EC Number   |
|---|
   1.5.3.5 | - |
| 1.5.3.5 | forms hexagonal crystals in ammonium sulfate solution |
| 1.5.3.5 | hanging-drop vapor diffusion method, X-ray crystal structures of the N462V and N462Y/W427Y variants complexed with (S)-nicotine (at 2.7 and 2.3 A resolution, respectively) reveal no significant active-site rearrangements |
| 1.5.3.5 | His-tagged and untagged free enzyme and complex of dithionite-reduced 6HLNO with the natural substrate 6-hydroxy-L-nicotine X-ray diffraction structure determination and analysis at 1.95 A and 2.05 A resolution, respectively, combined isomorphous/multiple-wavelength anomalous dispersion phasing |
| 1.5.3.5 | to 1.95 A resolution. A diacylglycerophospholipid molecule is non-covalently bound to each protomer of 6HLNO. The fatty acid chains occupy hydrophobic channels that penetrate deep into the interior of the substrate-binding domain of each subunit. The solvent-exposed glycerophosphate moiety is located at the subunit-subunit interface. In the crystal structure of a complex of dithionite-reduced 6HLNO with the natural substrate 6-hydroxy-L-nicotine at 2.05 A resolution, the location of the substrate in a tight cavity suggests that the binding geometry of this unproductive complex may be closely similar as under oxidizing conditions. A comparison of the substrate-binding modes of 6HLNO and 6-hydroxy-D-nicotine oxidase, EC 1.5.3.6, based on models of complexes with the D-substrate, suggests that the two enzymes orient the enantiomeric substrates in mirror symmetry with respect to the plane of the flavin |
