parametersSTAP, SG-XIV, and KERAB proteases exhibited the classical kinet-ics of Michaelis-Menten for the two substrates used. The order ofthe catalytic efficiency (kcat/Km) values of each enzyme was almostthe same, i.e., Suc-(Ala)2-Pro-Met-pNA > BTEE (Table 5). When Suc-(Ala)2-Pro-Met-pNA was used as a synthetic substrate, STAP wasalso noted to exhibit kcat/Kmvalues that were 2.39 times and 5.12times higher than those SG-XIV and KERAB, respectively. WhenBTEE was used as an ester substrate, the kcat/Kmvalues exhibitedby STAP were 2.66 and 4.59 times higher than those of SG-XIV andKERAB, respectively