Table 1 Kinetic properties of the purified L-asparaginases used in this study.
From: Discovery of human-like L-asparaginases with potential clinical use by directed evolution
Enzyme name | # of residues | % identity to hASNase1 | % similarity to hASNase1 | kcat (sec−1) | KM (µM) | kcat/KM (sec−1µM−1) | kobs (sec−1) @50 µM |
|---|---|---|---|---|---|---|---|
hASNase1* | 573 | 100 | 100 | 17 ± 0.8 | 3,500 ± 300 | 0.005 | ND |
ansB | 326 | 26.9 | 58.5 | 48 ± 1 | 11 ± 1 | 4.4 | 41 ± 0.3 |
gpASNase1 | 565 | 69.8 | 88.6 | 41 ± 2 | 50 ± 7 | 0.8 | 20 ± 1 |
gN-hC | 571 | 83.4 | 94.9 | 24 ± 1 | 35 ± 4 | 0.7 | 14 ± 1 |
hN-gC | 567 | 86.5 | 93.7 | 14 ± 0.5 | 3,800 ± 120 | 0.004 | ND |
63N-hC | 571 | 85.7 | 95.6 | 32 ± 0.6 | 47 ± 3 | 0.7 | 17 ± 0.5 |
64N -hC | 571 | 91.1 | 96.7 | 60 ± 2 | 202 ± 17 | 0.3 | 10 ± 1 |
65N -hC | 571 | 87.1 | 95.8 | 40 ± 1 | 74 ± 5 | 0.5 | 17 ± 1 |
SAN -hC | 571 | 91.6 | 97.4 | 32 ± 2 | 165 ± 19 | 0.2 | 6 ± 1 |
