. 2022 Aug 15;2(5):521–528. doi: 10.1021/acsbiomedchemau.2c00032

Table 2. Steady-State Kinetic Parameters Derived for MpPCO and KnPCO Activity toward O₂^a.

enzyme/substrate	k_cat, s^–1	K_M, %_sat (μM)	V_max, μmol min^–1 mg^–1
MpPCO/AtRAP2_2–15	15.5 ± 0.7	3.2 ± 0.6 (39 ± 7)	31.3 ± 1.4
MpPCO_c/ MpERF_2–15	18.2 ± 0.9	8.7 ± 1.7 (106 ± 21)	39.1 ± 2.0
KnPCO/AtRAP2_2–15	59.3 ± 3.7	28.9 ± 4.1 (351 ± 50)	120.2 ± 7.6
KnPCO/MpERF_2–15	112.2 ± 6.8	26.3 ± 3.8 (319 ± 46)	227.5 ± 13.8

Experiments were conducted in the presence of nonlimiting AtRAP2_2-15 and MpERF-like_2-15.

Table 2. Steady-State Kinetic Parameters Derived for MpPCO and KnPCO Activity toward O2a.