1.4.3.3: D-amino-acid oxidase
This is an abbreviated version!
For detailed information about D-amino-acid oxidase, go to the full flat file.
Word Map on EC 1.4.3.3
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1.4.3.3
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d-serine
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schizophrenia
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peroxisomal
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flavin
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n-methyl-d-aspartate
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d-alanine
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catalase
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fad
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nmda
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deamination
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benzoate
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flavoenzyme
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flavoproteins
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racemase
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variabilis
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l-amino
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neurotransmission
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d-aspartate
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gracilis
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co-agonist
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rhodotorula
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cephalosporin
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glutamatergic
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urate
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d-proline
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d-ala
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d-ser
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imino
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antipsychotic
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hypofunction
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d-methionine
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isoalloxazine
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acylase
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fad-containing
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toruloides
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rhodosporidium
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d-glutamate
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fad-dependent
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d-cysteine
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kynurenic
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sulfurtransferase
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d-valine
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synthesis
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medicine
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d-leucine
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cerium
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7-aminocephalosporanic
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d-tryptophan
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d-phenylalanine
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neuregulin
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3-mercaptopyruvate
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sarcosine
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industry
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biotechnology
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analysis
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diagnostics
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drug development
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pharmacology
- 1.4.3.3
- d-serine
-
schizophrenia
- peroxisomal
- flavin
- n-methyl-d-aspartate
- d-alanine
- catalase
- fad
- nmda
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deamination
- benzoate
-
flavoenzyme
- flavoproteins
- racemase
- variabilis
-
l-amino
-
neurotransmission
- d-aspartate
- gracilis
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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
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7-aminocephalosporanic
- d-tryptophan
- d-phenylalanine
- neuregulin
- 3-mercaptopyruvate
- sarcosine
- industry
- biotechnology
- analysis
- diagnostics
- drug development
- pharmacology
Reaction
Synonyms
chDAO, D-AAO, D-amino acid oxidase, D-amino-acid-oxidase, D-aminoacid oxidase, DAAO, DAMOX, DAO, DAO1, DaoE, hDAAO, ophio-amino-acid oxidase, oxidase, D-amino acid, PEG-DAO, pkDAAO, RgDAAO, TvDAAO, TvDAO, LH99
ECTree
1.4.3.3 D-amino-acid oxidaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.4.3.3 - D-amino-acid oxidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
G183R
inactive apoprotein, substitution negatively affects the ability to bind the flavin cofactor in the correct orientation. The overexpressed G183R protein is not fully targeted to peroxisomes, shows colocalization with ubiquitin, and increases 7fold both the D-serine cellular concentration and the D/(D+L)-serine ratio
