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Gene Review

DAO1  -  D-amino acid oxidase

Sus scrofa

Synonyms: DAAO, DAMOX, DAO
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Disease relevance of DAO1

  • Expression conditions in Escherichia coli of wild-type, Y224F, and Y228F mutants of pig kidney D-amino acid oxidase (DAAO) have been changed to yield more enzyme [1].
  • In chick dorsal root ganglion explant cultures, purified porcine DAO induced neurite outgrowth in the low nanomolar range [2].
  • The behavior of this enzyme toward halogeno substrates is therefore similar to that of baker's yeast L-lactate dehydrogenase and in part different from that of Mycobacterium smegmatis lactate oxidase and porcine kidney D-amino-acid oxidase [3].
  • The activity of HMT decreased linearly with time from the onset of the Arthus reaction, reaching about 20% of the control activity at 48 h; the activity of DAO decreased even from the early stages of the reaction, and this decrease continued throughout first 48 h of the reaction [4].
  • The activities of two histamine-metabolizing enzymes, histamine-N-methyltransferase (HMT) and diamine oxidase (DAO), were examined in various types of experimentally induced cutaneous inflammations in guinea pigs [4].

High impact information on DAO1

  • Saturation of binding sites with 5,000 U of DAO/ml resulted in levels of bound activity (up to 11-13 U/mg of endothelial cells) in excess of that observed in all tissues except placenta [5].
  • The demonstration of DAO binding to vascular endothelial cells provides a further example of the ability of these cells to bind enzymes at their surface and thereby act on biologically active substances in the circulation [5].
  • Both enzymes, however, were displaced by heparin (0.05-5 U/ml) and DAO binding was impaired by prior treatment of cells with proteolytic and glycosaminoglycandegrading enzymes [5].
  • As part of an effort to understand how proteins are imported into the peroxisome, we have sought to identify the peroxisomal targeting signals in four unrelated peroxisomal proteins: human catalase, rat hydratase:dehydrogenase, pig D-amino acid oxidase, and rat acyl-CoA oxidase [6].
  • Comparison of the properties of these two mutant enzyme forms with those of the wild-type DAAO indicate that both tyrosine residues have their main function in the reductive half-reaction of the enzyme [1].

Chemical compound and disease context of DAO1

  • The X-ray crystallographic structure of porcine kidney D-amino acid oxidase, which had been expressed in Escherichia coli transformed with a vector containing DAO cDNA, was determined by the isomorphous replacement method for the complex form with benzoate [7].

Biological context of DAO1


Anatomical context of DAO1


Associations of DAO1 with chemical compounds


Analytical, diagnostic and therapeutic context of DAO1


  1. Studies on the kinetic mechanism of pig kidney D-amino acid oxidase by site-directed mutagenesis of tyrosine 224 and tyrosine 228. Pollegioni, L., Fukui, K., Massey, V. J. Biol. Chem. (1994) [Pubmed]
  2. Diamine oxidase induces neurite outgrowth in chick dorsal root ganglia by a nonenzymatic mechanism. Munis, J.R., Steiner, J.T., Ruat, M., Snyder, S.H. J. Neurochem. (1998) [Pubmed]
  3. Rat kidney L-2-hydroxyacid oxidase. Structural and mechanistic comparison with flavocytochrome b2 from baker's yeast. Urban, P., Chirat, I., Lederer, F. Biochemistry (1988) [Pubmed]
  4. Impaired histamine metabolism in the Arthus reaction induced in guinea-pig skin. Imamura, S., Tachibana, T., Taniguchi, S. Arch. Dermatol. Res. (1985) [Pubmed]
  5. Binding of diamine oxidase activity to rat and guinea pig microvascular endothelial cells. Comparisons with lipoprotein lipase binding. Robinson-White, A., Baylin, S.B., Olivecrona, T., Beaven, M.A. J. Clin. Invest. (1985) [Pubmed]
  6. Identification of peroxisomal targeting signals located at the carboxy terminus of four peroxisomal proteins. Gould, S.J., Keller, G.A., Subramani, S. J. Cell Biol. (1988) [Pubmed]
  7. Three-dimensional structure of porcine kidney D-amino acid oxidase at 3.0 A resolution. Mizutani, H., Miyahara, I., Hirotsu, K., Nishina, Y., Shiga, K., Setoyama, C., Miura, R. J. Biochem. (1996) [Pubmed]
  8. Molecular cloning and sequence analysis of cDNAs encoding porcine kidney D-amino acid oxidase. Fukui, K., Watanabe, F., Shibata, T., Miyake, Y. Biochemistry (1987) [Pubmed]
  9. The kinetic mechanism of D-amino acid oxidase with D-alpha-aminobutyrate as substrate. Effect of enzyme concentration on the kinetics. Fitzpatrick, P.F., Massey, V. J. Biol. Chem. (1982) [Pubmed]
  10. Methylation of the active center histidine 217 in D-amino acid oxidase by methyl-p-nitrobenzenesulfonate. Swenson, R.P., Williams, C.H., Massey, V. J. Biol. Chem. (1984) [Pubmed]
  11. The primary structure of D-amino acid oxidase from pig kidney. I. Isolation and sequence of the tryptic peptides. Swenson, R.P., Williams, C.H., Massey, V., Ronchi, S., Minchiotti, L., Galliano, M., Curti, B. J. Biol. Chem. (1982) [Pubmed]
  12. Biosynthesis of porcine kidney D-amino acid oxidase. Fukui, K., Momoi, K., Watanabe, F., Miyake, Y. Biochem. Biophys. Res. Commun. (1986) [Pubmed]
  13. Histamine inactivation in the colon of pigs in relationship to abundance of catabolic enzymes. Aschenbach, J.R., Schwelberger, H.G., Ahrens, F., Fürll, B., Gäbel, G. Scand. J. Gastroenterol. (2006) [Pubmed]
  14. Thermodynamic control of D-amino acid oxidase by benzoate binding. Van den Berghe-Snorek, S., Stankovich, M.T. J. Biol. Chem. (1985) [Pubmed]
  15. 8-Azidoflavins as photoaffinity labels for flavoproteins. Fitzpatrick, P.F., Ghisla, S., Massey, V. J. Biol. Chem. (1985) [Pubmed]
  16. The reaction of 8-mercaptoflavins and flavoproteins with sulfite. Evidence for the role of an active site arginine in D-amino acid oxidase. Fitzpatrick, P.F., Massey, V. J. Biol. Chem. (1983) [Pubmed]
  17. Identification of the histidine residue in D-amino acid oxidase that is covalently modified during inactivation by 5-dimethylaminonaphthalene-1-sulfonyl chloride. Swenson, R.P., Williams, C.H., Massey, V. J. Biol. Chem. (1983) [Pubmed]
  18. Effect of pH on the interaction of benzoate and D-amino acid oxidase. Quay, S., Massey, V. Biochemistry (1977) [Pubmed]
  19. Limited proteolysis and X-ray crystallography reveal the origin of substrate specificity and of the rate-limiting product release during oxidation of D-amino acids catalyzed by mammalian D-amino acid oxidase. Vanoni, M.A., Cosma, A., Mazzeo, D., Mattevi, A., Todone, F., Curti, B. Biochemistry (1997) [Pubmed]
  20. Identification of methionine-110 as the residue covalently modified in the electrophilic inactivation of D-amino-acid oxidase by O-(2,4-dinitrophenyl) hydroxylamine. D'Silva, C., Williams, C.H., Massey, V. Biochemistry (1987) [Pubmed]
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