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Information on EC 1.4.3.3 - D-amino-acid oxidase and Organism(s) Sus scrofa and UniProt Accession P00371
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1.4.3.3 D-amino-acid oxidaseIUBMB Comments
A flavoprotein (FAD). Wide specificity for D-amino acids. Also acts on glycine.
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Word Map
- 1.4.3.3
- d-serine
-
schizophrenia
- peroxisomal
- flavin
- n-methyl-d-aspartate
- d-alanine
- catalase
- fad
- nmda
-
deamination
- benzoate
-
flavoenzyme
- flavoproteins
- racemase
- variabilis
-
l-amino
-
neurotransmission
- d-aspartate
- gracilis
-
co-agonist
- rhodotorula
- cephalosporin
-
glutamatergic
- urate
- d-proline
- d-ala
- d-ser
-
imino
-
antipsychotic
-
hypofunction
- d-methionine
- isoalloxazine
- acylase
-
fad-containing
- toruloides
- rhodosporidium
- d-glutamate
-
fad-dependent
- d-cysteine
-
kynurenic
- sulfurtransferase
- d-valine
- synthesis
- medicine
- d-leucine
- cerium
-
7-aminocephalosporanic
- d-tryptophan
- d-phenylalanine
- neuregulin
- 3-mercaptopyruvate
- sarcosine
- industry
- biotechnology
- analysis
- diagnostics
- drug development
- pharmacology
The taxonomic range for the selected organisms is: Sus scrofa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
d-amino acid oxidase, d-amino-acid oxidase, hdaao, d-aao, rgdaao, tvdao, tvdaao, d-aminoacid oxidase, peg-dao, pkdaao, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-aminoacid oxidase
-
-
-
-
DAAO
DAMOX
-
-
-
-
DAO
ophio-amino-acid oxidase
-
-
-
-
oxidase, D-amino acid
-
-
-
-
DAAO
-
-
-
-
DAO
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
oxidative deamination
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -
SYSTEMATIC NAME
IUBMB Comments
D-amino-acid:oxygen oxidoreductase (deaminating)
A flavoprotein (FAD). Wide specificity for D-amino acids. Also acts on glycine.
CAS REGISTRY NUMBER
COMMENTARY
9000-88-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(1R)-1-(2-naphthyl)ethylamine + H2O + O2
1-(naphthalen-2-yl)ethan-1-one + NH3 + H2O2
substrate of mutant Y228L/F242I/R283G
-
-
?
(1R)-1-phenylpropan-1-amine + H2O + O2
1-phenylpropan-1-one + NH3 + H2O2
mutant Y228L/R283G, 109% of the activity with (1R)-1-phenylethan-1-amine
-
-
?
(R)-alpha-methylbenzylamine + H2O + O2
alpha-methylbenzaldehyde + NH3 + H2O2
substrate of mutant Y228L/R283G, the neutral amine is the substrate
-
-
?
(RS)-1-(4-chlorophenyl)-1-phenylmethanamine + H2O + O2
(4-chlorophenyl)(phenyl)methanone + NH3 + H2O2
no substrate of wild-type
-
-
?
1,1-diphenylmethanamine + H2O + O2
diphenylmethanone + NH3 + H2O2
no substrate of wild-type
-
-
?
1-(4-fluorophenyl)ethan-1-amine + H2O + O2
1-phenylethan-1-one + NH3 + H2O2
mutant Y228L/R283G, 22.7% of the activity with (1R)-1-phenylethan-1-amine
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
-
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
-
?
D-alanine + 2,6-dichlorophenolindophenol + H2O
pyruvate + reduced 2,6-dichlorophenolindophenol + H2O2
-
-
-
-
r
D-alanine + H2O + O2
pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-alanine + oxidized methylene blue + H2O
pyruvate + reduced methylene blue + H2O2
-
-
-
-
r
D-histidine + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + H2O2
-
-
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-threonine + H2O + O2
2-oxo-3-hydroxybutyrate + NH3 + H2O2
-
2% of the activity with D-Pro
-
-
?