G281C
L56T
increase in activity towards D-alanine, decrease in activity towards D-serine, D-tryptophan
P219L
mutation to corresponding residue of porcine DAO. The turnover numbers (kcat) of P219L are unchanged, but its Km values are decreased compared with wild-type, leading to an increase in the catalytic efficiency (kcat/Km). Benzoate inhibits P219L with lower Ki value
R120E
substitution in order to mimic the active nuclear translocation signal, slightly alters protein conformation, thermal stability, and kinetic properties, while the dimeric structure and the ligand-binding properties are unchanged. Mutant shows an increase in cytosolic localization that promotes nuclear targeting, without affecting cell viability
R120L
substitution in order to eliminate the positive charge, slightly alters protein conformation, thermal stability, and kinetic properties, while the dimeric structure and the ligand-binding properties are unchanged
R199W
Y55A
slight reduction in activity towards D-alanine, D-serine, increase in activity towards D-tryptophan, D-histidine, D-methionine, D-phenylalanine, D-tyrosine
Y55A/L56T
about 40-60% reduction in activity towards D-alanine, D-serine, slight reduction in activity towards D-tryptophan
Y55W
20-40% reduction in activity towards D-alanine, D-serine, no change in activity towards D-tryptophan
Y55W/L56T
50-70% reduction in activity towards D-alanine, D-serine, no change in activity towards D-tryptophan
D481N
G181R
G181R/D481N
compared to animals with only the Grin1D481N mutation, mice with both the Dao1G181R and Grin1D481N mutations display an improvement in social approach and spatial memory retention, as well as a reversal of abnormally persistent latent inhibition and a partial normalization of startle responses
D481N
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homozygous Grin1D481N mutant mice with reduced NMDA-NR1 glycine affinity exhibit an altered anxiety-like behavior. Deficient DAO activity also reverses the anxiolytic effects of diminished NMDAR function in mice carrying both the homozygous Grin1D481N and Dao1G181R mutation, phenotypes, overview
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G181R
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homozygous Dao1G181R mutant mice that lack function of the D-serine catabolic enzyme DAO display an elevation in anxiety, homozygous Grin1D481N mutant mice with reduced NMDA-NR1 glycine affinity exhibit also an altered anxiety-like behavior. Deficient DAO activity also reverses the anxiolytic effects of diminished NMDAR function in mice carrying both the homozygous Grin1D481N and Dao1G181R mutation, phenotypes, overview
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DELTAS308-K321
deletion of 14 amino acids from Ser308 to Lys321 in a surface loop (connecting beta-strands 12 and 13) transforms the enzyme from a dimeric protein into a stable monomer. The mutant enzyme is still catalytically competent and retains its binding with the FAD coenzyme. The Kd value of the apoprotein-FAD complex is 5fold higher than that of the wild-type enzyme. 1.9fold increase in Km-value for D-Ala, 1.8fold decrease in Vmax value with D-Trp
G52V
site-directed mutagenesis, in the mutant the reactivity of the reduced enzyme with O2 is decreased about 100fold and the turnover number about 1000fold compared to the wild-type enzyme
M213E
M213G
M213R
M213R/Y238R
the ratio of turnover number to Km-value for D-Asp is 36.6fold higher than that of the wild-type enzyme, the ratio of turnover number to Km-value for D-Ala is 1000fold lower than that of the wild-type enzyme
Q144R
Q339E
Q339N
mutant shows lower activity on neutral and basic amino acids compared to the wild type enzyme
S19G/S120P/Q144R/K321M/A345V
S335G
S335H
mutant shows lower activity on neutral and basic amino acids compared to the wild type enzyme
S335R
mutant shows lower activity on neutral and basic amino acids compared to the wild type enzyme
T60A/Q144R/K152E
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increased overall activity compared to the wild type enzyme
W243I
mutant ezyme with a significantly lower content of flavin cofactor. Loss of the tertiary structure elements and of the flavin cofactor occurs at lower temperatures in mutant than in the dimeric wild-type enzyme. The midpoint concentration of urea required for unfolding is significanlty lower than for the wild-type enzyme
W243Y
mutant enzyme retains the FAD coenzyme. Loss of the tertiary structure elements and of the flavin cofactor occurs at lower temperatures in mutant than in the dimeric wild-type enzyme
Y223F
mutant shows lower activity on neutral and basic amino acids compared to the wild type enzyme
Y223S
Y238F
Y238R
Y238S
E220D/Y224G
E222D/Y224G
decreased catalytic activity for D-Ala compared to the wild type enzyme
F42C
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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
G313A
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
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
