EC Number   |
|---|
   3.1.1.25 | hanging drop vapor diffusion method, in order to understand the structural consequences of variations at position 263, the crystal structures of the mutant enzymes (W263F, W263M, W263L, W263I, W263V, W263T) is solved |
| 3.1.1.25 | phosphate ion is bound to the catalytic calcium in the structure of crystallized recombinant G2E6 |
| 3.1.1.25 | protein at pH 6.5 and in complex with 2-hydroxyquinoline. The models suggest that promiscuity is driven by coincidental overlaps between the reactive intermediate for the native lactonase reaction and the ground and/or intermediate states of the promiscuous reactions. This overlap is also enabled by different active-site conformations: the lactonase activity utilizes one active-site conformation whereas the promiscuous phosphotriesterase activity utilizes another |
| 3.1.1.25 | sitting drop vapor diffusion method at 20°C, X-ray structures of the enzyme bound to a fatty acid and to its substrate acyl-homoserine lactone |
| 3.1.1.25 | to 2.4 A resolution, space group P64, with unit-cell parameters a=b=174.06, c = 61.32 A. The asymmetric unit contains one homodimer |