D-Tyr + H2O + O2
4-hydroxyphenylpyruvic acid + NH3 + H2O2
-
4% of the activity with D-Pro
-
-
?
D-valine + H2O + O2
alpha-ketoisovaleric acid + NH3 + H2O2
-
-
-
-
?
epsilon-N-benzoyl-D-lysine + H2O + O2
6-benzylamino-2-oxohexanoate + NH3 + H2O2
-
-
-
-
?
(1R)-1-phenylethan-1-amine + H2O + O2
1-phenylethan-1-one + NH3 + H2O2
no substrate of wild-type
-
-
?
(1R)-1-phenylethan-1-amine + H2O + O2
1-phenylethan-1-one + NH3 + H2O2
no substrate of wild-type, but mutant Y228L/R283G
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
-
?
D-proline + H2O + O2
2-oxopentanoate + NH3 + H2O2
best substrate
-
-
?
D-tryptophan + H2O + O2
indole-3-pyruvic acid + NH3 + H2O2
DAAO catalyzes the production of aryl hydrocarbon receptor, AHR, agonists through the enzymatic conversion of D-tryptophan to indole-3-pyruvic acid
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-Arg + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
-
4% of the activity with D-Pro
-
-
?
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
-
38.6% activity compared to D-Ser
-
-
?
D-Gln + H2O + O2
2-oxoglutaramate + NH3 + H2O2
-
1% of the activity with D-Pro
-
-
?
D-Glu + H2O + O2
alpha-ketoglutarate + NH3 + H2O2
-
4% of the activity with D-Pro
-
-
?
D-His + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2
-
3% of the activity with D-Pro
-
-
?
D-Ile + H2O + O2
3-methyl-2-oxopentanoate + NH3 + H2O2
-
35% of the activity with D-Pro
-
-
?
D-Leu + H2O + O2
4-methyl-2-oxopentanoate + NH3 + H2O2
-
21% of the activity with D-Pro
-
-
?
D-Met + H2O + O2
4-methylthio-2-oxobutanoate + NH3 + H2O2
-
-
-
-
?
D-Met + H2O + O2
4-methylthio-2-oxobutanoate + NH3 + H2O2
-
75% of the activity with D-Pro
-
-
?
D-Phe + H2O + O2
phenylpyruvate + NH3 + H2O2
-
84% of the activity with D-Pro
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-Ser + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
-
?
D-Ser + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
18% of the activity with D-Pro
-
-
?
D-Trp + H2O + O2
indol-3-pyruvate + NH3 + H2O2
-
2% of the activity with D-Pro
-
-
?
D-Val + H2O + O2
alpha-ketoisovalerate + NH3 + H2O2
-
28% of the activity with D-Pro
-
-
?
additional information
?
-
D-aspartate and D-glutamate are no substrates
-
-
?
additional information
?
-
D-proline is the best substrate followed by D-methionine, D-alanine, D-norleucine, D-isoleucine, and D-phenylalanine
-
-
?
additional information
?
-
-
D-proline is the best substrate followed by D-methionine, D-alanine, D-norleucine, D-isoleucine, and D-phenylalanine
-
-
?
additional information
?
-
the enzyme exhibits very low activity towards basic amino acids, and it does not oxidize those with an acidic side chain
-
-
?
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
-
-
?
additional information
?
-
-
DAAO is a flavoprotein that catalyzes the dehydrogenation of different D-amino acids to their imino counterparts via a reduced flavin product complex. The reduced flavin is then reoxidized by O2 to yield H2O2, whereas the imino acid spontaneously hydrolyzes to the corresponding keto acid and NH4+. DAAO is strictly stereospecific and oxidizes a variety of D-amino acids, with a preference for those having small hydrophobic side chains, followed by those bearing polar, aromatic, and basic groups
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-tryptophan + H2O + O2
indole-3-pyruvic acid + NH3 + H2O2
DAAO catalyzes the production of aryl hydrocarbon receptor, AHR, agonists through the enzymatic conversion of D-tryptophan to indole-3-pyruvic acid
-
-
?