C106C108-(SO2H)
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oxidatively modified enzyme shows 75% loss of activity
C108D
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site-directed mutagenesis, in contrast to the wild-type enzyme, the mutant releases the cofactor in a quasi-irreversible manner and is therefore not stabilized by external FAD against loss of activity. Conformational properties and kinetics of C108D, overview
C108S
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site-directed mutagenesis, in contrast to the wild-type enzyme, the mutant releases the cofactor in a quasi-irreversible manner and is therefore not stabilized by external FAD against loss of activity. Conformational properties and kinetics of C108S, overview
F258A
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the improvement of catalytic efficiency with D-Tyr, D-Phe, and D-Leu for mutant enzyme F258A is 3.66, 11.7, and 1.5fold, respectively. The mutant is inactive with D-Ala, D-Ser, D-Lys, and D-Thr, while the activity with D-Tyr, D-Leu and especially with D-Phe significantly increases
F258S
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the improvement of catalytic efficiency with D-Tyr, D-Phe, and D-Leu for mutant enzyme F258S is 1.7, 4.75, and 6.61fold, respectively. The mutant is inactive with D-Ala, D-Ser, D-Lys, and D-Thr, while the activity with D-Tyr, D-Leu and especially with D-Phe significantly increases
F258Y
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the mutant is inactive with D-Val, D-Tyr, D-Ala, D-Ser, D-Lys, and D-Thr
F54Y
site-directed mutagenesis, the mutant shows 6fold improvement in kcat,app and about 2.5fold increase in Ki of glutaryl-7-aminocephalosporanic acid, the substitution improves the catalytic activity and thermostability of mutant DAAO compared to the wild-type enzyme. Heat treatment at 55° for 60 min does not decrease the activity of F54Y. The Tyr substitution might initiate hydrogen bond formation with the amino group of CPC and facilitate deamination
R110A
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site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme, but shows increased temperature denaturation. Release of FAD is the dominant path of thermal denaturation of R110A
C108D
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site-directed mutagenesis, in contrast to the wild-type enzyme, the mutant releases the cofactor in a quasi-irreversible manner and is therefore not stabilized by external FAD against loss of activity. Conformational properties and kinetics of C108D, overview
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C108S
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site-directed mutagenesis, in contrast to the wild-type enzyme, the mutant releases the cofactor in a quasi-irreversible manner and is therefore not stabilized by external FAD against loss of activity. Conformational properties and kinetics of C108S, overview
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R110A
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site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme, but shows increased temperature denaturation. Release of FAD is the dominant path of thermal denaturation of R110A
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additional information
R199W
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naturally occuring mutation, the mutation in the D-amino acid oxidase gene is associated with classical adult onset familial amyotrophic lateral sclerosis the 14.52 cM region on chromosome 12q22-23 is linked to disease. Neuronal cell lines expressing R199W DAO show decreased viability and increased ubiquitinated aggregates compared with cells expressing the wild-type protein, overview. Lentiviral-mediated expression of mutant R199W DAO in primary motor neuron cultures causes increased TUNEL labeling
R199W
transgenic mice overexpressing mutant R199W show marked abnormal motor features, e.g. kyphosis, associated with a significant loss (19%) of lumbar spinal cord motor neurons, analyzed at 14 months. This effect is greater in females. In transgenic mice expressing mutant R199W and superoxide dismutase SOD1 G93A mutant, overall survival is not affected, but the onset of neurological signs is significantly earlier in female double transgenic animals than their female SOD1 G93A littermates
D481N
Grin1D481N mice show deficits in sociability, prolonged latent inhibition, enhanced startle reactivity and impaired spatial memory
D481N
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homozygous Grin1D481N mutant mice with reduced NMDA-NR1 glycine affinity exhibit an altered anxiety-like behavior. Deficient DAO activity also reverses the anxiolytic effects of diminished NMDAR function in mice carrying both the homozygous Grin1D481N and Dao1G181R mutation, phenotypes, overview
G181R
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homozygous Dao1G181R mutant mice that lack function of the D-serine catabolic enzyme DAO display an elevation in anxiety, homozygous Grin1D481N mutant mice with reduced NMDA-NR1 glycine affinity exhibit also an altered anxiety-like behavior. Deficient DAO activity also reverses the anxiolytic effects of diminished NMDAR function in mice carrying both the homozygous Grin1D481N and Dao1G181R mutation, phenotypes, overview
