Table 1.
Mus81-Mms4 kinetic parameters on DNA joint molecules
Substrate | Vmax (nM/min) | KM (nM) | kcat (min−1) | Catalytic cycle (min) | kcat/KMa (nM−1 min−1) |
---|---|---|---|---|---|
3′-FL | 4.9 ± 0.7 | 5.5 ± 2.6 | 0.97 | 1.03 | 0.19 |
RF-like | 6.7 ± 0.6 | 7.3 ± 2.0 | 1.35 | 0.74 | 0.19 |
nXO12 | 6.0 ± 1.7 | 3.1 ± 2.0 | 1.20 | 0.83 | 0.39 |
pXO12-3′ | 1.6 ± 0.2 | 5.6 ± 1.8 | 0.32 | 3.13 | 0.06 |
DL | 0.5 ± 0.2 | 1.2 ± 1.6 | 0.09 | 10.75 | 0.08 |
Y | 1.3 ± 0.04 | 30.4 ± 11.3 | 0.26 | 3.85 | 0.009 |
XO12 | −b | ||||
X12 | −b |
akcat/KM traditionally defines a ‘selectivity coefficient’ that can be used to rank substrates for their relative ‘selectability’ by an enzyme. In this case, nXO12 > 3′-FL′ ∼ RF-like > DL > pXO12-3′ > Y.
bThe catalytic parameters could not be determined because of the negligible activity on these substrates.