1.4.3.3: D-amino-acid oxidase
This is an abbreviated version!
For detailed information about D-amino-acid oxidase, go to the full flat file.
Word Map on EC 1.4.3.3
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1.4.3.3
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d-serine
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schizophrenia
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peroxisomal
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flavin
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n-methyl-d-aspartate
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d-alanine
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catalase
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fad
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nmda
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deamination
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benzoate
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flavoenzyme
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flavoproteins
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racemase
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variabilis
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l-amino
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neurotransmission
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d-aspartate
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gracilis
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co-agonist
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rhodotorula
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cephalosporin
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glutamatergic
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urate
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d-proline
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d-ala
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d-ser
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imino
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antipsychotic
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hypofunction
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d-methionine
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isoalloxazine
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acylase
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fad-containing
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toruloides
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rhodosporidium
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d-glutamate
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fad-dependent
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d-cysteine
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kynurenic
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sulfurtransferase
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d-valine
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synthesis
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medicine
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d-leucine
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cerium
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7-aminocephalosporanic
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d-tryptophan
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d-phenylalanine
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neuregulin
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3-mercaptopyruvate
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sarcosine
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industry
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biotechnology
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analysis
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diagnostics
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drug development
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pharmacology
- 1.4.3.3
- d-serine
-
schizophrenia
- peroxisomal
- flavin
- n-methyl-d-aspartate
- d-alanine
- catalase
- fad
- nmda
-
deamination
- benzoate
-
flavoenzyme
- flavoproteins
- racemase
- variabilis
-
l-amino
-
neurotransmission
- d-aspartate
- gracilis
-
co-agonist
- rhodotorula
- cephalosporin
-
glutamatergic
- urate
- d-proline
- d-ala
- d-ser
-
imino
-
antipsychotic
-
hypofunction
- d-methionine
- isoalloxazine
- acylase
-
fad-containing
- toruloides
- rhodosporidium
- d-glutamate
-
fad-dependent
- d-cysteine
-
kynurenic
- sulfurtransferase
- d-valine
- synthesis
- medicine
- d-leucine
- cerium
-
7-aminocephalosporanic
- d-tryptophan
- d-phenylalanine
- neuregulin
- 3-mercaptopyruvate
- sarcosine
- industry
- biotechnology
- analysis
- diagnostics
- drug development
- pharmacology
Reaction
Synonyms
chDAO, D-AAO, D-amino acid oxidase, D-amino-acid-oxidase, D-aminoacid oxidase, DAAO, DAMOX, DAO, DAO1, DaoE, hDAAO, ophio-amino-acid oxidase, oxidase, D-amino acid, PEG-DAO, pkDAAO, RgDAAO, TvDAAO, TvDAO, LH99
ECTree
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Cofactor
Cofactor on EC 1.4.3.3 - D-amino-acid oxidase
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FAD
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FAD
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FAD
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FAD
mutant enzyme DELTASer308-Lys321 retains the binding of the FAD coenzyme, binding of mutant apoenzyme is weaker than that of wild-type apoenzyme to FAD
FAD
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human enzyme weakly binds FAD and shows a significantly slower rate of flavin reduction compared to porcine enzyme
FAD
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the enzyme contains one molecule of non-covalently bound FAD per protein monomer, which can be easily isolated from the apoprotein by dialysis in the presence of 1 M KBr
FAD
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added FAD does not stabilize DAO at and below 35°C, but it contributes up to 3.6fold extra stability to the enzyme activity at temperatures higher than 35°C
FAD
contains one molecule of noncovalently bound FAD per subunit
FAD
contains one molecule of noncovalently bound FAD per subunit
FAD
contains one molecule of noncovalently bound FAD per subunit
FAD
contains one molecule of noncovalently bound FAD per subunit
FAD
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dependent, dissociation of FAD is a main contributor to the loss of activity
FAD
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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
FAD
the apoprotein form of hDAAO binds the substrate D-serine, this interaction increases FAD binding thus increasing the amount of active holoenzyme in solution, binding analysis of FAD, overview
FAD
Kd value 0.008 mM for FAD-apoprotein complex. Benzoate binding favors a protein conformation with a higher affinity for the cofactor FAD
FAD
R120E and R120L variants show absorbance maxima at 448, 384, and 279 nm and an Abs279nm/Abs448nm ratio of 10.4 and 11.2, respectively, which are close to the value of 10.6 reported for the wild-type enzyme
flavin
the mutant enzyme M213R has a more polar microenvironment surrounding the flavin coenzyme