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PROSITE documentation PDOC00573

D-amino acid oxidases signature

Description:

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.

Technical section:

PROSITE method (with tools and information) covered by this documentation:

DAO, PS00677; D-amino acid oxidases signature  (PATTERN)
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
• Retrieve an alignment of Swiss-Prot true positive hits:
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• Retrieve the sequence logo from the alignment
• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00677
• Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00677
• Scan Swiss-Prot/TrEMBL entries against PS00677
• view ligand binding statistics
Matching PDB structures: 1AN9 1C0I 1C0K 1C0L ... [ALL]

References:

1 AuthorsNegri A., Ceciliani F., Tedeschi G., Simonic T., Ronchi S.
TitleThe primary structure of the flavoprotein D-aspartate oxidase from beef kidney.
SourceJ. Biol. Chem. 267:11865-11871(1992).
PubMed ID1601857
2 AuthorsMiyano M., Fukui K., Watanabe F., Takahashi S., Tada M., Kanashiro M., Miyake Y.
TitleStudies on Phe-228 and Leu-307 recombinant mutants of porcine kidney D-amino acid oxidase: expression, purification, and characterization.
SourceJ. Biochem. 109:171-177(1991).
PubMed ID1673125

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