Table 1.
Km | kcat-appa | IC50 | Inhibition | α | KD | |
---|---|---|---|---|---|---|
nm | nm | % | nm | |||
MMP9-MYC-His6 | ≤0.043b | |||||
MMP9-pro-cat | ≤0.008b | |||||
MMP9-MYC-His6 APMA | 9.6 ± 0.1 | 55.3 ± 1.0 | 0.26 ± 0.02 | 56 ± 2 | 1.2 ± 0.0 | 2.0 ± 0.3 |
MMP9-pro-catAPMA | 880 ± 160 | 3.1 ± 0.3 | 0.32 ± 0.01 | 88 ± 8 | NDc | 6.6 ± 1.3 |
MMP9-cat | 710 ± 70 | 5.3 ± 0.1 | 1.3 ± 0.1 | 73 ± 0 | 1.1 ± 0.2 | 3.3 ± 0.6 |
akcat-app (relative fluorescence units × min−1 × nm−1) is defined as Vmax/[Etot].
bDissociation rates were below the limit of detection and could only be estimated at ≤10−5 s−1.
cα value for competitive inhibition could not be determined due to the low activity of MMP9-pro-catAPMA.