EC Number   |
|---|
    4.1.1.45 | - |
| 4.1.1.45 | EPR spectroscopic study on the Cu-substituted enzyme and crystal structure in the native catalytically active state at 1.99 A resolution, a substrate analogue-bound form at 2.50 A resolution, and a selected active site mutant form with one of the putative substrate binding residues altered at 2.32 A resolution. Each asymmetric unit contains three pairs of dimers. The substrate analogue does not directly coordinate to the metal ion but is bound to the active site by two arginine residues through noncovalent interactions |
| 4.1.1.45 | hanging drop vapour diffusion method with 0.1 M Tris (pH 8.75), 15% PEG 5000, and 0.2 M MgCl2, at 20°C |
| 4.1.1.45 | molecular docking of inhibitor 3-[[[5-cyano-1,6-dihydro-6-oxo-4-(2-thienyl)-2-pyrimidinyl]thio]methyl]phenylacetic acid. The 2-thiophene ring fits the hydrophobic cleft defined by the Trp191 and Met180 residues |
| 4.1.1.45 | mutant enzymes Co(II)-H228Y, Zn(II)-H228Y, and Zn(II)-H228G, hanging drop vapor diffusion method, using 0.1 M Tris-HCl (pH 8.75), 0.2 M MgCl2, and 15% (w/v) PEG 5000 |
| 4.1.1.45 | vapour diffusion technique in hanging drop, crystal structure of human alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase in complex with the glycolytic intermediate 1,3-dihydroxyacetonephosphate (DHAP), refined to an R-factor of 0.19, 1 mM DHAP, 2% poly(ethylene glycol) (PEG 400), 0.1 M Na/Hepes pH 7.5, 2.0 M ammonium sulphate, mixed with the same amount of a protein solution at a concentration of 12.7 mg/ml, and equilibrated against 500 microL of the reservoir solution, at 20°C |
