BRENDA - Enzyme Database
show all sequences of 1.4.3.3

D-amino acid oxidase: physiological role and applications

Khoronenkova, S.V.; Tishkov, V.I.; Biochemistry (Moscow) 73, 1511-1518 (2008)

Data extracted from this reference:

Application
Application
Commentary
Organism
analysis
the enzyme is useful as a model FAD-containing protein
Sus scrofa
medicine
the purified recombinant or native enzyme is used in therapeutic treatment of cancer combined with injection of D-proline. The enzyme is a target in the development of medical treatment for neurodegeneration and cancer
Homo sapiens
synthesis
the enzyme is used to produce phenyl pyruvate from D-phenylalanine with the yield of 99%
Rhodotorula toruloides
synthesis
pig kidney enzyme is used to make L-pipecolic acid from a racemic mixture via D-isomer oxidation
Sus scrofa
synthesis
the enzyme is used to develop biocatalysts for the production of 7-aminocephalosporanic acid from the natural antibiotic cephalosporin C, and to produce optically active L-methionine from D-amino acid with the yield of 100% in a cascade system of four enzymes, or to produce phenyl pyruvate from D-phenylalanine with the yield of 99%
Trigonopsis variabilis
Cloned(Commentary)
Cloned (Commentary)
Organism
recombinant enzyme expression in Escherichia coli
Homo sapiens
Crystallization (Commentary)
Crystallization (Commentary)
Organism
crystallization of a single point mutant, X-ray diffraction structure determination and analysis at 1.8 A resolution
Trigonopsis variabilis
Engineering
Protein Variants
Commentary
Organism
additional information
for development of a micro-biosensor for determination of D-serine in vivo, the enzyme is physically adsorbed on an electrode surface. For in vivo experiments, the enzyme layer is protected with an additional Nafion membrane
Rhodotorula toruloides
additional information
for development of a micro-biosensor for determination of D-serine in vivo, the enzyme is adsorbed on a cylindrical platinum microelectrode covered by a layer of poly-m-phenylenediamine, a selective mediator for H2O2
Sus scrofa
additional information
construction of point mutants with altered substrate specificity compared to the wild-type enzyme, the created mutant forms of TvDAAO are perfectly suitable for selective determination of D-Ser in excess of D-Ala, D-Asp, and D-Pro
Trigonopsis variabilis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
D-3,4-dihydroxyphenylalanine + H2O + O2
Homo sapiens
-
? + H2O2 + NH3
-
-
?
D-alanine + H2O + O2
Trigonopsis variabilis
-
pyruvate + NH3 + H2O2
-
-
?
D-alanine + H2O + O2
Homo sapiens
-
pyruvate + H2O2 + NH3
-
-
?
D-proline + H2O + O2
Trigonopsis variabilis
-
2-oxopentanoate + NH3 + H2O2
-
-
?
D-serine + H2O + O2
Homo sapiens
-
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
?
D-serine + H2O + O2
Trigonopsis variabilis
-
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
?
additional information
Homo sapiens
the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview
?
-
-
-
additional information
Sus scrofa
the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview
?
-
-
-
additional information
Trigonopsis variabilis
the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview
?
-
-
-
additional information
Rhodotorula toruloides
the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview
?
-
-
-
Organism
Organism
UniProt
Commentary
Textmining
Homo sapiens
-
-
-
Rhodotorula toruloides
P80324
-
-
Sus scrofa
-
-
-
Trigonopsis variabilis
Q99042
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
kidney
-
Sus scrofa
-
kidney
-
Homo sapiens
-
liver
-
Homo sapiens
-
liver
-
Sus scrofa
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
D-3,4-dihydroxyphenylalanine + H2O + O2
-
696158
Homo sapiens
? + H2O2 + NH3
-
-
-
?
D-3,4-dihydroxyphenylalanine + H2O + O2
best substrate
696158
Homo sapiens
? + H2O2 + NH3
-
-
-
?
D-alanine + H2O + O2
-
696158
Trigonopsis variabilis
pyruvate + NH3 + H2O2
-
-
-
?
D-alanine + H2O + O2
-
696158
Homo sapiens
pyruvate + H2O2 + NH3
-
-
-
?
D-proline + H2O + O2
-
696158
Trigonopsis variabilis
2-oxopentanoate + NH3 + H2O2
-
-
-
?
D-serine + H2O + O2
-
696158
Homo sapiens
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
?
D-serine + H2O + O2
-
696158
Trigonopsis variabilis
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
?
additional information
the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview
696158
Homo sapiens
?
-
-
-
-
additional information
the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview
696158
Sus scrofa
?
-
-
-
-
additional information
the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview
696158
Trigonopsis variabilis
?
