EC Number   |
|---|
    1.14.15.35 | modeling of the substrate-binding pocket with ketoconazole bound shos that the secondary nitrogen of the azole ring is coordinated to the heme iron, and nearby regions are positioned in the active site similarly to 6-deoxyerythronolide B, the remainder of the molecule extends into the active site pocket, which is occupied by water in the 6-deoxyerythronolide B complex. The large water-binding pocket in the P450eryF active site appears to provide flexibility in substrate binding and allows for molecules that are larger than 6-deoxyerythronolide B to be accommodated in the active site |
| 1.14.15.35 | molecular dynamics and hybrid quantum mechanics/molecular mechanics analysis. Two water networks exist around the active site, the one found in the crystal structure involving E360 and an alternative one involving E244. The first proton transfer that converts the peroxo to the hydroperoxo intermediate proceeds via the E244 water network with direct involvement of the 5-OH group of the substrate. For the second proton transfer, the computed barriers for the rate-limiting homolytic O-O cleavage are similar for the E360 and E244 pathways, and hence both glutamate residues may serve as proton source in this step |
| 1.14.15.35 | NMR studies on lgad binding. Binding of 9-aminophenanthrene and testosterone occurs with apparent negative homotropic cooperativity for testosterone and positive homotropic cooperativity for 9-aminophenanthrene with Hill-equation-derived dissociation constants of 4 and 200 microM, respectively. Binding occurs on intermediate and fast chemical exhange time scales, respectively. The 15N-Phe NMR resonances most affected are the same in each titration, suggesting that the two ligands contact the same phenylalanines within the active site of P450eryF |
| 1.14.15.35 | sitting drop vapor diffusion crystallization, crystal structures of the ferrous dioxygen complex of wild-type enzyme and its mutants, A245S and A245T |
| 1.14.15.35 | to 2.2 A resolution. The substrate is positioned with the macrolide ring perpendicular to the heme plane and contacts seven hydrophobic residues and three solvent molecules. The substrate participates in a network of hydrogen bonds that may provide a proton shuttle pathway in the oxygen cleavage reaction |
