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Literature summary for 1.4.3.3 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

Protein Variants Comment Organism
D242V/Q253R/D304V mutant with altered substrate specificity Rhodotorula toruloides
E220D/Y224G decreased catalytic activity for D-Ala compared to the wild type enzyme Sus scrofa
E222D/Y224G decreased catalytic activity for D-Ala compared to the wild type enzyme Sus scrofa
G281C inactive Homo sapiens
G313A decreased catalytic activity for D-Ala compared to the wild type enzyme Sus scrofa
H307L Kd for FAD is 28fold higher with respect to the wild type enzyme while activity is mostly retained Sus scrofa
H324L inactive Trigonopsis variabilis
H324N decreased activity Trigonopsis variabilis
H324Q decreased activity Trigonopsis variabilis
H324R inactive Trigonopsis variabilis
L118H mutant with altered substrate specificity Rhodotorula toruloides
M156L mutant shows increased H2O2 resistance Trigonopsis variabilis
M209L mutant shows increased H2O2 resistance Trigonopsis variabilis
Q144R mutant with altered substrate specificity Rhodotorula toruloides
R221D/Y224G decreased catalytic activity for D-Ala compared to the wild type enzyme Sus scrofa
Y223S strongly decreased turnover number Rhodotorula toruloides
Y228F 50% activity compared to the wild type enzyme, 120fold decreased reduction rate Sus scrofa
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
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

General Stability Organism
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

Inhibitors Comment Organism Structure
benzoate
-
Sus scrofa

KM Value [mM]

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

Localization

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
2 * 40000, SDS-PAGE Rhodotorula toruloides
40000
-
2 * 40000, SDS-PAGE Homo sapiens
80000
-
SDS-PAGE Rhodotorula toruloides
80000
-
SDS-PAGE Sus scrofa
80000
-
SDS-PAGE Homo sapiens

Organism

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

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
Sus scrofa
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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

Temperature Stability [°C]

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

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

pH Stability

pH Stability pH Stability Maximum Comment Organism
6 8.2
-
Rhodotorula toruloides

Cofactor

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