Fig. 2: Biochemical characterization of the 1,3-PD defence gene and its functional activity within a bacterial host.
From: Plasmid-encoded toxin defence mediates mutualistic microbial interactions
a, Enzymatic activity of the 1,3-PD enzyme over time, using 1,3-propanediol as a substrate. b,c, Michaelis–Menten analysis of 1,3-PD activity at increasing concentrations of either NAD+ (b) or 1,3-propanediol (c). The measurements were carried out in technical triplicates, for which actual data are presented. The solid curves were generated by fitting the Michaelis–Menten equation to the data, assuming non-cooperative binding of NAD+ and 1,3-propanediol by the enzyme. d, Protective effect against reuterin of 1,3-PD expression in E. coli. ER2566 strains constitutively expressing 1,3-PD from plasmid pBR322 were grown in increasing concentrations of reuterin (0 to 1 mM final concentration) in 200 μl of LB medium (volumes of cultures were homogenized across samples using sterile water). Following 24 h at 37 °C, turbidity was measured at 600 nm. Control strains carried an empty vector. The measurements were carried out in biological triplicates, for which actual data, averages and standard deviations are presented.
