AbstractA comparative study of theBacillus subtilisneutral protease and Bacillus thermoproteolyticus thermolysin calalyzed hydrolysis of a few dipeptide sustrates including furylacryloylglycyl‐L‐leucine amide is reported. While differences in thekcat/Kmwere observed between the two enzymes toward substrates in which phenylalanine or leucine donated the amino group of the peptide bond, secondary effects of substituents on the carbonyl donating amino acid and pH profiles were quite similar. Differences were also observed toward protein substrates as compared to dipepti