D-alanine + H2O + O2
pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-histidine + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + H2O2
-
-
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-valine + H2O + O2
alpha-ketoisovaleric acid + 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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(5R)-4-hydroxy-3,5-dimethyl-5-[(1E)-2-methyl-1,3-butadienyl]-2(5H)-thiophenone
-
i.e. thiolactomycin, competitive inhibition, competes with both the substrate and the coenzyme FAD
Sodium benzoate
inhibits the enzyme activity by impeding the interaction of the enzyme with the flavin prosthetic group
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.9
(R)-alpha-methylbenzylamine
mutant Y228L/R283G, pH 8, 25°C. The kcat/Km profile exhibits a maximum at pH 10
additional information
additional information
-
the dextran-conjugated enzyme shows decreased KM-values for D-amino acids
-
2.94
(RS)-1-(4-chlorophenyl)-1-phenylmethanamine
mutant I230A/R283G, 30°C, pH 8.0
-
2.96
(RS)-1-(4-chlorophenyl)-1-phenylmethanamine
mutant I230C/R283G, 30°C, pH 8.0
-
3.73
(RS)-1-(4-chlorophenyl)-1-phenylmethanamine
mutant I230F/R283G, 30°C, pH 8.0
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.33
(RS)-1-(4-chlorophenyl)-1-phenylmethanamine
mutant I230F/R283G, 30°C, pH 8.0
-
5.48
(RS)-1-(4-chlorophenyl)-1-phenylmethanamine
mutant I230C/R283G, 30°C, pH 8.0
-
6.01
(RS)-1-(4-chlorophenyl)-1-phenylmethanamine
mutant I230A/R283G, 30°C, pH 8.0
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.83
(1R)-1-(2-naphthyl)ethylamine
mutant Y228L/F242I/R283G, pH not specified in the publication, temperature not specified in the publication
-
1.15
(RS)-1-(4-chlorophenyl)-1-phenylmethanamine
mutant I230F/R283G, 30°C, pH 8.0
-
1.85
(RS)-1-(4-chlorophenyl)-1-phenylmethanamine
mutant I230C/R283G, 30°C, pH 8.0
-
2.05
(RS)-1-(4-chlorophenyl)-1-phenylmethanamine
mutant I230A/R283G, 30°C, pH 8.0
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
inhibition kinetics with risperidone, in vivo inhibition of cellular DAO activity in LLC-PK1 cells and cytotoxicity, overview
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
2,3-dioxo-1,2,3,4-tetrahydropyrido[2,3-b]pyrazine-7-carboxylic acid
Sus scrofa
-
at pH 8.2 and 37°C
0.00053
7,8-dibromo-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.00065
7,8-dichloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.00048
7-bromo-8-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.0004
7-bromo-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.00026
7-chloro-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.00015
7-fluoro-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.0229
7-trifluoromethyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.00024
8-bromo-7-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.3
8-phenylethoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.3
8-phenylpropoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.00052
8-trifluoromethyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
1
methyl 2,3-dioxo-1,2,3,4-tetrahydropyrido[2,3-b]pyrazine-7-carboxylate
Sus scrofa
-
at pH 8.2 and 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
21.5
mutant Y228L/R283G, substrate (1R)-1-phenylethan-1-amine, pH not specified in the publication, temperature not specified in the publication
4.6
-
recombinant polyethylene glycol-conjugated D-amino acid oxidase, at 25°C in 0.1 M Tris-HCl buffer (pH 8.2)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9 - 10
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.3 - 10.3
-
less than 50% of maximal activity above and below, D-alanine, immobilized enzyme
7.7 - 10.5
-
less than 50% of maximal activity above and below, D-alanine, free enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 60
-
