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. 2014 Oct;196(19):3410–3420. doi: 10.1128/JB.01851-14

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FIG 5 — Kinetic characterization of CysK2, CysK2_R243A mutant, and CysK2_NT. (A) First half-reaction parameters investigated by stopped-flow spectrophotometry. Pseudo-first-order rate constants (k_obs) at different OPS concentrations. The linear fit used to derive the second-order rate constant (k_max/K_s) is shown in the inset. (B) Comparison of k_obs at 5 mM OPS between wild-type CysK2 (wt), CysK2_R243A (R243A), and CysK2_NT (NT) constructs. (C) Michaelis-Menten kinetics of CysK2 based on phosphate release using the malachite green calorimetric assay. (D) Relative activity of wild-type CysK2 compared to CysK2_R243A based on inorganic phosphate release. (E) Michaelis-Menten kinetics of CysK2 in the presence of sulfide as a sulfur donor substrate. The inset shows the dependence of l-cysteine production on enzyme concentration. (F) Michaelis-Menten kinetics of CysK2 in the presence of thiosulfate as an S donor substrate.