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Literature summary extracted from

  • Kuan, I.; Liao, R.; Hsieh, H.; Chen, K.; Yu, C.
    Properties of Rhodotorula gracilis D-amino acid oxidase immobilized on magnetic beads through His-tag (2008), J. Biosci. Bioeng., 105, 110-115.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.4.3.3 expressed in Escherichia coli BL21(DE3) cells Rhodotorula toruloides

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.3.3 0.9
-
 D-alanine free enzyme, in 100 mM potassium phosphate buffer at pH 8.0 and 25°C Rhodotorula toruloides
1.4.3.3 1.6
-
 D-alanine immobilized enzyme, in 100 mM potassium phosphate buffer at pH 8.0 and 25°C Rhodotorula toruloides

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.3.3 40000
-
 2 * 40000, SDS-PAGE Rhodotorula toruloides
1.4.3.3 80000
-
 SDS-PAGE Rhodotorula toruloides

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.3 Rhodotorula toruloides
-
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
1.4.3.3 the immobilized enzyme (onto Ni2+-chelated NTA magnetic beads) does not show any loss of activity in the presence of 10 mM H2O2 after 2 h incubation which is observed in case of free enzyme, the residual activity of the immoblized enzyme after 9 h is 72% compared with 22% of the free enzyme Rhodotorula toruloides

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.3.3 His-Bind column chromatography Rhodotorula toruloides

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Storage Stability

EC Number Storage Stability Organism
1.4.3.3 22°C, free enzyme, 10 days, 20% residual activity Rhodotorula toruloides
1.4.3.3 22°C, immobilized enzyme, 10 days, 74% residual activity Rhodotorula toruloides

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
1.4.3.3 homodimer 2 * 40000, SDS-PAGE Rhodotorula toruloides

Synonyms

EC Number Synonyms Comment Organism
1.4.3.3 D-amino acid oxidase
-
 Rhodotorula toruloides
1.4.3.3 DAO
-
 Rhodotorula toruloides

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.4.3.3 50
-
 free and immobilized enzymes Rhodotorula toruloides

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.4.3.3 50
-
 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 Rhodotorula toruloides

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.4.3.3 23.3
-
 D-alanine immobilized enzyme, in 100 mM potassium phosphate buffer at pH 8.0 and 25°C Rhodotorula toruloides
1.4.3.3 52.4
-
 D-alanine free enzyme, in 100 mM potassium phosphate buffer at pH 8.0 and 25°C Rhodotorula toruloides

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.3.3 8
-
 free enzyme Rhodotorula toruloides
1.4.3.3 9
-
 immobilized enzyme Rhodotorula toruloides

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.4.3.3 8 9 at pH 8 immobilized enzyme (onto Ni2+-chelated NTA magnetic beads) activity decreases to 44% while the free enzyme showed optimal activity, the activities of both enzyme forms decay similarily at pH values above 9, the free enzyme activity is less affected for pH values below 9 than the immobilized enzyme Rhodotorula toruloides

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.3.3 FAD
-
 Rhodotorula toruloides