EC Number   |
|---|
    1.1.1.195 | - |
| 1.1.1.195 | 10 mg/ml purified recombinant enzyme, hanging drop vapour diffusion method, 0.001 ml of both protein and reservoir solution, the latter containing 1. 1.6 M ammonium sulfate, 0.1 M HEPES, pH 7.0, or 2.30% w/v PEG 4000, 0.1 M Tris-HCl, pH 8.5, room temperature, about 1 week, trigonal or monoclinic crystals, X-ray diffraction structure determination and analysis at 3.1 A resolution |
| 1.1.1.195 | homology modeling based on structure of Arabidopsis thaliana isoform CAD5. The model reveals a trilobed structure. The two major lobes contribute to constitution of NADP+ binding, catalytic Zn2+ binding and substrate binding domains. The substrate binding pocket is protected by these two major lobes and is in close proximity of catalytic Zn2+ and NADP+ binding domains |
| 1.1.1.195 | in complex with NADP(H), to 2.18 A resolution. NADP(H) is bound through hydrophobic interactions within the well-conserved GXGGXG motif from residues Gly184 to Gly189 and the adenine ring is the syn-conformation and is sandwiched between the guanidino group of Arg208 and Thr244 side chains. The aromatic side chains of residues Phe114 and Tyr116 in the active site could bind aromatic aldehydes by stacking the aromatic head of the substrates |
| 1.1.1.195 | isoform CAD4, hanging drop vapor diffusion method, using 2% (v/v) tacsimate, pH 7.0, 5% (v/v) 2-propanol, 0.1 M imidazole, pH 7.0, and 8% (w/v) polyethylene glycol 3350 |
| 1.1.1.195 | purified recombinant isozyme CAD5, 4-10 mg/ml apo-protein in 20 mM Tris-HCl, pH 8.0, 1 mM EDTA, and 1 mM DTT, hanging drop vapour diffusion method, at 4°C or at 20°C, 2fold dilution with reservoir solution containing 20% w/v PEG 3350, and 0.2 M trilithium citrate tetrahydrate, pH 8.1 3 days, X-ray diffraction structure determination an analysis at 2.0-2.6 A resolution |
