EC Number   |
Reference |
|---|
   4.4.1.3 | in complex with Fe(III) and substrate dimethylsulfoniopropionate, to 2.0-2.5 A resolution. The enzyme undergoes conformational changes upon substrate-binding. The substrate is positioned optimally to bind iron and is in the proximity of Tyr120 that acts as a Lewis base to initiate catalysis |
747110 |
| 4.4.1.3 | to 1.5 A resolution. DddY contains a cap domain and a catalytic domain with a Zn2+ bound at its active site. Residues His265, Glu269, His338 and the acetate molecule participate in coordinating Zn2+. The DddY catalytic domain adopts a typical beta-barrel fold and contains two conserved cupin motifs. In the catalytic mechanism, residue Tyr271 acts as a general base to attack DMSP |
748399 |
| 4.4.1.3 | wild-type in complex with inhibitor 2-(N-morpholino)ethanesulfonic acid or PO43-, to 2.1 A resolution, and mutants Y366A and D377N bound to acrylate |
748685 |
