Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.4.3.3 extracted from

  • Wang, S.J.; Yu, C.Y.; Kuan, I.C.
    Stabilization of native and double D-amino acid oxidases from Rhodosporidium toruloides and Trigonopsis variabilis by immobilization on streptavidin-coated magnetic beads (2008), Biotechnol. Lett., 30, 1973-1981.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli strain BL21 Rhodotorula toruloides
expressed in Escherichia coli strain BL21 Trigonopsis variabilis

General Stability

General Stability Organism
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% Rhodotorula toruloides
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% Trigonopsis variabilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2
-
D-alanine free enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C Rhodotorula toruloides
2
-
D-alanine immobilized enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C Rhodotorula toruloides
3
-
D-alanine free enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C Trigonopsis variabilis
4
-
D-alanine immobilized enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C Trigonopsis variabilis
5
-
cephalosporin C immobilized enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C Rhodotorula toruloides
6
-
cephalosporin C free enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C Rhodotorula toruloides
6
-
cephalosporin C immobilized enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C Trigonopsis variabilis
9
-
cephalosporin C free enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C Trigonopsis variabilis

Organism

Organism UniProt Comment Textmining
Rhodotorula toruloides
-
-
-
Trigonopsis variabilis
-
-
-

Oxidation Stability

Oxidation Stability Organism
in the presence of 10 mM H2O2, immobilized DAO exhibits a half-life of about 3 h giving 6fold greater stability than the soluble form Trigonopsis variabilis
in the presence of 10 mM H2O2, immobilized DAO exhibits a half-life of about 8 h giving 16fold greater stability than the soluble form Rhodotorula toruloides

Purification (Commentary)

Purification (Comment) Organism
His-Bind column chromatography Rhodotorula toruloides
His-Bind column chromatography Trigonopsis variabilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
59
-
immobilized enzyme, at 25°C Rhodotorula toruloides
61
-
immobilized enzyme, at 25°C Trigonopsis variabilis

Storage Stability

Storage Stability Organism
25°C, free enzyme, 14 days, 50% loss of activity Rhodotorula toruloides
25°C, immobilized enzyme, 18 days, 50% loss of activity Rhodotorula toruloides
4°C, immobilized enzyme, 1 month, 10% loss of activity Rhodotorula toruloides
4°C, immobilized enzyme, 1 month, 10% loss of activity Trigonopsis variabilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cephalosporin C + H2O + O2
-
Rhodotorula toruloides 7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
?
cephalosporin C + H2O + O2
-
Trigonopsis variabilis 7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
?
D-alanine + H2O + O2
-
Rhodotorula toruloides pyruvate + NH3 + H2O2
-
?
D-alanine + H2O + O2
-
Trigonopsis variabilis pyruvate + NH3 + H2O2
-
?

Synonyms

Synonyms Comment Organism
D-amino acid oxidase
-
Rhodotorula toruloides
D-amino acid oxidase
-
Trigonopsis variabilis
DAO
-
Rhodotorula toruloides
DAO
-
Trigonopsis variabilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
free enzyme Rhodotorula toruloides
55
-
immobilized enzyme Rhodotorula toruloides
55
-
immobilized and soluble enzyme Trigonopsis variabilis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25 65 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 Rhodotorula toruloides
25 65 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 Trigonopsis variabilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3 6 cephalosporin C immobilized enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C Trigonopsis variabilis
44
-
D-alanine immobilized enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C Trigonopsis variabilis
51
-
D-alanine immobilized enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C Rhodotorula toruloides
55
-
cephalosporin C free enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C Trigonopsis variabilis
57
-
cephalosporin C immobilized enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C Rhodotorula toruloides
60
-
D-alanine free enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C Rhodotorula toruloides
70
-
cephalosporin C free enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C Rhodotorula toruloides
74
-
D-alanine free enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C Trigonopsis variabilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
immobilized and soluble enzyme Rhodotorula toruloides
8.5
-
immobilized and soluble enzyme Trigonopsis variabilis

pH Stability

pH Stability pH Stability Maximum Comment Organism
4 11 at pH 4, about 40% of the maximal activity is observed for the immobilized DAO while no activity is detected for the soluble enzyme, at pH 11 immobilized DAO has 65% of the maximal activity, whereas the soluble DAOs retains only 39% of the maximal activity Rhodotorula toruloides
4 11 at pH 4, about 40% of the maximal activity is observed for the immobilized DAO while no activity is detected for the soluble enzyme, at pH 11 immobilized DAO has 75% of the maximal activity, whereas the soluble DAOs retains only 13% of the maximal activity Trigonopsis variabilis

Cofactor

Cofactor Comment Organism Structure
FAD
-
Rhodotorula toruloides
FAD
-
Trigonopsis variabilis