Pressure dependence of thermolysin catalysis

摘要: A comparison of the pressure and temperature dependences catalytic reaction thermolysin, a thermostable neutral protease from Bacillus thermoproteolyticus, with those non-thermostable subtilis revealed distinct difference in Km values these enzymes for 3-(2-furyl)acryloyl-blocked dipeptide tripeptide substrates, but not kcat. Namely, volume changes binding process (ΔV) substrates several competitive inhibitors were –20––30 ml/mol thermolysin nearly 0 protease. The enthalpy entropy negative positive latter enzyme. activation volumes (ΔV≠) kcat 25–35 both proteases, showed no significant between two enzymes. characteristic seen is discussed relation to thermostability proteases.