30°C: about 50% of maximal activity, 60°C: about 40% of maximal activity, wild-type enzyme
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzymatic function of DAAO is required for AHR activation by D-Trp and D-Tyr. DAAO catalyzes the production of aryl hydrocarbon receptor, AHR, agonists through the enzymatic conversion of D-tryptophan to indole-3-pyruvic acid, followed by nonenzymatic oxidation and condensation of indole-3-pyruvic acid is a critical step in the generation of receptor agonists by DAAO and aspartate aminotransferase, AST. Products of this process include the two agonists, 1,3-di(1H-indol-3-yl)propan-2-one and 1-(1H-indol-3-yl)-3-(3H-indol- 3-ylidene) propan-2-one, overview
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). OXDA_PIG
347
0
39336
Swiss-Prot
Secretory Pathway (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
113000
-
recombinant polyethylene glycol-conjugated D-amino acid oxidase, gel filtration
65000
-
2 * 65000, recombinant polyethylene glycol-conjugated D-amino acid oxidase, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
monomer
homodimer
-
2 * 65000, recombinant polyethylene glycol-conjugated D-amino acid oxidase, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
fluorescence lifetimes are 45 ps in the dimer, 185 ps in the monomer. The fluorescence lifetimes of the hDAAO did not change upon the inhibitor bindings. Three fastest electron transfer donors are Tyr314, Tyr224 and Tyr228 in the dimer, and Tyr224, Tyr314 and Tyr228 in the monomer
structure of mutant Y228L/R283G in complex with (R)-1-phenylethan-1-amine. The phenyl ring is flipped to the xylene ring of the isoalloxadine ring of FAD. The side chain of Phe242 rotates approximately 60 degrees between the wild-type and variant and forms part of the active site wall, while the phenyl ring of (R)-1-phenylethan-1-amine forms a hydrophobic interaction along with this rotation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E220D/Y224G
decreased catalytic activity for D-Ala compared to the wild type enzyme
E222D/Y224G
decreased catalytic activity for D-Ala compared to the wild type enzyme
G313A
decreased catalytic activity for D-Ala compared to the wild type enzyme
H307L
Kd for FAD is 28fold higher with respect to the wild type enzyme while activity is mostly retained
I230A/R283G
mutant accepts 1-(4-chlorophenyl)-1-phenylmethanamine as substrate, activity with (R)-1-phenylethylamine is diminished 10fold as compared with the Y228L/R283G variant
R221D/Y224G
decreased catalytic activity for D-Ala compared to the wild type enzyme
R283G
mutant has completely lost the activity for D-amino acids but accepts 1-(4-chlorophenyl)-1-phenylmethanamine as substrate
T56L
decrease in activity towards D-alanine, increase in activity towards D-serine, D-tryptophan
Y228F
50% activity compared to the wild type enzyme, 120fold decreased reduction rate
Y228L/R283G
Y55A
strong reduction in activity towards D-alanine, D-serine, increase in activity towards D-tryptophan, D-phenylalanine, D-tyrosine, D-arginine
Y55A/T56L
decrease in activity towards D-alanine, D-serine, increase in activity towards D-tryptophan
Y55W
strong reduction in activity towards D-alanine, D-serine, increase in activity towards D-tryptophan
Y55W/T56L
increase in activity towards D-alanine, D-tryptophan, D-arginine, D-cysteine, D-phenylalanine, D-tyrosine, decrease in activity towards D-serine
E220D/Y224G
-
kcat/KM for D-Arg is 5fold higher than wild-type value, kcat/Km for L-Lys is 2.91fold higher than wild-type value, kcat/KM for D-Ala is 124fold lower than wild-type value, kcat/Km for D-Ser is more than 110fold lower than wild-type value, kcat/Km for D-Pro is 17.5fold lower than wild-type value, kcat/Km for D-Val is 12fold lower than wild-type value, kcat/KM for D-Met is 1.5fold higher than wild-type value, kcat/KM for D-Phe is 3.3fold higher than wild-type value
