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Identification
HMDB Protein ID HMDBP00206
Secondary Accession Numbers
  • 5438
Name D-amino-acid oxidase
Synonyms
  1. DAAO
  2. DAMOX
  3. DAO
Gene Name DAO
Protein Type Unknown
Biological Properties
General Function Involved in D-amino-acid oxidase activity
Specific Function Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids.
Pathways
  • Arginine and proline metabolism
  • Arginine and proline metabolism
  • Arginine: Glycine Amidinotransferase Deficiency (AGAT Deficiency)
  • Creatine deficiency, guanidinoacetate methyltransferase deficiency
  • D-Arginine and D-ornithine metabolism
  • D-Arginine and D-Ornithine Metabolism
  • Glycine, serine and threonine metabolism
  • Guanidinoacetate Methyltransferase Deficiency (GAMT Deficiency)
  • Hyperornithinemia with gyrate atrophy (HOGA)
  • Hyperornithinemia-hyperammonemia-homocitrullinuria [HHH-syndrome]
  • Hyperprolinemia Type I
  • Hyperprolinemia Type II
  • L-arginine:glycine amidinotransferase deficiency
  • Ornithine Aminotransferase Deficiency (OAT Deficiency)
  • Peroxisome
  • Prolidase Deficiency (PD)
  • Prolinemia Type II
Reactions
A D-amino acid + Water + Oxygen → a 2-oxo acid + Ammonia + Hydrogen peroxide details
Glycine + Water + Oxygen → Glyoxylic acid + Ammonia + Hydrogen peroxide details
D-Ornithine + Water + Oxygen → 5-Amino-2-oxopentanoic acid + Ammonia + Hydrogen peroxide details
D-Proline + Oxygen → 1-Pyrroline-2-carboxylic acid + Hydrogen peroxide details
cis-4-Hydroxy-D-proline + Oxygen → 1-Pyrroline-4-hydroxy-2-carboxylate + Hydrogen peroxide details
Cephalosporin C + Water + Oxygen → (7R)-7-(5-Carboxy-5-oxopentanoyl)aminocephalosporinate + Ammonia + Hydrogen peroxide details
GO Classification
Biological Process
cellular nitrogen compound metabolic process
glyoxylate metabolic process
dopamine biosynthetic process
D-alanine catabolic process
D-serine catabolic process
leucine metabolic process
proline catabolic process
Cellular Component
cytosol
peroxisomal matrix
peroxisomal membrane
Function
binding
catalytic activity
oxidoreductase activity, acting on the ch-nh2 group of donors
oxidoreductase activity, acting on the ch-nh2 group of donors, oxygen as acceptor
d-amino-acid oxidase activity
oxidoreductase activity
Molecular Function
D-amino-acid oxidase activity
FAD binding
protein dimerization activity
Process
metabolic process
oxidation reduction
Cellular Location
  1. Peroxisome
Gene Properties
Chromosome Location 12
Locus 12q24
SNPs DAO
Gene Sequence
>1044 bp
ATGCGTGTGGTGGTGATTGGAGCAGGAGTCATCGGGCTGTCCACCGCCCTCTGCATCCAT
GAGCGCTACCACTCAGTCCTGCAGCCACTGCACATAAAGGTCTACGCGGACCGCTTCACC
CCACTCACCACCACCGACGTGGCTGCCGGCCTCTGGCAGCCCTACCTTTCTGACCCCAAC
AACCCACAGGAGGCGGACTGGAGCCAACAGACCTTTGACTATCTCCTGAGCCATGTCCAT
TCTCCCAACGCTGAAAACCTGGGCCTGTTCCTAATCTCGGGCTACAACCTCTTCCATGAA
