Location via proxy:   [ UP ]  
[Report a bug]   [Manage cookies]                

About: Amine oxidase (copper-containing)

An Entity of Type: enzyme, from Named Graph: http://dbpedia.org, within Data Space: dbpedia.org

Amine oxidase (copper-containing) (AOC) (EC 1.4.3.21 and EC 1.4.3.22; formerly EC 1.4.3.6) is a family of amine oxidase enzymes which includes both primary-amine oxidase and diamine oxidase; these enzymes catalyze the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. They act as a disulphide-linked homodimer. They catalyse the oxidation of primary amines to aldehydes, with the subsequent release of ammonia and hydrogen peroxide, which requires one copper ion per subunit and topaquinone as cofactor:

thumbnail
Property Value
dbo:abstract
  • Amine oxidase (copper-containing) (AOC) (EC 1.4.3.21 and EC 1.4.3.22; formerly EC 1.4.3.6) is a family of amine oxidase enzymes which includes both primary-amine oxidase and diamine oxidase; these enzymes catalyze the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. They act as a disulphide-linked homodimer. They catalyse the oxidation of primary amines to aldehydes, with the subsequent release of ammonia and hydrogen peroxide, which requires one copper ion per subunit and topaquinone as cofactor: RCH2NH2 + H2O + O2 RCHO + NH3 + H2O2 The 3 substrates of this enzyme are primary amines (RCH2NH2), H2O, and O2, whereas its 3 products are RCHO, NH3, and H2O2. Copper-containing amine oxidases are found in bacteria, fungi, plants and animals. In prokaryotes, the enzyme enables various amine substrates to be used as sources of carbon and nitrogen. This enzyme belongs to oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is amine:oxygen oxidoreductase (deaminating) (copper-containing). This enzyme participates in 8 metabolic pathways: urea cycle and metabolism of amino groups, , histidine metabolism, tyrosine metabolism, phenylalanine metabolism, tryptophan metabolism, beta-alanine metabolism, and . It has 2 cofactors: copper, and PQQ. (en)
  • La ammina ossidasi (contenente rame) è un enzima appartenente alla classe delle ossidoreduttasi, che catalizza la seguente reazione: RCH2NH2 + H2O + O2 ⇄ RCHO + NH3 + H2O2 Si tratta di un gruppo di enzimi in grado di ossidare istamina, monoammine e diammine primarie. Si tratta di contenenti rame. Anche una forma della orotato reduttasi (NADPH) (proveniente da rene di Rattus norvegicus) è in grado di catalizzare la reazione. La diamminossidasi (DAO) è prodotta dal nostro organismo e si trova principalmente nel duodeno e in misura nettamente minore nel fegato e a livello renale. La diaminossidasi è continuamente prodotta e riversata nel lume intestinale, questo permette ad un organismo sano di eliminare, a livello duodenale, l'istamina contenuta negli alimenti. L'attività dell'enzima DAO è promossa da cofattori, quali vitamina B6, rame, zinco, vitamina C. È inibita da alcool, diversi farmaci, l'alterazione degli enterociti nel tratto gastro-intestinale. (it)
dbo:ecNumber
  • 1.4.3.6
dbo:thumbnail
dbo:wikiPageID
  • 14147665 (xsd:integer)
dbo:wikiPageLength
  • 11729 (xsd:nonNegativeInteger)
dbo:wikiPageRevisionID
  • 1032085059 (xsd:integer)
dbo:wikiPageWikiLink
dbp:caption
  • Crystal structure of a copper-containing benzylamine oxidase from Hansenula polymorpha. (en)
  • crystal structure of hansenula polymorpha amine oxidase in complex with xe to 1.6 angstroms (en)
  • crystal structure of a eukaryotic copper-containing amine oxidase at 2.2a resolution (en)
  • crystal structure of e. coli amine oxidase anaerobically reduced with beta-phenylethylamine (en)
dbp:casNumber
  • 9001 (xsd:integer)
dbp:ecNumber
  • 1.400000 (xsd:double)
dbp:goCode
  • 8131 (xsd:integer)
dbp:interpro
  • IPR012854 (en)
  • IPR015798 (en)
  • IPR015800 (en)
  • IPR015802 (en)
dbp:iubmbEcNumber
  • 1 (xsd:integer)
dbp:membranomeSuperfamily
  • 252 (xsd:integer)
dbp:name
  • Copper amine oxidase N-terminal domain (en)
  • Copper amine oxidase, N2 domain (en)
  • Copper amine oxidase, N3 domain (en)
  • Copper amine oxidase, enzyme domain (en)
  • amine oxidase (en)
dbp:pfam
  • PF01179 (en)
  • PF02727 (en)
  • PF02728 (en)
  • PF07833 (en)
dbp:pfamClan
  • CL0047 (en)
dbp:prosite
  • PDOC00895 (en)
dbp:scop
  • 1 (xsd:integer)
dbp:symbol
  • Cu_amine_oxid (en)
  • Cu_amine_oxidN1 (en)
  • Cu_amine_oxidN2 (en)
  • Cu_amine_oxidN3 (en)
dbp:wikiPageUsesTemplate
dcterms:subject
rdf:type
rdfs:comment
  • Amine oxidase (copper-containing) (AOC) (EC 1.4.3.21 and EC 1.4.3.22; formerly EC 1.4.3.6) is a family of amine oxidase enzymes which includes both primary-amine oxidase and diamine oxidase; these enzymes catalyze the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. They act as a disulphide-linked homodimer. They catalyse the oxidation of primary amines to aldehydes, with the subsequent release of ammonia and hydrogen peroxide, which requires one copper ion per subunit and topaquinone as cofactor: (en)
  • La ammina ossidasi (contenente rame) è un enzima appartenente alla classe delle ossidoreduttasi, che catalizza la seguente reazione: RCH2NH2 + H2O + O2 ⇄ RCHO + NH3 + H2O2 Si tratta di un gruppo di enzimi in grado di ossidare istamina, monoammine e diammine primarie. Si tratta di contenenti rame. Anche una forma della orotato reduttasi (NADPH) (proveniente da rene di Rattus norvegicus) è in grado di catalizzare la reazione. (it)
rdfs:label
  • Amine oxidase (copper-containing) (en)
  • Ammina ossidasi (contenente rame) (it)
owl:sameAs
prov:wasDerivedFrom
foaf:depiction
foaf:isPrimaryTopicOf
foaf:name
  • amine oxidase (en)
is dbo:wikiPageRedirects of
is dbo:wikiPageWikiLink of
is foaf:primaryTopic of
Powered by OpenLink Virtuoso    This material is Open Knowledge     W3C Semantic Web Technology     This material is Open Knowledge    Valid XHTML + RDFa
This content was extracted from Wikipedia and is licensed under the Creative Commons Attribution-ShareAlike 3.0 Unported License