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Human lysozymes were shown to be metal-dependent peptidase enzymes (C, S and A subtypes) having remarkable structural stability at low pH. Tripeptide aldehydes, amino acyl compounds with an α,β-unsaturated aldehyde, were synthesized as potent and selective inhibitors of these enzymes. The crystal structures of three complexes of the A subtype with the tripeptide aldehydes were determined at 1.7-2.5 A resolution. In all cases the tripeptide aldehydes occupied the space between the S1 and S4 subsites of the protease. The aromatic and α,β-unsaturated aldehyde moieties were buried in the active site cleft, and the aliphatic tail protr
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