F42C
-
mutant retains more than 70% of activity after 1 h, while the wild-type enzyme retains only 10% activity. Optimal temperature of mutant enzyme is about 10°C higher than that of wild-type enzyme. Activity at the optimal temperature is about 20% higher than that of wild-type enzyme. KM-values for D-Ala, D-Met, D-Phe and D-Ser are 40-50% of the wild-type value
additional information
Y228L/R283G
(R)-alpha-methylbenzylamine as neutral amine is substrate of mutant Y228L/R283G, while an active-site residue, likely Tyr224, must be uncharged for productive binding. The oxidative half-reaction is unperturbed by the mutation and with flavin oxidation preceding product release
Y228L/R283G
mutant accepts 1-(4-chlorophenyl)-1-phenylmethanamine as substrate
Y228L/R283G
mutant displays altered substrate specificity toward (R)-amines acting on alpha-methylbenzylamine and its derivatives, alpha-ethylbenzylamine, alkylamine, and cyclic secondary amines, and totally losing the activities toward the original substrates, D-amino acids
additional information
mutations in residues located on the loops on the border between the active site and the secondary binding pocket. Mutations modulate substrate specificity, product egress and enzyme activity
additional information
-
mutations in residues located on the loops on the border between the active site and the secondary binding pocket. Mutations modulate substrate specificity, product egress and enzyme activity
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
additional information
-
immobilization of the enzyme, interaction of D-amino acid oxidase with single-walled carbon nanotubes, analysis by spectroscopic ellipsometry. DAAO can adopt multiple orientations on the surface, which are ultimately responsible for significant differences in catalytic activity, highest enzymatic activity by adsorbing the protein at pH 5.7 and 0.1 mg/ml, adsorption kinetics at different pH values, overview
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
45
50
55
55
-
1 h, mutant enzyme F42C retains more than 70% of activity, wild-type enzyme retains only 10% activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Triton X-114
-
less than 10% decrease of enzyme activity after Triton X-114 treatment, sonication, lyophilization or repeated freezing-thawing
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
use of mutant Y228L/R283G for the deracemization of racemic(RS)-1-phenylethan-1-amine with NaBH4 to produce (1S)-1-phenylethan-1-amine with an enantiomeric excess of 99%
analysis
medicine
-
polyethylene glycol-conjugated D-amino acid oxidase exhibits potent antitumor activity by generating toxic reactive oxygen species, namely oxidation therapy, subsequently shows remarkable antitumor effect on murine sarcoma 180 solid tumor
synthesis
-
pig kidney enzyme is used to make L-pipecolic acid from a racemic mixture via D-isomer oxidation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bright, H.J.; Porter, D.J.T.
Flavoprotein oxidases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
12
421-505
1975
Sus scrofa
-
Dixon, M.; Kleppe, K.
D-Amino acid oxidase I. Dissociation and recombination of the holoenzyme
Biochim. Biophys. Acta
96
357-367
1965
Sus scrofa
Dixon, M.; Kleppe, K.
D-Amino acid oxidase II. specificity, competitive inhibition and reaction sequence
Biochim. Biophys. Acta
96
368-382
1965
Sus scrofa
-
Dixon, M.; Kleppe, K.
D-Amino acid oxidase II. Effect of pH
Biochim. Biophys. Acta
96
383-389
1965
Sus scrofa
Tosa, T.; Sano, R.; Chibata, I.
Immobilized D-amino acid oxidase. Preparation, some enzymatic properties, and potential uses
Agric. Biol. Chem.
38
1529-1534
1974
Sus scrofa
-
Harbron, S.; Fisher, M.; Rabin, B.R.
Large scale preparation and purification of apo-D-aminoacid oxidase for use in novel amplification assays
Biotechnol. Tech.
