EC Number   |
Reference |
|---|
   1.2.3.3 | by the hanging-drop vapour-diffusion method. POX complexed with FAD, with FAD and thiamine diphosphate, and with FAD and the 2-acetyl-thiamine diphosphate intermediate at 1.6, 1.8 and 1.9 A resolution, respectively. Each subunit of the homotetrameric POX enzyme consists of three domains. FAD is bound within one subunit in the elongated conformation and with the flavin moiety being planar in the oxidized form, while thiamine diphosphate is bound in a conserved V-conformation at the subunit-subunit interface. The structures reveal flexible regions in the active-site tunnel which may undergo conformational changes to allow the entrance of the substrates and the exit of the reaction products. Lys478, the side chain of which may be bent or extended depending on the stage of catalysis |
684189 |
| 1.2.3.3 | in complex with the thiamin diphosphate carbanion-enamine and two-electron reduced FAD, hanging drop vapor diffusion method |
726382 |
| 1.2.3.3 | mutant V265A |
654686 |
| 1.2.3.3 | the full-length form and a proteolytically activated C-terminal truncation variant which lacks the last 23 amino acids, by the hanging-drop vapour-diffusion method using either protamine sulfate (fulllength POX) or 2-methyl-2,4-pentanediol (DELTA23 POX) as precipitants. To 2.9 A resolution. Fulllength POX crystallizes in the tetragonal space group P43212 with two monomers per asymmetric unit, the crystals of DELTA23 POX belong to the orthorhombic space group P212121 and contain 12 monomers per asymmetric unit |
684193 |
| 1.2.3.3 | triple mutant at 2.1 A resolution |
114312 |
| 1.2.3.3 | V265A mutant |
672023 |
| 1.2.3.3 | wild-type at 2.5 A resolution, triple mutant at 2.1 A resolution, hanging drop vapour diffusion technique |
390433 |
