Peptide deformylase (PDF) is an important enzyme in the post-translational processing of bacterial proteins. When synthesised, bacterial proteins have a formyl group on their N-terminus methionine (fMet). PDF cleaves off the formyl group, giving a functional protein.
As this process is unique to bacteria, PDF makes an ideal target for an antimicrobial. By preventing the PDF enzyme from binding to the ribosome, such as through using an allosteric modulator, the deformylating activity could be suppressed.
PDF has three coordination sites for a metal ion, so a substrate mimic altering the coordination of the metal 2+ ion could reduce the catalytic activity of the enzyme, by preventing the correct positioning of the H2O molecule within the active site.