6
55-60
1992
Sus scrofa
-
Watanabe, F.; Fukui, K.; Momoi, K.; Miyake, Y.
Expression of normal and abnormal porcine kidney D-amino acid oxidase in Escherichia coli: purification and characterization of the enzymes
Biochem. Biophys. Res. Commun.
165
1422-1427
1989
Sus scrofa
Tarelli, G.T.; Vanoni, M.A.; Negri, A.; Curti, B.
Characterization of a fully active N-terminal 37-kDa polypeptide obtained by limited tryptic cleavage of pig kidney D-amino acid oxidase
J. Biol. Chem.
265
21242-21246
1990
Sus scrofa
Yagi, K.
D-Amino acid oxidase and its complexes (hog kidney)
Methods Enzymol.
17B
608-622
1971
Sus scrofa
-
Parkin, K.; Hultin, H.O.
Immobilization and characterization of D-amino acid oxidase
Biotechnol. Bioeng.
21
939-953
1979
Sus scrofa
Hamilton, G.A.; Buckthal, D.J.
The inhibition of mammalian D-amino acid oxidase by metabolites and drugs. Inferences concerning physiological function
Bioorg. Chem.
11
350-370
1982
Sus scrofa
-
Carrera, G.; Pasta, P.; Curti, B.
Renaturation studies of free and immobilized D-amino-acid oxidase
Biochim. Biophys. Acta
745
181-188
1983
Sus scrofa
Bergmeyer, H.U.
D-Aminosure-Oxydase
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
1
460-461
1974
Sus scrofa
-
Leonil, J.; Langrene, S.; Sicsic, S.; Le Goffic, F.
Purification of D-amino acid oxidase apoenzyme by affinity chromatography on Cibacron Blue Sepharose
J. Chromatogr.
347
316-319
1985
Sus scrofa
Tu, S.C.; Edelstein, S.J.; McCormick, D.B.
A modified purification method and properties of pure porcine D-amino acid oxidase
Arch. Biochem. Biophys.
159
889-896
1973
Sus scrofa
-
Setoyama, C.; Nishina,Y.; Tamaoki, H.; Mizutani, H.; Miyahara, I.; Hirotsu, K.; Shiga, K.; Miura, R.
Effects of hydrogen bond in association with flavin and substrate in flavoenzyme D-amino acid oxidase. The catalytic and structural roles of gly313 and thr317
J. Biochem.
131
59-69
2002
Sus scrofa
Pollegioni, L.; Fukui, K.; Massey, V.
Studies on the kinetic mechanism of pig kidney D-amino acid oxidase by site-directed mutagenesis of tyrosine 224 and tyrosine 228
J. Biol. Chem.
269
31666-31673
1994
Sus scrofa
Pilone, M.S.
D-Amino acid oxidase: new findings
Cell. Mol. Life Sci.
57
1732-1747
2000
Homo sapiens, Rhodotorula toruloides, Sus scrofa, Trigonopsis variabilis
Moreno, J.A.; Montes, F.J.; Catalan, J.; Galan, M.A.
Inhibition of D-amino acid oxidase by alpha-keto acids analogs of amino acids
Enzyme Microb. Technol.
18
379-382
1996
Sus scrofa
Bakke, M.; Kajiyama, N.
Improvement in thermal stability and substrate binding of pig kidney D-amino acid oxidase by chemical modification
Appl. Biochem. Biotechnol.
112
123-131
2004
Sus scrofa
Tishkov, V.I.; Khoronenkova, S.V.
D-Amino acid oxidase: structure, catalytic mechanism, and practical application
Biochemistry
70
40-54
2005
Candida parapsilosis, Fusarium oxysporum, Rhodotorula toruloides, Sus scrofa, Trigonopsis variabilis, Acrostalagmus luteoalbus, [Candida] boidinii (Q9HGY3)
Pollegioni, L.; Caldinelli, L.; Molla, G.; Sacchi, S.; Pilone, M.S.