-
-
-
-
additional information
the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview
696158
Rhodotorula toruloides
?
-
-
-
-
additional information
the enzyme catalyzes oxidative deamination of D-amino acids yielding hydrogen peroxide and an imino acid. The latter is further non-enzymatically hydrolyzed to an alpha-keto acid and ammonium. DAAO is highly specific towards D-isomers of amino acids, it is almost inactive towards the corresponding L-isomer
696158
Homo sapiens
?
-
-
-
-
additional information
the enzyme catalyzes oxidative deamination of D-amino acids yielding hydrogen peroxide and an imino acid. The latter is further non-enzymatically hydrolyzed to an alpha-keto acid and ammonium. DAAO is highly specific towards D-isomers of amino acids, it is almost inactive towards the corresponding L-isomer
696158
Sus scrofa
?
-
-
-
-
additional information
the enzyme catalyzes oxidative deamination of D-amino acids yielding hydrogen peroxide and an imino acid. The latter is further non-enzymatically hydrolyzed to an alpha-keto acid and ammonium. DAAO is highly specific towards D-isomers of amino acids, it is almost inactive towards the corresponding L-isomer
696158
Rhodotorula toruloides
?
-
-
-
-
additional information
the enzyme catalyzes oxidative deamination of D-amino acids yielding hydrogen peroxide and an imino acid. The latter is further non-enzymatically hydrolyzed to an alpha-keto acid and ammonium. DAAO is highly specific towards D-isomers of amino acids, it is almost inactive towards the corresponding L-isomer. The wild-type enzyme is inactive towards D-Asp, being however very active with D-Ala
696158
Trigonopsis variabilis
?
-
-
-
-
Synonyms
Synonyms
Commentary
Organism
DAAO
-
Rhodotorula toruloides
DAAO
-
Trigonopsis variabilis
DAAO
-
Homo sapiens
DAAO
-
Sus scrofa
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
dependent on
Homo sapiens
FAD
dependent on
Rhodotorula toruloides
FAD
dependent on
Sus scrofa
FAD
dependent on
Trigonopsis variabilis
Application (protein specific)
Application
Commentary
Organism
analysis
the enzyme is useful as a model FAD-containing protein
Sus scrofa
medicine
the purified recombinant or native enzyme is used in therapeutic treatment of cancer combined with injection of D-proline. The enzyme is a target in the development of medical treatment for neurodegeneration and cancer
Homo sapiens
synthesis
the enzyme is used to produce phenyl pyruvate from D-phenylalanine with the yield of 99%
Rhodotorula toruloides
synthesis
pig kidney enzyme is used to make L-pipecolic acid from a racemic mixture via D-isomer oxidation
Sus scrofa
synthesis
the enzyme is used to develop biocatalysts for the production of 7-aminocephalosporanic acid from the natural antibiotic cephalosporin C, and to produce optically active L-methionine from D-amino acid with the yield of 100% in a cascade system of four enzymes, or to produce phenyl pyruvate from D-phenylalanine with the yield of 99%
Trigonopsis variabilis
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant enzyme expression in Escherichia coli
Homo sapiens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
dependent on
Homo sapiens
FAD
dependent on
Rhodotorula toruloides
FAD
dependent on
Sus scrofa
FAD
dependent on
Trigonopsis variabilis
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystallization of a single point mutant, X-ray diffraction structure determination and analysis at 1.8 A resolution
Trigonopsis variabilis
Engineering (protein specific)
Protein Variants
Commentary
Organism
additional information
for development of a micro-biosensor for determination of D-serine in vivo, the enzyme is physically adsorbed on an electrode surface. For in vivo experiments, the enzyme layer is protected with an additional Nafion membrane
Rhodotorula toruloides
additional information
for development of a micro-biosensor for determination of D-serine in vivo, the enzyme is adsorbed on a cylindrical platinum microelectrode covered by a layer of poly-m-phenylenediamine, a selective mediator for H2O2
Sus scrofa
additional information
construction of point mutants with altered substrate specificity compared to the wild-type enzyme, the created mutant forms of TvDAAO are perfectly suitable for selective determination of D-Ser in excess of D-Ala, D-Asp, and D-Pro
Trigonopsis variabilis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
D-3,4-dihydroxyphenylalanine + H2O + O2
Homo sapiens
-
? + H2O2 + NH3
-
-
?
D-alanine + H2O + O2
Trigonopsis variabilis
-
pyruvate + NH3 + H2O2
-
-
?
D-alanine + H2O + O2
Homo sapiens
-
pyruvate + H2O2 + NH3
-
-
?
D-proline + H2O + O2
Trigonopsis variabilis
-
2-oxopentanoate + NH3 + H2O2
-
-
?
D-serine + H2O + O2
Homo sapiens
-
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
?
