Table I.
Kinetic comparisons of peptidyl nitroanilide hydrolysis by chymotryptic peptidases
AAPF-4NA | AEPF-4NA | RETF-4NA | VPF-4NA | ||
---|---|---|---|---|---|
Chymase | kcata | 9.3 ± 0.8 | 8.8 ± 0.2 | 19.7 ± 0.1 | 17.2 ± 0.4 |
Kma | 0.31 ± 0.07 | 0.15 ± 0.01 | 0.64 ± 0.05 | 0.29 ± 0.04 | |
kcat/Kma | 30 | 59 | 31 | 59 | |
+ α2M | kcat | 49 ± 2 | 51 ± 1 | 87 ± 1 | 8.9 ± 0.6 |
Km | 0.28 ± 0.02 | 0.08 ± 0.08 | 0.32 ± 0.01 | 0.16 ± 0.03 | |
kcat/Km | 170 | 640 | 270 | 55 | |
Cathepsin G | kcat | 1.4 ± 0.1 | 3.7 ± 0.8 | 7.3 ± 11.9 | 13.8 ± 0.4 |
Km | 0.97 ± 0.06 | 0.93 ± 0.08 | 13 ± 36 | 0.69 ± 0.07 | |
kcat/Km | 1.4 | 3.9 | 0.56 | 20 | |
+ α2M | kcat | 0 ± 0 | 0.71 ± 0.26 | 0 ± 0 | 2.4 ± 2.1 |
Km | - | 0.12 ± 0.15 | - | 0.8 ± 1.4 | |
kcat/Km | - | 5.9 | - | 3.0 | |
Chymotrypsin | kcat | 68 ± 8 | 12.8 ± 0.5 | 5.0 ± 0.4 | 11.8 ± 0.4 |
Km | 0.52 ± 0.14 | 0.39 ± 0.04 | 1.1 ± 0.2 | 0.07 ± 0.01 | |
kcat/Km | 130 | 33 | 4.5 | 170 | |
+ α2M | kcat | 48 ± 1 | 31 ± 1 | 3.9 ± 0.4 | 22 ± 1 |
Km | 0.035 ± 0.003 | 0.17 ± 0.02 | 0.057 ± 0.026 | 0.037 ± 0.007 | |
kcat/Km | 1400 | 180 | 68 | 59 |
Units of turnover number kcat, Michaelis constant Km and specificity constant kcat/Km are s−1, mM, and s−1 mM−1, respectively