EC Number   |
|---|
    1.4.3.3 | - |
| 1.4.3.3 | 3D structure of the enzyme in complex with the competitive inhibitor anthranilate is solved at 1.9 A resolution |
| 1.4.3.3 | crystallization of a single point mutant, X-ray diffraction structure determination and analysis at 1.8 A resolution |
| 1.4.3.3 | enzyme with bound inhibitor 3-hydroxyquinolin-2(1H)-one, X-ray diffraction structure determination and analysis |
| 1.4.3.3 | 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 |
| 1.4.3.3 | 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 |
| 1.4.3.3 | hanging-drop vapor diffusion method, crystal structure of the enzyme in complex with the competitive inhibitor benzoate at a resolution of 2.5 A |
| 1.4.3.3 | in complex with benzoate |
| 1.4.3.3 | in complex with D-serine or 3,4-dihydroxy-D-phenylalanine, hanging drop vapour diffusion method |
| 1.4.3.3 | molecular modeling of active site loop of wild-type and amyotrophic lateral sclerosis?associated DAO mutants such as R199W, R38H, R199Q, and Q201R |