D-serine + H2O + O2
Trigonopsis variabilis
-
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
?
additional information
Homo sapiens
the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview
?
-
-
-
additional information
Sus scrofa
the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview
?
-
-
-
additional information
Trigonopsis variabilis
the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview
?
-
-
-
additional information
Rhodotorula toruloides
the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview
?
-
-
-
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
kidney
-
Sus scrofa
-
kidney
-
Homo sapiens
-
liver
-
Homo sapiens
-
liver
-
Sus scrofa
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
D-3,4-dihydroxyphenylalanine + H2O + O2
-
696158
Homo sapiens
? + H2O2 + NH3
-
-
-
?
D-3,4-dihydroxyphenylalanine + H2O + O2
best substrate
696158
Homo sapiens
? + H2O2 + NH3
-
-
-
?
D-alanine + H2O + O2
-
696158
Trigonopsis variabilis
pyruvate + NH3 + H2O2
-
-
-
?
D-alanine + H2O + O2
-
696158
Homo sapiens
pyruvate + H2O2 + NH3
-
-
-
?
D-proline + H2O + O2
-
696158
Trigonopsis variabilis
2-oxopentanoate + NH3 + H2O2
-
-
-
?
D-serine + H2O + O2
-
696158
Homo sapiens
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
?
D-serine + H2O + O2
-
696158
Trigonopsis variabilis
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
?
additional information
the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview
696158
Homo sapiens
?
-
-
-
-
additional information
the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview
696158
Sus scrofa
?
-
-
-
-
additional information
the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview
696158
Trigonopsis variabilis
?
-
-
-
-
additional information
the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview
696158
Rhodotorula toruloides
?
-
-
-
-
additional information
the enzyme catalyzes oxidative deamination of D-amino acids yielding hydrogen peroxide and an imino acid. The latter is further non-enzymatically hydrolyzed to an alpha-keto acid and ammonium. DAAO is highly specific towards D-isomers of amino acids, it is almost inactive towards the corresponding L-isomer
696158
Homo sapiens
?
-
-
-
-
additional information
the enzyme catalyzes oxidative deamination of D-amino acids yielding hydrogen peroxide and an imino acid. The latter is further non-enzymatically hydrolyzed to an alpha-keto acid and ammonium. DAAO is highly specific towards D-isomers of amino acids, it is almost inactive towards the corresponding L-isomer
696158
Sus scrofa
?
-
-
-
-
additional information
the enzyme catalyzes oxidative deamination of D-amino acids yielding hydrogen peroxide and an imino acid. The latter is further non-enzymatically hydrolyzed to an alpha-keto acid and ammonium. DAAO is highly specific towards D-isomers of amino acids, it is almost inactive towards the corresponding L-isomer
696158
Rhodotorula toruloides
?
-
-
-
-
additional information
the enzyme catalyzes oxidative deamination of D-amino acids yielding hydrogen peroxide and an imino acid. The latter is further non-enzymatically hydrolyzed to an alpha-keto acid and ammonium. DAAO is highly specific towards D-isomers of amino acids, it is almost inactive towards the corresponding L-isomer. The wild-type enzyme is inactive towards D-Asp, being however very active with D-Ala
696158
Trigonopsis variabilis
?
-
-
-
-
General Information
General Information
Commentary
Organism
physiological function
physiological role of D-amino acids and DAAOs, regulation of the nervous system, hormone secretion, and other processes by D-amino acids, detailed overview
Homo sapiens
physiological function
physiological role of D-amino acids and DAAOs, regulation of the nervous system, hormone secretion, and other processes by D-amino acids, detailed overview
Rhodotorula toruloides
physiological function
physiological role of D-amino acids and DAAOs, regulation of the nervous system, hormone secretion, and other processes by D-amino acids, detailed overview
Sus scrofa
physiological function
physiological role of D-amino acids and DAAOs, regulation of the nervous system, hormone secretion, and other processes by D-amino acids, detailed overview
Trigonopsis variabilis
General Information (protein specific)
General Information
Commentary
Organism
physiological function
physiological role of D-amino acids and DAAOs, regulation of the nervous system, hormone secretion, and other processes by D-amino acids, detailed overview
Homo sapiens
physiological function
physiological role of D-amino acids and DAAOs, regulation of the nervous system, hormone secretion, and other processes by D-amino acids, detailed overview
Rhodotorula toruloides
physiological function
physiological role of D-amino acids and DAAOs, regulation of the nervous system, hormone secretion, and other processes by D-amino acids, detailed overview
Sus scrofa
physiological function
physiological role of D-amino acids and DAAOs, regulation of the nervous system, hormone secretion, and other processes by D-amino acids, detailed overview
Trigonopsis variabilis
Other publictions for EC 1.4.3.3
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)