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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-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

Temperature Stability

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

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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 40
-
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
-
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 - 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
-
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
30 - 65
-
the half-life reaches 14.5 d at 30°C
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
-
retains more than 80% of the maximal activity after incubation for 60 min at 37-60°C
4
-
24 h, 50% loss of activity
42
-
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
46.1
mutant R120E, TM value, circular dichroism method
47.6
mutant R120L, TM value, circular dichroism method
48
-
melting temperature of dimeric wild-type enzyme
52.7
mutant R120E, TM value, protein fluoprescence method
53.1
wild-type, melting temperature, via protein fluorescence
54
-
melting temperature of DELTAloop mutant in which 14 residues belonging to a loop connecting strands betaF5-beta-F6 have been deleted
54.2
mutant R120L, TM value, protein fluoprescence method
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
57
wild-type, TM value, circular dichroism method
57.7
wild-type, TM value, protein fluoprescence method
58.8
wild-type, melting temperature, via circular dichroism
59.1
mutant G183R, melting temperature, via protein fluorescence
63.2
mutant G183R, melting temperature, via circular dichroism
70
-
dextran-conjugated enzyme is stable
additional information
-
thermal inactivation of D-amino acid oxidase from Trigonopsis variabilis occurs via three parallel paths of irreversible denaturation