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
-
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
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
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Purification
Purification on EC 1.4.3.3 - D-amino-acid oxidase
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ammonium sulfate precipitation, Toyopearl butyl column chromatography, and Q Sepharose column chromatography
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enzyme intracellularly expressed under P(GAP) integrant in Pichia pastoris
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His-Bind column chromatography
Hitrap chelating chromatography
Mono Q HR 10/10 column chromatography and Sephacryl S-200 gel filtration
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partial
Q-Sepharose column chromatography and hydroxyapatite column chromatography
recombinant DAAO from Spodoptera frugiperda Sf9 cells
recombinant DAo from Pichia pastoris strain CBS 7435, the yeast cells are permeabilized by freeze-drying and incubation in 10% v/v 2-propanol resulting in a highly active, 1.6 kUnits/g dry matter, and stable oxidase preparation
recombinant enzyme by ammonium sulfate fractionation, anion exchange chromatography, and dialysis
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recombinant enzyme fused to the maltose-binding protein from Escherichia coli strain TB1 by maltose affinity chromatography
recombinant N-terminally Strep-tagged enzyme to homogeneity from Escherichia coli strain BL21(DE3) by affinity chromatography
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recombinant Strep-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by ultracentrifugation, affinity and anion exchange chromatography
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recombinant wild-type enzyme and mutants from Escherichia coli BL21(DE3)
Talon metal affinity column chromatography, and Superdex 200 gel filtration
use of surface layer (S-layer) protein of Lactobacillus brevis as a self-aggregating protein tag to enable cost-effective separation of human and yeast D-amino acid oxidases expressed in Escherichia coli cells. Human and yeast D-amino acid oxidases fused with S-layer proteins can be easily separated by aggregates at the interface and/or in a few conditions by precipitates to the bottom of the PEG-phosphate aqueous system
use of surface layer (S-layer) protein of Lactobacillus brevis as a self-aggregating protein tag to enable cost-effective separation of human and yeast D-amino acid oxidases expressed in Escherichia coli cells. Human and yeast D-amino acid oxidases fused with S-layer proteins can be easily separated by aggregates at the interface and/or in a few conditions by precipitates to the bottom of the PEG-phosphate aqueous system
use of surface layer (S-layer) protein of Lactobacillus brevis as a self-aggregating protein tag to enable cost-effective separation of human and yeast D-amino acid oxidases expressed in Escherichia coli cells. Human and yeast D-amino acid oxidases fused with S-layer proteins can be easily separated by aggregates at the interface and/or in a few conditions by precipitates to the bottom of the PEG-phosphate aqueous system