Catalytic properties of D-amino acid oxidase in cephalosporin C bioconversion: a comparison between proteins from different sources
Biotechnol. Prog.
20
467-473
2004
Rhodotorula toruloides, Sus scrofa, Trigonopsis variabilis
Bakke, M.; Setoyama, C.; Miura, R.; Kajiyama, N.
Thermostabilization of porcine kidney D-amino acid oxidase by a single amino acid substitution
Biotechnol. Bioeng.
93
1023-1027
2006
Sus scrofa
Setoyama, C.; Nishina, Y.; Mizutani, H.; Miyahara, I.; Hirotsu, K.; Kamiya, N.; Shiga, K.; Miura, R.
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the active-site lid
J. Biochem.
139
873-879
2006
Sus scrofa
Pernot, P.; Mothet, J.P.; Schuvailo, O.; Soldatkin, A.; Pollegioni, L.; Pilone, M.; Adeline, M.T.; Cespuglio, R.; Marinesco, S.
Characterization of a yeast D-amino acid oxidase microbiosensor for D-serine detection in the central nervous system
Anal. Chem.
80
1589-1597
2008
Rhodotorula toruloides, Sus scrofa
Pollegioni, L.; Piubelli, L.; Sacchi, S.; Pilone, M.S.; Molla, G.
Physiological functions of D-amino acid oxidases: from yeast to humans
Cell. Mol. Life Sci.
64
1373-1394
2007
Chlorella vulgaris, Rattus norvegicus (O35078), Sus scrofa (P00371), Homo sapiens (P14920), Homo sapiens, Mus musculus (P18894), Rhodotorula toruloides (P80324), Cyprinus carpio (Q6TGN2), Trigonopsis variabilis (Q99042), [Candida] boidinii (Q9HGY3)
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
Curr. Protein Pept. Sci.
8
600-618
2007
Sus scrofa (P00371), Sus scrofa, Homo sapiens (P14920), Homo sapiens, Rhodotorula toruloides (P80324), Trigonopsis variabilis (Q99042)
Fang, J.; Deng, D.; Nakamura, H.; Akuta, T.; Qin, H.; Iyer, A.K.; Greish, K.; Maeda, H.
Oxystress inducing antitumor therapeutics via tumor-targeted delivery of PEG-conjugated D-amino acid oxidase
Int. J. Cancer
122
1135-1144
2008
Sus scrofa
Sacchi, S.; Bernasconi, M.; Martineau, M.; Mothet, J.P.; Ruzzene, M.; Pilone, M.S.; Pollegioni, L.; Molla, G.
pLG72 modulates intracellular D-serine levels through its interaction with D-amino acid oxidase: Effect on schizophrenia susceptibility
J. Biol. Chem.
283
22244-22256
2008
Homo sapiens, Sus scrofa
Mora, M.F.; Giacomelli, C.E.; Garcia, C.D.
Interaction of D-amino acid oxidase with carbon nanotubes: implications in the design of biosensors
Anal. Chem.
81
1016-1022
2009
Sus scrofa
Khoronenkova, S.V.; Tishkov, V.I.
D-amino acid oxidase: physiological role and applications
Biochemistry (Moscow)
73
1511-1518
2008
Homo sapiens, Sus scrofa, Rhodotorula toruloides (P80324), Trigonopsis variabilis (Q99042)
Nguyen, L.P.; Hsu, E.L.; Chowdhury, G.; Dostalek, M.; Guengerich, F.P.; Bradfield, C.A.
D-amino acid oxidase generates agonists of the aryl hydrocarbon receptor from D-tryptophan
Chem. Res. Toxicol.
22
1897-1904
2009
Homo sapiens, Sus scrofa (P00371)
Abou El-Magd, R.; Park, H.; Kawazoe, T.; Iwana, S.; Ono, K.; Chung, S.; Miyano, M.; Yorita, K.; Sakai, T.; Fukui, K.
