The active sites in PepA and in bovine lens LAP have been found to be similar. Shown in the picture below is the proposed model for the active site of LAP-A in tomato based on the work of Strater et al. It is also known that the biochemistry of the LAPs from these three kingdoms is very similar. PepA, bovine lens LAP, and LAP-A preferentially cleave N-terminal leucine, arginine, and methionine residues. These enzymes are all metallopeptidases requiring divalent metal cations for their enzymatic activity Enzymes are active in the presence of Mn, Mg and Zn. These enzymes are also known to have high pH (pH 8) and temperature optima. At pH 8, the highest enzymatic activity is seen at 60 °C. PepA, bovine lens LAP and LAP-A are also known to form hexamers in vivo. The Gu et al. from 1999 demonstrated that six 55kDA enzymatically inactive LAP-A protomers come together to form the 353kDa bioactive LAP-A hexamer. Structures of the bovine lens LAP protomer and the biologically active hexamer have been constructed can be found through Protein Data Bank (2J9A).