{PDOC00573}
{PS00677; DAO}
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* D-amino acid oxidases signature *
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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.

-Consensus pattern: [LIVM](2)-H-[NHA]-Y-G-x-[GSA](2)-x-G-x(5)-G-x-A
                    [H may be an active site residue]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: May 2004 / Text revised.

[ 1] Negri A., Ceciliani F., Tedeschi G., Simonic T., Ronchi S.
     "The primary structure of the flavoprotein D-aspartate oxidase from
     beef kidney."
     J. Biol. Chem. 267:11865-11871(1992).
     PubMed=1601857
[ 2] Miyano M., Fukui K., Watanabe F., Takahashi S., Tada M., Kanashiro M.,
     Miyake Y.
     "Studies on Phe-228 and Leu-307 recombinant mutants of porcine kidney
     D-amino acid oxidase: expression, purification, and
     characterization."
     J. Biochem. 109:171-177(1991).
     PubMed=1673125

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