Comparative kinetic studies on the neutral protease and thermolysin catalyzed hydrolysis of simple dipeptide substrates

Abstract A comparative study of the Bacillus subtilis neutral protease and Bacillus thermoproteolyticus thermolysin calalyzed hydrolysis of a few dipeptide sustrates including furylacryloylglycyl‐L‐leucine amide is reported. While differences in the kcat/Km were 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 dipeptides.