G181R
the hypofunctional Dao1G181R mutation elevates brain levels of D-serine, but alone it does not affect performance in the behavioral measures
M213E
mutant shows lower activity on neutral and basic amino acids compared to the wild type enzyme
M213G
mutant shows lower activity and substrate specificity constant on the natural aromatic D-amino acids and higher acitivy on artificial amino acids compared to the wild type enzyme
M213R
the ratio of turnover number to Km-value for D-Asp is 74fold higher than that of the wild-type enzyme, the ratio of turnover number to Km-value for D-Glu is 29.5fold higher than that of the wild-type enzyme, the ratio of turnover number to Km-value for D-Ala is 172fold lower than that of the wild-type enzyme, the ratio of turnover number to Km-value for D-Pro is 166fold lower than that of the wild-type enzyme, the ratio of turnover number to Km-value for D-Asn is 9.4fold lower than that of the wild-type enzyme, the ratio of turnover number to Km-value for D-Gln is 3.2fold higher than that of the wild-type enzyme, the ratio of turnover number to Km-value for D-Met is 56fold lower than that of the wild-type enzyme
M213R
mutant shows lower activity on neutral and basic amino acids compared to the wild type enzyme
Q144R
site-directed mutagenesis, the mutant shows reduced activity comapared to the wild-type enzyme
Q339E
mutant shows lower activity on neutral and basic amino acids compared to the wild type enzyme
S19G/S120P/Q144R/K321M/A345V
library screening and identification of a naturally occuring DAAO mutant with increased activity at low O2 and D-Ala concentrations and a 10fold lower Km for O2
S19G/S120P/Q144R/K321M/A345V
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the mutant possesses a 10fold lower KM,O2, thus resulting in dramatically increased activity at low O2 concentrations
S335G
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mutant enzyme has a lower turnover number with D-Ala than wild-type enzyme. The spectral and ligand binding properties of the mutant are similar to those of the wild-type enzyme
S335G
mutant shows lower activity on neutral and basic amino acids compared to the wild type enzyme
Y223S
mutant shows lower activity on neutral and basic amino acids compared to the wild type enzyme
Y238F
3fold slower turnover on D-Ala as substrate than wild-type enzyme. KM-value for D-Ala is 2fold lower than the wild-type value, Km-value for D-Ser is 4.7fold lower than the wild-type value, Km-value for D-Pro is 1.7fold lower than the wild-type value, Km-value for D-Trp is 1.5fold lower than the wild-type value, Km-value for cephalosporin is 2.6fold lower than the wild-type value, Km-value for D-Val is 3fold lower than the wild-type value, Km-value for D-Phe is 4.3fold lower than the wild-type value
Y238F
mutant shows lower activity on neutral and basic amino acids compared to the wild type enzyme
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
Y238R
mutant shows lower activity on neutral and basic amino acids compared to the wild type enzyme
Y238S
3fold slower turnover on D-Ala as substrate than wild-type enzyme. KM-value for D-Ala is 2fold lower than the wild-type value, Km-value for D-Ser is 8fold lower than the wild-type value, Km-value for D-Pro is 1.6fold lower than the wild-type value, Km-value for D-Trp is identical to wild-type value, Km-value for cephalosporin is 2.6fold lower than the wild-type value, Km-value for D-Val is 3.2fold lower than the wild-type value, Km-value for D-Phe is 7.5fold lower than the wild-type value
Y238S
mutant shows lower activity on neutral and basic amino acids compared to the wild type enzyme
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
E220D/Y224G
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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
E220D/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
Y228F
50% activity compared to the wild type enzyme, 120fold decreased reduction rate
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
DAO variants including V5A, D46N, F90V, P103L, R115W, P119L, L215F, P268S, R283Q, R286C, L329F and G331E significantly reduce fluctuations around the active site loop residues and close to the hydrophobic stretch region of residues 47-51. In molecular dynamics simulations, V5A, D46N, F90V, P103L, R115W, P119L, L215F, P268S, R283Q, R286C, L329F and G331E variants exhibit nearly similar radius of gyration, the H78Y, R279Q and S340F variants including the wild-type exhibit a slightly increased profile. Variants V5A, D46N, F90V, P103L, R115W, P119L, L215F, P268S, R283Q, R286C, L329F and G331E experience more compact structure than wild-type and H78Y, R279Q and S340F during the course of simulations
additional information