GCCATTCCGGACCCTTCCTGGAAGGACACAGTTCTGGGATTTCGGAAGCTGACCCCCAGA
GAGCTGGATATGTTCCCAGATTACGGCTATGGCTGGTTCCACACAAGCCTAATTCTGGAG
GGAAAGAACTATCTACAGTGGCTGACTGAAAGGTTAACTGAGAGGGGAGTGAAGTTCTTC
CAGCGGAAAGTGGAGTCTTTTGAGGAGGTGGCAAGAGAAGGCGCAGACGTGATTGTCAAC
TGCACTGGGGTATGGGCTGGGGCGCTACAACGAGACCCCCTGCTGCAGCCAGGCCGGGGG
CAGATCATGAAGGTGGACGCCCCTTGGATGAAGCACTTCATTCTCACCCATGACCCAGAG
AGAGGCATCTACAATTCCCCGTACATCATCCCAGGGACCCAGACAGTTACTCTTGGAGGC
ATCTTCCAGTTGGGAAACTGGAGTGAACTAAACAATATCCAGGACCACAACACCATTTGG
GAAGGCTGCTGCAGACTGGAGCCCACACTGAAGAATGCAAGAATTATTGGTGAAGCAACT
GGCTTCCGGCCAGTACGCCCCCAGATTCGGCTAGAAAGAGAACAGCTTCGCACTGGACCT
TCAAACACAGAGGTCATCCACAACTATGGCCATGGAGGCTACGGGCTCACCATCCACTGG
GGATGTGCCCTGGAGGCAGCCAAGCTCTTTGGGAGAATCCTGGAAGAAAAGAAATTGTCC
AGAATGCCACCATCCCACCTCTGA
Protein Properties
Number of Residues 347
Molecular Weight 39473.75
Theoretical pI 6.844
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>D-amino-acid oxidase
MRVVVIGAGVIGLSTALCIHERYHSVLQPLDIKVYADRFTPLTTTDVAAGLWQPYLSDPN
NPQEADWSQQTFDYLLSHVHSPNAENLGLFLISGYNLFHEAIPDPSWKDTVLGFRKLTPR
ELDMFPDYGYGWFHTSLILEGKNYLQWLTERLTERGVKFFQRKVESFEEVAREGADVIVN
CTGVWAGALQRDPLLQPGRGQIMKVDAPWMKHFILTHDPERGIYNSPYIIPGTQTVTLGG
IFQLGNWSELNNIQDHNTIWEGCCRLEPTLKNARIIGERTGFRPVRPQIRLEREQLRTGP
SNTEVIHNYGHGGYGLTIHWGCALEAAKLFGRILEEKKLSRMPPSHL
GenBank ID Protein 30446
UniProtKB/Swiss-Prot ID P14920
UniProtKB/Swiss-Prot Entry Name OXDA_HUMAN
PDB IDs
GenBank Gene ID X13227
GeneCard ID DAO
GenAtlas ID DAO
HGNC ID HGNC:2671
References
General References
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  3. Momoi K, Fukui K, Watanabe F, Miyake Y: Molecular cloning and sequence analysis of cDNA encoding human kidney D-amino acid oxidase. FEBS Lett. 1988 Sep 26;238(1):180-4. [PubMed:2901986 ]
  4. Fukui K, Miyake Y: Molecular cloning and chromosomal localization of a human gene encoding D-amino-acid oxidase. J Biol Chem. 1992 Sep 15;267(26):18631-8. [PubMed:1356107 ]
  5. Kawazoe T, Tsuge H, Pilone MS, Fukui K: Crystal structure of human D-amino acid oxidase: context-dependent variability of the backbone conformation of the VAAGL hydrophobic stretch located at the si-face of the flavin ring. Protein Sci. 2006 Dec;15(12):2708-17. Epub 2006 Nov 6. [PubMed:17088322 ]
  6. Kawazoe T, Tsuge H, Imagawa T, Aki K, Kuramitsu S, Fukui K: Structural basis of D-DOPA oxidation by D-amino acid oxidase: alternative pathway for dopamine biosynthesis. Biochem Biophys Res Commun. 2007 Apr 6;355(2):385-91. Epub 2007 Feb 8. [PubMed:17303072 ]
  7. Sparey T, Abeywickrema P, Almond S, Brandon N, Byrne N, Campbell A, Hutson PH, Jacobson M, Jones B, Munshi S, Pascarella D, Pike A, Prasad GS, Sachs N, Sakatis M, Sardana V, Venkatraman S, Young MB: The discovery of fused pyrrole carboxylic acids as novel, potent D-amino acid oxidase (DAO) inhibitors. Bioorg Med Chem Lett. 2008 Jun 1;18(11):3386-91. doi: 10.1016/j.bmcl.2008.04.020. Epub 2008 Apr 13. [PubMed:18455394 ]