FAD dependent oxidoreductase
crystal structure of d-amino acid oxidase in complex with two anthranylate molecules
Identifiers
SymbolDAO
PfamPF01266
Pfam clanCL0063
InterProIPR006076
PROSITEPDOC00753
SCOP21kif / SCOPe / SUPFAM
Membranome249
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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) [1] 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 [2] to be important for the enzyme's catalytic activity.

See also

References

  1. Negri A, Ceciliani F, Tedeschi G, Simonic T, Ronchi S (June 1992). "The primary structure of the flavoprotein D-aspartate oxidase from beef kidney". J. Biol. Chem. 267 (17): 11865–71. doi:10.1016/S0021-9258(19)49778-0. PMID 1601857.
  2. Miyano M, Fukui K, Watanabe F, Takahashi S, Tada M, Kanashiro M, Miyake Y (January 1991). "Studies on Phe-228 and Leu-307 recombinant mutants of porcine kidney D-amino acid oxidase: expression, purification, and characterization". J. Biochem. 109 (1): 171–7. doi:10.1093/oxfordjournals.jbchem.a123340. PMID 1673125.
This article incorporates text from the public domain Pfam and InterPro: IPR006076
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