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DAO variants including V5A, D46N, F90V, P103L, R115W, P119L, L215F, P268S, R283Q, R286C, L329F and G331E significantly reduce fluctuations around the active site loop residues and close to the hydrophobic stretch region of residues 47-51. In molecular dynamics simulations, V5A, D46N, F90V, P103L, R115W, P119L, L215F, P268S, R283Q, R286C, L329F and G331E variants exhibit nearly similar radius of gyration, the H78Y, R279Q and S340F variants including the wild-type exhibit a slightly increased profile. Variants V5A, D46N, F90V, P103L, R115W, P119L, L215F, P268S, R283Q, R286C, L329F and G331E experience more compact structure than wild-type and H78Y, R279Q and S340F during the course of simulations
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
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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
comparison of D-Ser and D-Ala contents in different tissues in wild-type DAO+/+ mice with knockout mice DAO-/- and heterozygous DAO+/- mice, detailed overview
additional information
long-term increases in the brain levels of the endogenous N-methyl-D-aspartate receptor, NMDAR, glycine site agonist D-serine, through the genetic inactivation of its catabolic enzyme D-amino acid oxidase in mice
additional information
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construction of a mutant rat strain LEA/SENDAI lacking D-amino-acid oxidase
additional information
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development of an implantable D-serine biosensor for in vivo monitoring using mammalian D-amino acid oxidase on a poly (o-phenylenediamine) and Nafion-modified platinum-iridium disk electrode, method evaluation, overview
additional information
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DELTAloop mutant in which 14 residues belonging to a loop connecting strands betaF5-beta-F6 have been deleted is monomeric and thermodynamically less stable than dimeric wild-type DAAO, with melting temperatures of 48°C and 54°C, respectively
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
additional information
immobilization of the enzyme onto magnetic nanoparticles stabilizes the enzyme
additional information
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immobilization of the enzyme onto magnetic nanoparticles stabilizes the enzyme
additional information
establishing the transformed Pichia pastoris, expressing RgDAO, as whole-cell catalyst
additional information
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establishing the transformed Pichia pastoris, expressing RgDAO, as whole-cell catalyst
additional information
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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
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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
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
oxidation of Cys108 into cysteine sulfinic acid causes a global conformational response that affects the protein environment of the FAD cofactor. In comparison with the native enzyme, the mutation results in a fourfold-decreased specific activity, reflecting a catalytic efficiency for reduction of dioxygen lowered by about the same factor, and a markedly decreased propensity to aggregate under conditions of thermal denaturation
additional information
oxidation of Cys108 into cysteine sulfinic acid causes a global conformational response that affects the protein environment of the FAD cofactor. In comparison with the native enzyme, the mutation results in a fourfold-decreased specific activity, reflecting a catalytic efficiency for reduction of dioxygen lowered by about the same factor, and a markedly decreased propensity to aggregate under conditions of thermal denaturation
additional information
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oxidation of Cys108 into cysteine sulfinic acid causes a global conformational response that affects the protein environment of the FAD cofactor. In comparison with the native enzyme, the mutation results in a fourfold-decreased specific activity, reflecting a catalytic efficiency for reduction of dioxygen lowered by about the same factor, and a markedly decreased propensity to aggregate under conditions of thermal denaturation
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
additional information
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immobilization of the recombinant enzyme on solid beads through affinity of its N-terminal Strep-tag to Strep-Tactin coated on insoluble particles, covalent attachment, re-usable in multiple cycles of substrate conversion, the surfactant Pluronic F-68 stabilizes DAO by protecting the enzyme from the deleterious effect of gas-liquid interfaces
additional information
development of a robust and highly active Pichia pastoris TvDAO whole-cell biocatalyst in a multistep engineering process for use in cephalosporin C conversion on industrial scale, overview. Usage of a fed-batch cultivation of the multicopy strain
additional information
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development of a robust and highly active Pichia pastoris TvDAO whole-cell biocatalyst in a multistep engineering process for use in cephalosporin C conversion on industrial scale, overview. Usage of a fed-batch cultivation of the multicopy strain
