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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

Reaction

a D-amino acid
+
H2O
 +
O2
=
a 2-oxo carboxylate
 +
NH3
 +
H2O2

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 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.3 With oxygen as acceptor
                1.4.3.3 D-amino-acid oxidase

Crystallization

Crystallization on EC 1.4.3.3 - D-amino-acid oxidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme with bound inhibitor 3-hydroxyquinolin-2(1H)-one, X-ray diffraction structure determination and analysis
fluorescence lifetimes are 47 ps in the dimer, 235 ps in the monomer. The fluorescence lifetimes of the hDAAO did not change upon the inhibitor bindings. Three fastest electron transfer donors are Tyr314, Trp52 and Tyr224 in the dimer, while Tyr314, Tyr224 and Tyr55 in the monomer
hanging-drop vapor diffusion method, crystal structure of the enzyme in complex with the competitive inhibitor benzoate at a resolution of 2.5 A
-
in complex with benzoate
in complex with D-serine or 3,4-dihydroxy-D-phenylalanine, hanging drop vapour diffusion method
-
molecular modeling of active site loop of wild-type and amyotrophic lateral sclerosis?associated DAO mutants such as R199W, R38H, R199Q, and Q201R
search for binding pockets of DAO to its inhibitor 4-bromo-3-nitrobenzoate by combining in silico docking simulation and labeling experiments employing an N-sulfanylethylanilide-based labeling technology. There are two binding pockets: one is shared with D-Ser and FAD, and the other is an cleft between the subunits of a DAO dimer
sitting drop vapor diffusion method, using 10-15% (w/v) PEG 4000, 0.1 M sodium citrate, pH 8.0, 0.2 M ammonium dihydrogen phosphate, and 10% (v/v) glycerol
-
structure of mutant P219L in complex with FAD and benzoate at 2.25 A resolution displays conformational changes of the active site and lid. The distances between the H-bond-forming atoms of arginine 283 and benzoate and the relative position between the aromatic rings of tyrosine 224 and benzoate are changed in the P219L complex
structures of DAO in complex with thiophene carboxylic acid inhibitors. Residue Tyr224 is tightly stacked with the thiophene ring of the inhibitors, resulting in the disappearance of the secondary pocket observed with other DAO inhibitors. Tyr224 prefers the stacked conformation irrespective of whether Tyr224 is stacked or not in the initial state of the simulations. The active site is tightly closed with an extensive network of hydrogen bonds including those from Tyr224 in the stacked conformation
substrate-free or in complex with imino-DOPA, hanging drop vapour diffusion method, at 20°C
enzyme with bound inhibitor 3-hydroxyquinolin-2(1H)-one, X-ray diffraction structure determination and analysis
-
3D structure of the enzyme in complex with the competitive inhibitor anthranilate is solved at 1.9 A resolution
-
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
crystallization of a single point mutant, X-ray diffraction structure determination and analysis at 1.8 A resolution