Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli strain BL21 | Rhodotorula toruloides |
expressed in Escherichia coli strain BL21 | Trigonopsis variabilis |
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 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 | UniProt | Comment | Textmining |
---|---|---|---|
Rhodotorula toruloides | - |
- |
- |
Trigonopsis variabilis | - |
- |
- |
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 (Comment) | Organism |
---|---|
His-Bind column chromatography | Rhodotorula toruloides |
His-Bind column chromatography | Trigonopsis variabilis |
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 | 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 | 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 | 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 Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | - |
free enzyme | Rhodotorula toruloides |
55 | - |
immobilized enzyme | Rhodotorula toruloides |
55 | - |
immobilized and soluble enzyme | Trigonopsis variabilis |
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 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 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 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 | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Rhodotorula toruloides | |
FAD | - |
Trigonopsis variabilis |