Amine oxidase (copper-containing) (original) (raw)
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:
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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 | wiki-commons:Special:FilePath/3LOY.pdb.png?width=300 |
dbo:wikiPageID | 14147665 (xsd:integer) |
dbo:wikiPageLength | 11729 (xsd:nonNegativeInteger) |
dbo:wikiPageRevisionID | 1032085059 (xsd:integer) |
dbo:wikiPageWikiLink | dbr:Amidase dbr:Amine_oxidase dbr:Pyrroloquinoline_quinone dbr:List_of_enzymes dbr:Hydrogen_peroxide dbc:Enzymes_of_known_structure dbr:Copper_in_health dbr:Enzyme dbr:Copper dbr:Substrate_(biochemistry) dbc:EC_1.4.3 dbr:Topaquinone dbr:Tryptophan_metabolism dbr:Tyrosine_metabolism dbr:Helix dbr:Ammonia dbr:Oxygen dbr:Cell_wall dbr:Diamine_oxidase dbr:Product_(chemistry) dbr:Protein dbc:Copper_enzymes dbr:AOC1 dbr:Histidine_metabolism dbr:Hydrolase dbr:Hansenula_polymorpha dbr:AOC2 dbr:AOC3 dbc:Pyrroloquinoline_quinone_enzymes dbr:Cofactor_(biochemistry) dbr:Phenylalanine_metabolism dbr:Metabolism dbr:X-ray_crystallography dbr:Vascular_adhesion_protein dbr:Water dbr:Primary-amine_oxidase dbr:Oxidoreductase dbr:Urea_cycle_and_metabolism_of_amino_groups dbr:RCHO dbr:Proceedings_of_the_Royal_Society_B dbr:Redox_cofactor dbr:Beta-alanine_metabolism dbr:Beta-sheet dbr:Primary_amines dbr:Alkaloid_biosynthesis_ii dbr:Glycine,_serine_and_threonine_metabolism dbr:Histidine_residue |
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 | dbt:Cite_journal dbt:EC_number dbt:Enzyme dbt:Enzymes dbt:Infobox_protein_family dbt:Portal_bar dbt:Refbegin dbt:Refend dbt:Reflist dbt:CH-NH2_oxidoreductases dbt:Pfam_box |
dcterms:subject | dbc:Enzymes_of_known_structure dbc:EC_1.4.3 dbc:Copper_enzymes dbc:Pyrroloquinoline_quinone_enzymes |
rdf:type | owl:Thing dbo:Biomolecule wikidata:Q206229 wikidata:Q8047 yago:WikicatCopperEnzymes yago:Abstraction100002137 yago:Activator114723079 yago:Catalyst114723628 yago:Chemical114806838 yago:Compound114818238 yago:Enzyme114732946 yago:Macromolecule114944888 yago:Material114580897 yago:Matter100020827 yago:Molecule114682133 yago:OrganicCompound114727670 yago:Part113809207 yago:PhysicalEntity100001930 yago:Protein114728724 yago:Relation100031921 dbo:Enzyme yago:Substance100019613 yago:Thing100002452 yago:Unit109465459 yago:WikicatEnzymesOfKnownStructure yago:WikicatPyrroloquinolineQuinoneEnzymes |
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 | freebase:Amine oxidase (copper-containing) yago-res:Amine oxidase (copper-containing) http://www4.wiwiss.fu-berlin.de/drugbank/resource/targets/5633 wikidata:Amine oxidase (copper-containing) dbpedia-it:Amine oxidase (copper-containing) dbpedia-sh:Amine oxidase (copper-containing) dbpedia-sr:Amine oxidase (copper-containing) https://global.dbpedia.org/id/34J7V |
prov:wasDerivedFrom | wikipedia-en:Amine_oxidase_(copper-containing)?oldid=1032085059&ns=0 |
foaf:depiction | wiki-commons:Special:FilePath/3LOY.pdb.png wiki-commons:Special:FilePath/PDB_1d6u_EBI.jpg wiki-commons:Special:FilePath/PDB_1ksi_EBI.jpg wiki-commons:Special:FilePath/PDB_2oqe_EBI.jpg |
foaf:isPrimaryTopicOf | wikipedia-en:Amine_oxidase_(copper-containing) |
foaf:name | amine oxidase (en) |
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