Cloned (Comment) | Organism |
---|---|
recombinant enzyme expression in Escherichia coli | Homo sapiens |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
40000 | - |
2 * 40000, stable homodimer even in the apoprotein form | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Homo sapiens | DAAO is a catabolic flavoenzyme that catalyzes the oxidative deamination of D-amino acids to the corresponding a-keto acids, hydrogen peroxide, and ammonia. DAAO is strictly specific for D-isomers of amino acids | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
flavoprotein | - |
Homo sapiens |
Purification (Comment) | Organism |
---|---|
recombinant enzyme from Escherichia coli | Homo sapiens |
Renatured (Comment) | Organism |
---|---|
holo- and apoprotein samples of hDAAO are incubated for 60 min at 15°C in a buffer containing different concentrations of urea, 0-6 M, and then refolded by 10fold dilution in 50 mM sodium diphosphate, pH 8.0, 5% glycerol and 15°C, in the presence of a 10fold molar excess of FAD. Chemical denaturation of hDAAO holoenzyme is partially reversible, 50% of the initial activity is recovered starting with the refolding from 4 M urea-denatured holoprotein, while the refolding of apoprotein is largely irreversible even at 2 M urea , 15-20% of recovery of enzymatic activity versus 90-100% for the holoenzyme and even in the presence of the cofactor | Homo sapiens |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
brain | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | DAAO is a catabolic flavoenzyme that catalyzes the oxidative deamination of D-amino acids to the corresponding a-keto acids, hydrogen peroxide, and ammonia. DAAO is strictly specific for D-isomers of amino acids | Homo sapiens | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | 2 * 40000, stable homodimer even in the apoprotein form | Homo sapiens |
More | hDAAO exists as an equilibrium of holo- and apoprotein forms in solution | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
DAAO | - |
Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | flavoenzyme, weak interaction with the flavin cofactor in the free form,the cofactor binding is significantly tighter in the presence of an active site ligand. hDAAO exists as an equilibrium of holo- and apoprotein forms in solution | Homo sapiens |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Homo sapiens | the apoprotein gives a single band whose pI of 6.3 is very close to the theoretical value of 6.36, the holoenzyme yields three bands at pI 6.3, 5.9, and 5.4 | 6.3 | 5.4 |
General Information | Comment | Organism |
---|---|---|
physiological function | DAAO is involved in the degradation of the gliotransmitter D-serine, an important modulator of NMDA-receptor-mediated neurotransmission. An increase in DAAO activity, yielding a decrease in D-serine concentration, is among the molecular mechanisms leading to the onset of schizophrenia susceptibility, overview | Homo sapiens |