FAD dependent oxidoreductase family (original) (raw)
In molecular biology, the FAD dependent oxidoreductase family of proteins is a family of FAD dependent oxidoreductases. Members of this family include Glycerol-3-phosphate dehydrogenase EC 1.1.99.5, Sarcosine oxidase beta subunit EC 1.5.3.1, D-amino-acid dehydrogenase EC 1.4.99.1, D-aspartate oxidase EC 1.4.3.1. D-aspartate oxidase EC 1.4.3.1 (DASOX) is an enzyme, structurally related to DAO, which catalyses the same reaction but is active only toward dicarboxylic D-amino acids. In DAO, a conserved histidine has been shown to be important for the enzyme's catalytic activity.
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dbo:abstract | In molecular biology, the FAD dependent oxidoreductase family of proteins is a family of FAD dependent oxidoreductases. Members of this family include Glycerol-3-phosphate dehydrogenase EC 1.1.99.5, Sarcosine oxidase beta subunit EC 1.5.3.1, D-amino-acid dehydrogenase EC 1.4.99.1, D-aspartate oxidase EC 1.4.3.1. D-amino acid oxidase EC 1.4.3.3 (DAMOX or DAO) is an FAD flavoenzyme that catalyses the oxidation of neutral and basic D-amino acids into their corresponding keto acids. DAOs have been characterised and sequenced in fungi and vertebrates where they are known to be located in the peroxisomes. D-aspartate oxidase EC 1.4.3.1 (DASOX) is an enzyme, structurally related to DAO, which catalyses the same reaction but is active only toward dicarboxylic D-amino acids. In DAO, a conserved histidine has been shown to be important for the enzyme's catalytic activity. (en) |
dbo:symbol | DAO |
dbo:thumbnail | wiki-commons:Special:FilePath/PDB_1c0i_EBI.jpg?width=300 |
dbo:wikiPageID | 32571371 (xsd:integer) |
dbo:wikiPageLength | 2678 (xsd:nonNegativeInteger) |
dbo:wikiPageRevisionID | 1077642363 (xsd:integer) |
dbo:wikiPageWikiLink | dbr:Peroxisomes dbr:D-aspartate_oxidase dbr:Enzyme dbr:Fungus dbr:Conserved_sequence dbr:Catalytic dbr:D-amino_acid_oxidase dbr:DAO_(disambiguation) dbr:Amino_acids dbc:Molecular_biology dbr:Flavin_adenine_dinucleotide dbr:Glycerol-3-phosphate_dehydrogenase dbr:Redox dbc:Protein_domains dbr:Histidine dbr:D-amino-acid_dehydrogenase dbr:Catalysis dbr:Sarcosine_oxidase dbr:Oxidoreductases dbr:Vertebrates dbr:Sequenced dbr:Structurally |
dbp:caption | crystal structure of d-amino acid oxidase in complex with two anthranylate molecules (en) |
dbp:interpro | IPR006076 (en) |
dbp:membranomeSuperfamily | 249 (xsd:integer) |
dbp:name | FAD dependent oxidoreductase (en) |
dbp:pfam | PF01266 (en) |
dbp:pfamClan | CL0063 (en) |
dbp:prosite | PDOC00753 (en) |
dbp:scop | 1 (xsd:integer) |
dbp:symbol | DAO (en) |
dbp:wikiPageUsesTemplate | dbt:Cleanup_rewrite dbt:EC_number dbt:Infobox_protein_family dbt:InterPro_content dbt:Reflist |
dct:subject | dbc:Molecular_biology dbc:Protein_domains |
gold:hypernym | dbr:Family |
rdf:type | owl:Thing dbo:Biomolecule wikidata:Q206229 wikidata:Q8054 dbo:Protein |
rdfs:comment | In molecular biology, the FAD dependent oxidoreductase family of proteins is a family of FAD dependent oxidoreductases. Members of this family include Glycerol-3-phosphate dehydrogenase EC 1.1.99.5, Sarcosine oxidase beta subunit EC 1.5.3.1, D-amino-acid dehydrogenase EC 1.4.99.1, D-aspartate oxidase EC 1.4.3.1. D-aspartate oxidase EC 1.4.3.1 (DASOX) is an enzyme, structurally related to DAO, which catalyses the same reaction but is active only toward dicarboxylic D-amino acids. In DAO, a conserved histidine has been shown to be important for the enzyme's catalytic activity. (en) |
rdfs:label | FAD dependent oxidoreductase family (en) |
owl:sameAs | freebase:FAD dependent oxidoreductase family wikidata:FAD dependent oxidoreductase family https://global.dbpedia.org/id/8NSwU |
prov:wasDerivedFrom | wikipedia-en:FAD_dependent_oxidoreductase_family?oldid=1077642363&ns=0 |
foaf:depiction | wiki-commons:Special:FilePath/PDB_1c0i_EBI.jpg |
foaf:isPrimaryTopicOf | wikipedia-en:FAD_dependent_oxidoreductase_family |
is dbo:wikiPageWikiLink of | dbr:D-aspartate_oxidase dbr:D-amino_acid_oxidase dbr:Ergine |
is foaf:primaryTopic of | wikipedia-en:FAD_dependent_oxidoreductase_family |