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

Reaction

a D-amino acid
+
H2O
+
O2
=
a 2-oxo carboxylate
+
NH3
+
H2O2

Synonyms

chDAO, D-AAO, D-amino acid oxidase, D-amino acid oxidases, 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

     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.3 With oxygen as acceptor
                1.4.3.3 D-amino-acid oxidase

General Stability

General Stability on EC 1.4.3.3 - D-amino-acid oxidase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol stabilizes
benzoic acid stabilizes
-
carrier-free enzyme is entrapped in semipermeable microcapsules produced from the polycation poly(methylene-co-guanidine) in combination with CaCl2 and the polyanions alginate and cellulose sulfate, the effectiveness of the entrapped oxidase for O2-dependent conversion of D-methionine at 25°C is 75-95% of the free enzyme preparation
-
cetylpyridinium bromide stabilizes
-
changes in ionic strength, I: 16-82 mM, have only moderate effect on enzyme stability, stability maximum is 50 mM
-
chymotrypsin, 10% w/w, no effect
-
covalent modification of DAO using maleimide-activated PEG5000 yields a stable bionconjugate in which three exposed cysteine side chains are derivatized, the PEGylated enzyme shows approximately 3.3fold slowed dissociation of the FAD cofactor at 50°C, and this causes a 2fold thermostabilization of the enzyme activity
-
D-amino acid oxidase fused to an elastin-like polypeptide exhibits enzymatic activity that is about 1.6times that of the free enzyme and shows higher stability
-
DAAO immobilized on a macro-porous carrier is higher in water-insoluble organic solvents than in water-soluble ones
-
enzyme immobilized on Amberzyme oxirane resin can be recycled more than 14 times without significant loss of activity
-
glycerol, 10%, stabilizes
-
glycerol, 50% stabilizes
-
good stability to urea denaturation
-
His-tagged DAAO loses its flavin cofactor upon dilution or prolonged dialysis against FAD-free solvents leading to the catalytic inactivation
-
homodimer is stable even in the apoprotein form
-
immobilisation on PEI 25 kDa Sepabeads and treatment with 0.5% glutaraldehyde solution at pH 7-8 and 25°C for 16 h leads to 160fold increased enzyme stability
-
incubation of the mutant enzyme DELTASer308-Lys321 with 10% trypsin in presence of exogenous FAD, 0.2 mM, shows that the rate of activity loss is lower than that determined in absence of exogenous FAD
-
m-toluic acid stabilizes
-
multisubunit immobilization on highly activated glyoxyl agarose improves stability of the enzyme 1500fold, at a protein concentration of 0.0067 mg/ml.
-
multisubunit immobilization on highly activated glyoxyl agarose marginally improves stability of the enzyme, 15-20fold, at a protein concentration of 0.0067 mg/ml. Dissociation of FAD is not prevented by immobilization
-
oriented immobilization of a chimeric oxidase maintains 80% of the original activity in microparticle-bound enzymes. Mildly permeabilized cells in which N-terminally tagged TvDAO in which a 12-amino-acid peptide is fused in frame to the N-terminus (TvDAOstrepN) is physically entrapped are employed for the batchwise conversion of D-Ala in an aerated enzyme reactor. The cells could be reused for at least three rounds of reaction with only small losses of activity. The free enzyme, however, is rapidly inactivated under the same reaction conditions (half-life: 1.2 h)
-
stabilization of the enzyme by immobilization onto Fe3O4 magnetic nanoparticles, after immobilization the Tm increases from 45°C of the free form to 55°C. In the presence of 20 mM H2O2, the immobilized form retains 93% of its activity after 5 h while the free form is completely inactivated after 3.5 h
-
stable homodimer even in the apoprotein form
-
stable to guanidine
-
the catalytic efficiency of immobilized DAO (onto streptavidin-coated magnetic beads through the interaction between biotin and streptavidin) toward D-alanine is decreased by 56%
the half-life of the enzyme can be up to 15.5 days by treating the cetyltrimethylammonium bromide-permeabilized cells with 1% (w/v) glutaraldehyde
-
the midpoint contration of urea required for unfolding is 1.4-1.8 M for wild-type enzyme and 0.8-1.1 M for mutant enzyme W243Y
-
the surfactant Pluronic F-68 stabilizes immobilized DAO by protecting the enzyme from the deleterious effect of gas-liquid interfaces
-
trypsin, 10% w/w, inactivation and proteolysis under nondenaturing conditions
-