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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Temperature Stability
Temperature Stability on EC 1.4.3.3 - D-amino-acid oxidase
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15 - 40
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the response to D-serine increases with temperature, from 15 to 40°C, the sensitivity at 37°C is 75% higher than that at 25°C
25 - 50
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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, with a half-life of 60 h encapsulated DAO is 720fold more stable than the free enzyme under conditions of bubble aeration at 25°C, the soluble oxidase is stabilized by added FAD only at temperatures of 35°C or greater, at 50°C encapsulated preparations of the oxidase are much more stable than the free enzyme whose half-life is only 40 min
25 - 65
30
30 - 45
loss of secondary structure and inactivation occurs over a range of 30°C to 45°C, the melting temperature is at 41.4°C
30 - 50
does not lose activity at temperatures up to 30°C for at least 2 h and has a half-life of 21 min at 40°C and of 2 min at 50°C when it is incubated in 100 mM TEA-HCl buffer (pH 7.6)
30 - 60
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retains more than 80% of the maximal activity after incubation for 60 min at 30-60°C
30 - 64
50% of the initial enzymatic activity is lost after 1h at 64°C. The half-lives of the enzyme are 462 h at 30°C and 114 h at 50°C
35
35 - 45
when temperature exceeds 35°C, the recombinant enzyme dramatically loses ist activity after 15 min of incubation. When incubated over 45°C for 5 min, the enzyme maintains about 30 % residual activity
37 - 60
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retains more than 80% of the maximal activity after incubation for 60 min at 37-60°C
40
42
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50 h, pH 7.5, about 60% loss of activity of enzyme after multisubunit immobilization on highly activated glyoxyl agarose, protein concentration 0.067 mg/ml and 50 mM FAD, 95% loss of activity without FAD
45
50
52
54
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melting temperature of DELTAloop mutant in which 14 residues belonging to a loop connecting strands betaF5-beta-F6 have been deleted
55
55 - 70
soluble enzyme remains stable up to 55°C and retains more than 70% activity after 60 incubation, thermal stability up to 70°C is improved by chemical modification with soluble dextran
60
65
additional information
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thermal inactivation of D-amino acid oxidase from Trigonopsis variabilis occurs via three parallel paths of irreversible denaturation
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the activity profiles of soluble and immobilized DAOs at 25-65°C are similar, immobilized DAO exhibits a melting temperature of 60°C, which is 15°C higher than those for the soluble counterpart
25 - 65
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the activity profiles of soluble and immobilized DAOs at 25-65°C are similar, immobilized DAO exhibits a melting temperature of 60°C, which is 8°C higher than those for the soluble counterpart
after 30min incubation at 45°C, the activity is completely lost
30
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increasing the temperature to 30°C does not affect the specific activity but enhances the volumetric enzyme activity by 22% due to its effect on cell growth
35
stable up to 35°C, sharp decrease in activity at higher temperatures
40
30 min, wild-type holoenzym retains 60% of the initial activity, wild-type apoprotein retains 20% of the initial activity, mutant holoenzyme DELTASer308-Lys321 retains less than 5% of the initial activity
40
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50 h, pH 7.5, about 45% loss of activity of enzyme after multisubunit immobilization on highly activated glyoxyl agarose, protein concentration 0.0067 mg/ml
40
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50 h, pH 7.5, about 45% loss of activity of enzyme after multisubunit immobilization on highly activated glyoxyl agarose, protein concentration 0.2 mg/ml
40
stable up to 40°C, the enzyme has decreased stability at temperatures beyond and is completely inactivated at 65°C
45
fully stable up to 45°C (100% of residual activity after 30 min incubation)
50
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the native enzyme is inacivated after 1 h at 50°C whereas the immobilized enzyme (onto Ni2+-chelated NTA magnetic beads) retains 56% of the initial activity
50
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half-life time of native enzyme is 1.69 h, half-life time of oxidatively modified enzyme C106C108-(SO2H) is 0.85 h. Thermal inactivation of D-amino acid oxidase from Trigonopsis variabilis occurs via three parallel paths of irreversible denaturation. One main path leading to inactivation is FAD release, a process whose net rate is 25-fold lower in the oxidized form of TvDAO. Cofactor dissociation is kinetically coupled to aggregation and can be blocked completely by the addition of free FAD. Aggregation is markedly attenuated in the less stable Cys108-SO2H-containing enzyme. A third, however, slow process is the conversion of the native enzyme into the oxidized form
50
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inactivation of the enzyme at 50°C proceeds via two main pathways: partial loss of protein structure leading to a denatured holoenzyme, and reversible release of FAD cofactor generating inactive apoenzyme, mechanism, overview
55
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1 h, mutant enzyme F42C retains more than 70% of activity, wild-type enzyme retains only 10% activity