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Literature summary extracted from

  • Pollegioni, L.; Sacchi, S.; Caldinelli, L.; Boselli, A.; Pilone, M.S.; Piubelli, L.; Molla, G.
    Engineering the properties of D-amino acid oxidases by a rational and a directed evolution approach (2007), Curr. Protein Pept. Sci., 8, 600-618.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.4.3.3 D242V/Q253R/D304V mutant with altered substrate specificity Rhodotorula toruloides
1.4.3.3 E220D/Y224G decreased catalytic activity for D-Ala compared to the wild type enzyme Sus scrofa
1.4.3.3 E222D/Y224G decreased catalytic activity for D-Ala compared to the wild type enzyme Sus scrofa
1.4.3.3 G281C inactive Homo sapiens
1.4.3.3 G313A decreased catalytic activity for D-Ala compared to the wild type enzyme Sus scrofa
1.4.3.3 H307L Kd for FAD is 28fold higher with respect to the wild type enzyme while activity is mostly retained Sus scrofa
1.4.3.3 H324L inactive Trigonopsis variabilis
1.4.3.3 H324N decreased activity Trigonopsis variabilis
1.4.3.3 H324Q decreased activity Trigonopsis variabilis
1.4.3.3 H324R inactive Trigonopsis variabilis
1.4.3.3 L118H mutant with altered substrate specificity Rhodotorula toruloides
1.4.3.3 M156L mutant shows increased H2O2 resistance Trigonopsis variabilis
1.4.3.3 M209L mutant shows increased H2O2 resistance Trigonopsis variabilis
1.4.3.3 Q144R mutant with altered substrate specificity Rhodotorula toruloides
1.4.3.3 R221D/Y224G decreased catalytic activity for D-Ala compared to the wild type enzyme Sus scrofa
1.4.3.3 Y223S strongly decreased turnover number Rhodotorula toruloides
1.4.3.3 Y228F 50% activity compared to the wild type enzyme, 120fold decreased reduction rate Sus scrofa
1.4.3.3 Y238F the mutation decreases the rate of product release und to a lesser extend the rate of substrate binding and does not alter significantly the substrate specificity of the enzyme Rhodotorula toruloides
1.4.3.3 Y238S the mutation decreases the rate of product release und to a lesser extend the rate of substrate binding and does not alter significantly the substrate specificity of the enzyme Rhodotorula toruloides

General Stability

EC Number General Stability Organism
1.4.3.3 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 Trigonopsis variabilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.3.3 benzoate
-
Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.3.3 0.15
-
O2 at pH 8.3 and 25°C Sus scrofa
1.4.3.3 0.8
-
O2 at pH 8.3 and 25°C Trigonopsis variabilis
1.4.3.3 1.2
-
O2 at pH 8.3 and 25°C Homo sapiens
1.4.3.3 2
-
D-alanine at pH 8.3 and 25°C Sus scrofa
1.4.3.3 2.3
-
O2 at pH 8.3 and 25°C Rhodotorula toruloides
1.4.3.3 2.6
-
D-alanine at pH 8.3 and 25°C Rhodotorula toruloides
1.4.3.3 4.5
-
D-alanine at pH 8.3 and 25°C Trigonopsis variabilis
1.4.3.3 8.8
-
D-alanine at pH 8.3 and 25°C Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.4.3.3 peroxisome
-
Trigonopsis variabilis 5777
-
1.4.3.3 peroxisome
-
Rhodotorula toruloides 5777
-
1.4.3.3 peroxisome
-
Sus scrofa 5777
-
1.4.3.3 peroxisome
-
Homo sapiens 5777
-

