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The phosphinic acid functionality has emerged as an invaluable scaffold for the construction of biologically active compounds, in particular enzyme inhibitors. This article presents two examples of recent achievements in the preparation and application of phosphinic acids as ligands for hydrolases. Synthetic approaches to a dipeptide analog inhibitor of metalloaminopeptidases and a catechol-based inhibitor of urease are shown. The activity and mode of binding of phosphinic compounds to enzymes are further discussed.

Phosphinic acid-based enzyme inhibitors