TABLE 1.

Kinetic parameters of the Synechocystis 6803 aconitase.

	−DTT		+DTT
	Control	AcnSP	Control	AcnSP
Vmax (μmol mg–1 min–1)	2.10 ± 0.08	1.91 ± 0.25*	9.04 ± 0.13	8.34 ± 0.20*
Km (mM)	0.051 ± 0.002	0.047 ± 0.005*	0.371 ± 0.020	0.268 ± 0.007*
Kcat (s–1)	3.46	3.15	14.92	13.76

The aconitase activity was measured in the presence of different cis-aconitate concentrations. It showed Michaelis-Menten kinetics (see Supplementary Figure S5), which permitted to calculate the kinetic parameters V_max, K_m, and K_cat of aconitase under reducing (+10 mM DTT) or oxidizing (−DTT) conditions using a Lineweaver-Burk plot (see Supplementary Figure S6). Approximately 2 nmol recombinant Synechocystis 6803 aconitase was used per enzyme assay in the absence (control) or presence (AcnSP) of 2 nmol of the synthetic AcnSP peptide. The asterisks mark statistically significant differences between the WT and mutant (Student’s t-test, P-value < 0.05).