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 40000
-
2 * 40000, SDS-PAGE Homo sapiens
1.4.3.3 80000
-
SDS-PAGE Rhodotorula toruloides
1.4.3.3 80000
-
SDS-PAGE Sus scrofa
1.4.3.3 80000
-
SDS-PAGE Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.3 Homo sapiens P14920
-
-
1.4.3.3 Rhodotorula toruloides P80324
-
-
1.4.3.3 Sus scrofa P00371
-
-
1.4.3.3 Trigonopsis variabilis Q99042
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.4.3.3 kidney
-
Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.3 cephalosporin C + H2O + O2
-
Trigonopsis variabilis 7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
?
1.4.3.3 cephalosporin C + H2O + O2
-
Rhodotorula toruloides 7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
?
1.4.3.3 cephalosporin C + H2O + O2
-
Sus scrofa 7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
?
1.4.3.3 cephalosporin C + H2O + O2
-
Homo sapiens 7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
?
1.4.3.3 D-alanine + H2O + O2
-
Trigonopsis variabilis pyruvate + NH3 + H2O2
-
?
1.4.3.3 D-alanine + H2O + O2
-
Rhodotorula toruloides pyruvate + NH3 + H2O2
-
?
1.4.3.3 D-alanine + H2O + O2
-
Sus scrofa pyruvate + NH3 + H2O2
-
?
1.4.3.3 D-alanine + H2O + O2
-
Homo sapiens pyruvate + NH3 + H2O2
-
?
1.4.3.3 D-methionine + H2O + O2 by far best substrate Trigonopsis variabilis 4-methylthio-2-oxobutanoic acid + NH3 + H2O2
-
?
1.4.3.3 D-proline + H2O + O2 best substrate Sus scrofa 2-oxopentanoate + NH3 + H2O2
-
?
1.4.3.3 D-valine + H2O + O2 best substrate Rhodotorula toruloides alpha-ketoisovaleric acid + NH3 + H2O2
-
?
1.4.3.3 additional information best substrate is by far D-methionine followed by D-phenylalanine, D-tryptophan, D-valin, and D-alanine Trigonopsis variabilis ?
-
?
1.4.3.3 additional information best substrate is D-valine followed by D-tryptophan, D-phenylalanine, D-alanine, and D-cysteine Rhodotorula toruloides ?
-
?
1.4.3.3 additional information D-aspartate and D-glutamate are no substrates Trigonopsis variabilis ?
-
?
1.4.3.3 additional information D-aspartate and D-glutamate are no substrates Rhodotorula toruloides ?
-
?
1.4.3.3 additional information D-aspartate and D-glutamate are no substrates Sus scrofa ?
-
?
1.4.3.3 additional information D-aspartate and D-glutamate are no substrates Homo sapiens ?
-
?
1.4.3.3 additional information D-proline is the best substrate followed by D-methionine, D-alanine, D-norleucine, D-isoleucine, and D-phenylalanine Sus scrofa ?
-
?

Subunits

EC Number Subunits Comment Organism
1.4.3.3 homodimer 2 * 40000, SDS-PAGE Rhodotorula toruloides
1.4.3.3 homodimer 2 * 40000, SDS-PAGE Homo sapiens
1.4.3.3 homodimer x-ray crystallography Sus scrofa

Synonyms

EC Number Synonyms Comment Organism
1.4.3.3 D-amino acid oxidase
-
Trigonopsis variabilis
1.4.3.3 D-amino acid oxidase
-
Rhodotorula toruloides
1.4.3.3 D-amino acid oxidase
-
Sus scrofa
1.4.3.3 D-amino acid oxidase
-
Homo sapiens
1.4.3.3 DAAO
-
Trigonopsis variabilis
1.4.3.3 DAAO
-
Rhodotorula toruloides
1.4.3.3 DAAO
-
Sus scrofa
1.4.3.3 DAAO
-
Homo sapiens

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.4.3.3 35
-
stable up to 35°C, sharp decrease in activity at higher temperatures Rhodotorula toruloides
1.4.3.3 40
-
stable up to 40°C, the enzyme has decreased stability at temperatures beyond and is completely inactivated at 65°C Trigonopsis variabilis
1.4.3.3 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 Sus scrofa

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.4.3.3 10
-
D-alanine at pH 8.3 and 25°C Sus scrofa
1.4.3.3 14.7
-
D-alanine at pH 8.3 and 25°C Homo sapiens
1.4.3.3 53
-
D-alanine at pH 8.3 and 25°C Trigonopsis variabilis
1.4.3.3 350
-
D-alanine at pH 8.3 and 25°C Rhodotorula toruloides

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.4.3.3 6 8.2
-
Rhodotorula toruloides

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.3.3 FAD dependent Trigonopsis variabilis
1.4.3.3 FAD dependent Rhodotorula toruloides
1.4.3.3 FAD dependent Sus scrofa
1.4.3.3 FAD dependent Homo sapiens