PROSITE documentation PDOC00573D-amino acid oxidases signature
D-amino acid oxidase (EC 1.4.3.3) (DAMOX or DAO) is an FAD flavoenzyme that catalyzes the oxidation of neutral and basic D-amino acids into their corresponding keto acids. DAOs have been characterized 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 catalyzes 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. We have used the conserved region around this residue as a signature pattern for these enzymes.
Last update:May 2004 / Text revised.
-------------------------------------------------------------------------------
PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Negri A. Ceciliani F. Tedeschi G. Simonic T. Ronchi S. |
| Title | The primary structure of the flavoprotein D-aspartate oxidase from beef kidney. | |
| Source | J. Biol. Chem. 267:11865-11871(1992). | |
| PubMed ID | 1601857 |
| 2 | Authors | Miyano M. Fukui K. Watanabe F. Takahashi S. Tada M. Kanashiro M. Miyake Y. |
| Title | Studies on Phe-228 and Leu-307 recombinant mutants of porcine kidney D-amino acid oxidase: expression, purification, and characterization. | |
| Source | J. Biochem. 109:171-177(1991). | |
| PubMed ID | 1673125 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
View entry in original PROSITE document format
View entry in raw text format (no links)