FAD dependent oxidoreductase family

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FAD dependent oxidoreductase
PDB 1c0i EBI.jpg
crystal structure of d-amino acid oxidase in complex with two anthranylate molecules
Identifiers
Symbol DAO
Pfam PF01266
Pfam clan CL0063
InterPro IPR006076
PROSITE PDOC00753
SCOP 1kif
SUPERFAMILY 1kif

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[edit]

References[edit]

  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. 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. PMID 1673125. 

This article incorporates text from the public domain Pfam and InterPro IPR006076