The effect of risperidone on D-amino acid oxidase activity as a hypothesis for a novel mechanism of action in the treatment of schizophrenia
J. Psychopharmacol. (Oxford)
2009
1-13
2009
Homo sapiens, Mus musculus, Sus scrofa
Katane, M.; Saitoh, Y.; Hanai, T.; Sekine, M.; Furuchi, T.; Koyama, N.; Nakagome, I.; Tomoda, H.; Hirono, S.; Homma, H.
Thiolactomycin inhibits D-aspartate oxidase: a novel approach to probing the active site environment
Biochimie
92
1371-1378
2010
Sus scrofa
Xie, D.; Lu, J.; Xie, J.; Cui, J.; Li, T.F.; Wang, Y.C.; Chen, Y.; Gong, N.; Li, X.Y.; Fu, L.; Wang, Y.X.
Discovery and analgesic evaluation of 8-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione as a novel potent D-amino acid oxidase inhibitor
Eur. J. Med. Chem.
117
19-32
2016
Homo sapiens, Rattus norvegicus, Sus scrofa
Yoshimoto, M.; Okamoto, M.; Ujihashi, K.; Okita, T.
Selective oxidation of D-amino acids catalyzed by oligolamellar liposomes intercalated with D-amino acid oxidase
Langmuir
30
6180-6186
2014
Sus scrofa
Liu, Q.; Chen, L.; Zhang, Z.; Du, B.; Xiao, Y.; Yang, K.; Gong, L.; Wu, L.; Li, X.; He, Y.
pH-Dependent enantioselectivity of D-amino acid oxidase in aqueous solution
Sci. Rep.
7
2994
2017
Sus scrofa
Jiang, J.F.; Qiao, J.; Mu, X.Y.; Moon, M.H.; Qi, L.
Fabrication of enzyme reactor utilizing magnetic porous polymer membrane for screening D-amino acid oxidase inhibitors
Talanta
165
251-257
2017
Sus scrofa
Trimmer, E.E.; Wanninayake, U.S.; Fitzpatrick, P.F.
Mechanistic studies of an amine oxidase derived from D-amino acid oxidase
Biochemistry
56
2024-2030
2017
Sus scrofa (P00371)
Yasukawa, K.; Motojima, F.; Ono, A.; Asano, Y.
Expansion of the substrate specificity of porcine kidney D-amino acid oxidase for S-stereoselective oxidation of 4-Cl-benzhydrylamine
ChemCatChem
10
3500-3505
2018
Sus scrofa (P00371), Sus scrofa
Yasukawa, K.; Kawahara, N.; Motojima, F.; Nakano, S.; Asano, Y.
Porcine kidney D-amino acid oxidase-derived R-amine oxidases with new substrate specificities
Enzymes
47
117-136
2020
Sus scrofa (P00371), Sus scrofa
Taniguchi, S.; Chosrowjan, H.; Ito, S.; Miyasaka, H.; Katane, M.; Homma, H.; Tanaka, F.; Nueangaudom, A.; Lugsanangarm, K.; Kokpol, S.
Comparative studies on picosecond-resolved fluorescence of D-amino acid oxidases from human with one from porcine kidney. Photoinduced electron transfer from aromatic amino acids to the excited flavin
J. Photochem. Photobiol. B
198
111546
2019
Sus scrofa (P00371), Sus scrofa, Homo sapiens (P14920), Homo sapiens
Subramanian, K.; Gora, A.; Spruijt, R.; Mitusinska, K.; Suarez-Diez, M.; Martins Dos Santos, V.; Schaap, P.J.
Modulating D-amino acid oxidase (DAAO) substrate specificity through facilitated solvent access
PLoS ONE
13
e0198990
2018
Sus scrofa (P00371), Sus scrofa, Homo sapiens (P14920), Homo sapiens
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