
-
Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.4.3.22 37
-
assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.3.22 7.2
-
assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.3.22 topaquinone
-
Homo sapiens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.4.3.22 0.0011
-
4,4'-(pentane-1,5-diylbis(oxy))dibenzimidamide
-
Homo sapiens
1.4.3.22 0.013
-
Berenil
-
Homo sapiens
1.4.3.22 0.09
-
cimetidine
-
Homo sapiens
1.4.3.22 0.1
-
clonidine
-
Homo sapiens
1.4.3.22 0.29
-
Pentamidine
-
Homo sapiens
1.4.3.22 0.9
-
isoniazid
-
Homo sapiens